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Publications Départements Biologie Cellulaire


  • A. Agorio, J. Giraudat, M. W. Bianchi, J. Marion, C. Espagne, L. Castaings, F. Lelièvre, C. Curie, S. Thomine, et S. Merlot, « Phosphatidylinositol 3-phosphate–binding protein AtPH1 controls the localization of the metal transporter NRAMP1 in Arabidopsis », Proceedings of the National Academy of Sciences, p. 201702975, avr. 2017.
    Mots-clés : BIOCELL, DYNBSJ, late endosome, metal transport, MINION, NRAMP, phosphatidylinositol 3-phosphate, vacuole.

  • S. Ait-El-Mkadem, M. Dayem-Quere, M. Gusic, A. Chaussenot, S. Bannwarth, B. François, E. C. Genin, K. Fragaki, C. L. M. Volker-Touw, C. Vasnier, V. Serre, K. L. I. van Gassen, F. Lespinasse, S. Richter, G. Eisenhofer, C. Rouzier, F. Mochel, A. De Saint-Martin, M. - T. Abi Warde, M. G. M. de Sain-van der Velde, J. J. M. Jans, J. Amiel, Z. Avsec, C. Mertes, T. B. Haack, T. Strom, T. Meitinger, P. E. Bonnen, R. W. Taylor, J. Gagneur, P. M. van Hasselt, A. Rötig, A. Delahodde, H. Prokisch, S. A. Fuchs, et V. Paquis-Flucklinger, « Mutations in MDH2, Encoding a Krebs Cycle Enzyme, Cause Early-Onset Severe Encephalopathy », American Journal of Human Genetics, vol. 100, nᵒ 1, p. 151-159, 2017.

  • A. Arnal, C. Jacqueline, B. Ujvari, L. Leger, C. Moreno, D. Faugere, A. Tasiemski, C. Boidin-Wichlacz, D. Misse, F. Renaud, J. Montagne, A. Casali, B. Roche, F. Mery, et F. Thomas, « Cancer brings forward oviposition in the fly Drosophila melanogaster », Ecology and Evolution, vol. 7, nᵒ 1, p. 272-276, 2017.
    Résumé : Hosts often accelerate their reproductive effort in response to a parasitic infection, especially when their chances of future reproduction decrease with time from the onset of the infection. Because malignancies usually reduce survival, and hence potentially the fitness, it is expected that hosts with early cancer could have evolved to adjust their life-history traits to maximize their immediate reproductive effort. Despite the potential importance of these plastic responses, little attention has been devoted to explore how cancers influence animal reproduction. Here, we use an experimental setup, a colony of genetically modified flies Drosophila melanogaster which develop colorectal cancer in the anterior gut, to show the role of cancer in altering life-history traits. Specifically, we tested whether females adapt their reproductive strategy in response to harboring cancer. We found that flies with cancer reached the peak period of oviposition significantly earlier (i.e., 2 days) than healthy ones, while no difference in the length and extent of the fecundity peak was observed between the two groups of flies. Such compensatory responses to overcome the fitness-limiting effect of cancer could explain the persistence of inherited cancer-causing mutant alleles in the wild.
    Mots-clés : BIOCELL, cancer, fecundity, life‐history strategy, METABO, reproduction.

  • A. Aubusson-Fleury, G. Balavoine, M. Lemullois, K. Bouhouche, J. Beisson, et F. Koll, « Centrin diversity and basal body patterning across evolution: new insights from Paramecium », Biology Open, 2017.
    Résumé : First discovered in unicellular eukaryotes, centrins play crucial roles in basal body duplication and anchoring mechanisms. While the evolutionary status of the founding members of the family, Centrin2/Vfl2 and Centrin3/cdc31 has long been investigated, the evolutionary origin of other members of the family has received less attention. Using a phylogeny of ciliate centrins, we identify two other centrin families, the ciliary centrins and the centrins present in the contractile filaments (ICL centrins). In this paper, we carry on the functional analysis of still not well known centrins, the ICL1e subfamily identified in Paramecium, and show their requirement for correct basal body anchoring through interactions with Centrin2 and Centrin3. Using Paramecium as well as an Eukaryote-wide sampling of centrins from completely sequenced genomes, we revisited the evolutionary story of centrins. Their phylogeny shows that the centrins associated with the ciliate contractile filaments are widespread in eukaryotic lineages and could be as ancient as Centrin2 and Centrin3.
    Mots-clés : basal body anchoring, basal body assembly, BIOCELL, BIOCIL, centrin evolution, Ciliary centrins, ciliated epithelia polarity.

  • H. Bengueddach, M. Lemullois, A. Aubusson-Fleury, et F. Koll, « Basal body positioning and anchoring in the multiciliated cell Paramecium tetraurelia: roles of OFD1 and VFL3 », Cilia, vol. 6, nᵒ 1, 2017.

  • A. Bersweiler, B. D'Autréaux, H. Mazon, A. Kriznik, G. Belli, A. Delaunay-Moisan, M. B. Toledano, et S. Rahuel-Clermont, « A scaffold protein that chaperones a cysteine-sulfenic acid in H2O2 signaling », Nature Chemical Biology, 2017.
    Résumé : In Saccharomyces cerevisiae, Yap1 regulates an H2O2-inducible transcriptional response that controls cellular H2O2 homeostasis. H2O2 activates Yap1 by oxidation through the intermediary of the thiol peroxidase Orp1. Upon reacting with H2O2, Orp1 catalytic cysteine oxidizes to a sulfenic acid, which then engages into either an intermolecular disulfide with Yap1, leading to Yap1 activation, or an intramolecular disulfide that commits the enzyme into its peroxidatic cycle. How the first of these two competing reactions, which is kinetically unfavorable, occurs was previously unknown. We show that the Yap1-binding protein Ybp1 brings together Orp1 and Yap1 into a ternary complex that selectively activates condensation of the Orp1 sulfenylated cysteine with one of the six Yap1 cysteines while inhibiting Orp1 intramolecular disulfide formation. We propose that Ybp1 operates as a scaffold protein and as a sulfenic acid chaperone to provide specificity in the transfer of oxidizing equivalents by a reactive sulfenic acid species.
    Mots-clés : BIOCELL, SOC.

  • K. Bodvard, K. Peeters, F. Roger, N. Romanov, A. Igbaria, N. Welkenhuysen, G. Palais, W. Reiter, M. B. Toledano, M. Käll, et M. Molin, « Light-sensing via hydrogen peroxide and a peroxiredoxin », Nature Communications, vol. 8, p. 14791, mars 2017.

  • S. C. Brown, M. Bourge, N. Maunoury, M. Wong, M. W. Bianchi, S. Lepers-Andrzejewski, P. Besse, S. Siljak-Yakovlev, M. Dron, et B. Satiat-Jeunemaître, « DNA remodelling by Strict Partial Endoreplication in orchids, an original process in the plant kingdom », Genome Biology and Evolution, 2017.
    Résumé : DNA remodelling during endoreplication appears to be a strong developmental characteristic in orchids. In this study, we analysed DNA content and nuclei in 41 species of orchids to further map the genome evolution in this plant family. We demonstrate that the DNA remodelling observed in 36 out of 41 orchids studied corresponds to strict partial endoreplication. Such process is developmentally regulated in each wild species studied. Cytometry data analyses allowed us to propose a model where nuclear states 2C, 4E, 8E, etc. form a series comprising a fixed proportion, the euploid genome 2C, plus 2 to 32 additional copies of a complementary part of the genome. The fixed proportion ranged from 89% of the genome in Vanilla mexicana down to 19% in V. pompona, the lowest value for all 148 orchids reported. Insterspecific hybridisation did not suppress this phenomenon. Interestingly, this process was not observed in mass-produced epiphytes. Nucleolar volumes grow with the number of endocopies present, coherent with high transcription activity in endoreplicated nuclei. Our analyses suggest species-specific chromatin rearrangement. Towards understanding endoreplication, V. planifolia constitutes a tractable system for isolating the genomic sequences that confer an advantage via endoreplication from those that apparently suffice at diploid level.
    Mots-clés : BIOCELL, CYTO, cytogenetics, cytometry, DYNBSJ, endoreplication, genome imbalance, Genome Size, PF, Vanilla.

  • S. Chardonnet, T. Bessiron, C. I. Ramos, R. Dammak, M. - A. Richard, C. Boursier, C. Cadillac, F. M. Coquelle, S. Bossi, F. Ango, P. Le Maréchal, P. Decottignies, C. Berrier, H. McLean, et H. Daniel, « Native metabotropic glutamate receptor 4 depresses synaptic transmission through an unusual Gαq transduction pathway », Neuropharmacology, 2017.
    Résumé : In cerebellar cortex, mGlu4 receptors located on parallel fibers play an essential role in normal motor function, but the molecular mechanisms involved are not yet completely understood. Using a strategy combining biochemical and electrophysiological approaches in the rodent cerebellum, we demonstrate that presynaptic mGlu4 receptors control synaptic transmission through an atypical activation of Gαq proteins. First, the Gαq subunit, PLC and PKC signaling proteins present in cerebellar extracts are retained on affinity chromatography columns grafted with different sequences of the cytoplasmic domain of mGlu4 receptor. The i2 loop and the C terminal domain were used as baits, two domains that are known to play a pivotal role in coupling selectivity and efficacy. Second, in situ proximity ligation assays show that native mGlu4 receptors and Gαq subunits are in close physical proximity in cerebellar cortical slices. Finally, electrophysiological experiments demonstrate that the molecular mechanisms underlying mGlu4 receptor-mediated inhibition of transmitter release at cerebellar Parallel Fiber (PF) - Molecular Layer Interneuron (MLI) synapses involves the Gαq-PLC signaling pathway. Taken together, our results provide compelling evidence that, in the rodent cerebellar cortex, mGlu4 receptors act by coupling to the Gαq protein and PLC effector system to reduce glutamate synaptic transmission.
    Mots-clés : BIOCELL, Cerebellar cortex, DYNBSJ, G protein, Molecular layer interneurons, Presynaptic metabotropic glutamate receptor 4, Signaling pathway, Synaptic transmission.

  • C. Eisenach et A. De Angeli, « Ion Transport at the Vacuole During Stomatal Movements », Plant Physiology, p. pp.00130.2017, avr. 2017.

  • Y. Goulev, S. Morlot, A. Matifas, B. Huang, M. Molin, M. B. Toledano, et G. Charvin, « Nonlinear feedback drives homeostatic plasticity in H2O2 stress response », eLife, vol. 6, 2017.
    Résumé : Homeostatic systems that rely on genetic regulatory networks are intrinsically limited by the transcriptional response time, which may restrict a cell's ability to adapt to unanticipated environmental challenges. To bypass this limitation, cells have evolved mechanisms whereby exposure to mild stress increases their resistance to subsequent threats. However, the mechanisms responsible for such adaptive homeostasis remain largely unknown. Here, we used live-cell imaging and microfluidics to investigate the adaptive response of budding yeast to temporally controlled H2O2 stress patterns. We demonstrate that acquisition of tolerance is a systems-level property resulting from nonlinearity of H2O2 scavenging by peroxiredoxins and our study reveals that this regulatory scheme induces a striking hormetic effect of extracellular H2O2 stress on replicative longevity. Our study thus provides a novel quantitative framework bridging the molecular architecture of a cellular homeostatic system to the emergence of nonintuitive adaptive properties.
    Mots-clés : BIOCELL, cell biology, Computational Biology, S. cerevisiae, SOC, systems biology.

  • C. Jenzer et R. Legouis, « Les multiples facettes de l’autophagie au cours du développement », médecine/sciences, vol. 33, nᵒ 3, p. 238-245, 2017.

  • A. Johnson et G. Vert, « Single Event Resolution of Plant Plasma Membrane Protein Endocytosis by TIRF Microscopy », Frontiers in Plant Science, vol. 8, p. 612, 2017.
    Résumé : Endocytosis is a key process in the internalization of extracellular materials and plasma membrane proteins, such as receptors and transporters, thereby controlling many aspects of cell signaling and cellular homeostasis. Endocytosis in plants has an essential role not only for basic cellular functions but also for growth and development, nutrient delivery, toxin avoidance, and pathogen defense. The precise mechanisms of endocytosis in plants remain quite elusive. The lack of direct visualization and examination of single events of endocytosis has greatly hampered our ability to precisely monitor the cell surface lifetime and the recruitment profile of proteins driving endocytosis or endocytosed cargos in plants. Here, we discuss the necessity to systematically implement total internal reflection fluorescence microcopy (TIRF) in the Plant Cell Biology community and present reliable protocols for high spatial and temporal imaging of endocytosis in plants using clathrin-mediated endocytosis as a test case, since it represents the major route for internalization of cell-surface proteins in plants. We developed a robust method to directly visualize cell surface proteins using TIRF microscopy combined to a high throughput, automated and unbiased analysis pipeline to determine the temporal recruitment profile of proteins to single sites of endocytosis, using the departure of clathrin as a physiological reference for scission. Using this 'departure assay', we assessed the recruitment of two different AP-2 subunits, alpha and mu, to the sites of endocytosis and found that AP2A1 was recruited in concert with clathrin, while AP2M was not. This validated approach therefore offers a powerful solution to better characterize the plant endocytic machinery and the dynamics of one's favorite cargo protein.
    Mots-clés : Arabidopsis, BIOCELL, Endocytosis, imaging techniques, Plants, TIRF microscopy, trafficking, UBINET.

  • O. Khalimonchuk, M. Bestwick, B. Meunier, T. C. Watts, et D. R. Winge, « Correction for Khalimonchuk et al., "Formation of the Redox Cofactor Centers during Cox1 Maturation in Yeast Cytochrome Oxidase" », Molecular and Cellular Biology, vol. 37, nᵒ 11, 2017.

  • J. Marion, R. Le Bars, B. Satiat-Jeunemaitre, et C. Boulogne, « Optimizing CLEM protocols for plants cells: GMA embedding and cryosections as alternatives for preservation of GFP fluorescence in Arabidopsis roots », Journal of Structural Biology, 2017.
    Mots-clés : Arabidopsis, BIOCELL, Correlative microscopy, DYNBSJ, GFP, GMA resin, MET, PF, PHOT, Tokuyasu, Transmission electron microscopy.

  • S. Martins, G. Vert, et Y. Jaillais, « Probing Activation and Deactivation of the BRASSINOSTEROID INSENSITIVE1 Receptor Kinase by Immunoprecipitation », Methods in Molecular Biology (Clifton, N.J.), vol. 1564, p. 169-180, 2017.
    Résumé : Brassinosteroids (BRs) are sterol-derived hormones that control plant growth and development. The BR receptor complex is encoded by the BRASSINOSTEROID INSENSITIVE1 (BRI1) and members of the SOMATIC EMBRYOGENESIS RECEPTOR KINASE family. For activation and deactivation, the BR receptor complex uses different posttranslational modifications and recruits various partner proteins. Here, we describe optimized immunoprecipitation protocols and variants for biochemical analyses of posttranslational modifications of BRI1 and of protein-protein interactions.
    Mots-clés : BIOCELL, Brassinosteroids, BRI1, Immunoprecipitation, Phosphorylation, Protein–protein interaction, UBINET, Ubiquitination.

  • P. Pétriacq, L. de Bont, L. Genestout, J. Hao, C. Laureau, I. Florez-Sarasa, T. Rzigui, G. Queval, F. Gilard, C. Mauve, F. Guérard, M. Lamothe-Sibold, J. Marion, C. Fresneau, S. Brown, A. Danon, A. Krieger-Liszkay, R. Berthomé, M. Ribas-Carbo, G. Tcherkez, G. Cornic, B. Pineau, B. Gakière, et R. De Paepe, « Photoperiod Affects the Phenotype of Mitochondrial Complex I Mutants », Plant Physiology, vol. 173, nᵒ 1, p. 434-455, 2017.
    Mots-clés : B3S, BIOCELL, DYNBSJ, MROP, PF, PHOT.

  • P. Richards, S. Ourabah, J. Montagne, A. - F. Burnol, C. Postic, et S. Guilmeau, « MondoA/ChREBP: The usual suspects of transcriptional glucose sensing; Implication in pathophysiology », Metabolism: Clinical and Experimental, vol. 70, p. 133-151, 2017.
    Résumé : Identification of the Mondo glucose-responsive transcription factors family, including the MondoA and MondoB/ChREBP paralogs, has shed light on the mechanism whereby glucose affects gene transcription. They have clearly emerged, in recent years, as key mediators of glucose sensing by multiple cell types. MondoA and ChREBP have overlapping yet distinct expression profiles, which underlie their downstream targets and separate roles in regulating genes involved in glucose metabolism. MondoA can restrict glucose uptake and influences energy utilization in skeletal muscle, while ChREBP signals energy storage through de novo lipogenesis in liver and white adipose tissue. Because Mondo proteins mediate metabolic adaptations to changing glucose levels, a better understanding of cellular glucose sensing through Mondo proteins will likely uncover new therapeutic opportunities in the context of the imbalanced glucose homeostasis that accompanies metabolic diseases such as type 2 diabetes and cancer. Here, we provide an overview of structural homologies, transcriptional partners as well as the nutrient and hormonal mechanisms underlying Mondo proteins regulation. We next summarize their relative contribution to energy metabolism changes in physiological states and the evolutionary conservation of these pathways. Finally, we discuss their possible targeting in human pathologies.
    Mots-clés : BIOCELL, cancer, ChREBP, Diabetes, Glucose and lipid metabolism, METABO, MondoA.

  • L. Shi, K. France, O. Arnaiz, et J. Cohen, « The Ciliary Protein IFT57 in the Macronucleus of Paramecium », The Journal of Eukaryotic Microbiology, 2017.
    Résumé : The intraflagellar transport IFT57 protein is essential for ciliary growth and maintenance. Also known as HIPPI, human IFT57 can be translocated to the nucleus via a molecular partner of the Huntingtin, Hip1, inducing gene expression changes. In Paramecium tetraurelia, we identified four IFT57 genes forming two subfamilies IFT57A/B and IFT57C/D arising from whole genome duplications. The depletion of proteins of the two subfamilies induced ciliary defects and IFT57A and IFT57C localized in basal bodies and cilia. We observed that IFT57A, but not IFT57C, is also present in the macronucleus and able to traffic toward the developing anlage during autogamy. Analysis of chimeric IFT57A-IFT57C-GFP-tagged proteins allowed us to identify a region of IFT57A necessary for nuclear localization. We studied the localization of the unique IFT57 protein of Paramecium caudatum, a species, which diverged from Paramecium tetraurelia before the whole genome duplications. The Paramecium caudatum IFT57C protein was excluded from the nucleus. We also analyzed whether the overexpression of IFT57A in Paramecium could affect gene transcription as the human protein does in HeLa cells. The expression of some genes was indeed affected by overexpression of IFT57A, but the set of affected genes poorly overlaps the set of genes affected in human cells. This article is protected by copyright. All rights reserved.
    Mots-clés : ANGE, BIOCELL, BIOCIL, cilia, DBG, IFT57 /HIPPI, intraflagellar transport (IFT), Macronucleus, Paramecium.

  • C. Stringari, L. Abdeladim, G. Malkinson, P. Mahou, X. Solinas, I. Lamarre, S. Brizion, J. - B. Galey, W. Supatto, R. Legouis, A. - M. Pena, et E. Beaurepaire, « Multicolor two-photon imaging of endogenous fluorophores in living tissues by wavelength mixing », Scientific Reports, vol. 7, nᵒ 1, p. 3792, 2017.
    Résumé : Two-photon imaging of endogenous fluorescence can provide physiological and metabolic information from intact tissues. However, simultaneous imaging of multiple intrinsic fluorophores, such as nicotinamide adenine dinucleotide(phosphate) (NAD(P)H), flavin adenine dinucleotide (FAD) and retinoids in living systems is generally hampered by sequential multi-wavelength excitation resulting in motion artifacts. Here, we report on efficient and simultaneous multicolor two-photon excitation of endogenous fluorophores with absorption spectra spanning the 750-1040 nm range, using wavelength mixing. By using two synchronized pulse trains at 760 and 1041 nm, an additional equivalent two-photon excitation wavelength at 879 nm is generated, and achieves simultaneous excitation of blue, green and red intrinsic fluorophores. This method permits an efficient simultaneous imaging of the metabolic coenzymes NADH and FAD to be implemented with perfect image co-registration, overcoming the difficulties associated with differences in absorption spectra and disparity in concentration. We demonstrate ratiometric redox imaging free of motion artifacts and simultaneous two-photon fluorescence lifetime imaging (FLIM) of NADH and FAD in living tissues. The lifetime gradients of NADH and FAD associated with different cellular metabolic and differentiation states in reconstructed human skin and in the germline of live C. Elegans are thus simultaneously measured. Finally, we present multicolor imaging of endogenous fluorophores and second harmonic generation (SHG) signals during the early stages of Zebrafish embryo development, evidencing fluorescence spectral changes associated with development.
    Mots-clés : BIOCELL, OTOFAG.

  • F. Thomas, S. Rome, F. Mery, E. Dawson, J. Montagne, P. A. Biro, C. Beckmann, F. Renaud, R. Poulin, M. Raymond, et B. Ujvari, « Changes in diet associated with cancer: An evolutionary perspective », Evolutionary Applications, vol. 10, nᵒ 7, p. 651-657, 2017.
    Résumé : Changes in diet are frequently correlated with the occurrence and progression of malignant tumors (i.e., cancer) in both humans and other animals, but an integrated conceptual framework to interpret these changes still needs to be developed. Our aim is to provide a new perspective on dietary changes in tumor-bearing individuals by adapting concepts from parasitology. Dietary changes may occur alongside tumor progression for several reasons: (i) as a pathological side effect with no adaptive value, (ii) as the result of self-medication by the host to eradicate the tumor and/or to slow down its progression, (iii) as a result of host manipulation by the tumor that benefits its progression, and finally (iv) as a host tolerance strategy, to alleviate and repair damages caused by tumor progression. Surprisingly, this tolerance strategy can be beneficial for the host even if diet changes are beneficial to tumor progression, provided that cancer-induced death occurs sufficiently late (i.e., when natural selection is weak). We argue that more data and a unifying evolutionary framework, especially during the early stages of tumorigenesis, are needed to understand the links between changes in diet and tumor progression. We argue that a focus on dietary changes accompanying tumor progression can offer novel preventive and therapeutic strategies against cancer.
    Mots-clés : BIOCELL, malignant cells, manipulation, METABO, nutrition, self‐medication, resistance, tolerance.

  • A. Y. Torres, M. Malartre, A. - M. Pret, et F. Agnès, « JAK/STAT signaling is necessary for cell monosis prior to epithelial cell apoptotic extrusion », Cell Death & Disease, vol. 8, nᵒ 5, p. e2814, 2017.
    Résumé : Epithelial cell extrusion is crucial for proper development and tissue homeostasis. High-resolution 3D reconstruction and 4D imaging, combined with genetic analyis, have allowed us to reveal the highly-sterotyped morphogenetic events controlled by JAK/STAT signaling in a developmentally-programmed case of epithelial cell extrusion. Specialized somatic cells, Polar Cells (PCs), are produced in excess and then undergo apoptotic elimination from the follicular epithelium in the Drosophila ovary. We show that supernumerary PCs are first systematically enveloped by PC neighbors on all sides, first laterally, then apically in conjunction with highly-reinforced adherens junctions, and finally basally. The PC to be removed thus loses all contact with follicle cells, germline cells and the basement membrane in a process we have called cell 'monosis', for 'isolation' in Greek. PC monosis takes several hours, and always precedes, and is independent of, activation of apoptosis. JAK/STAT signaling is necessary within the surrounding follicular epithelium for PC monosis. Minutes after monosis is complete, PC apoptotic corpses are formed and extruded laterally within the epithelium, in contrast to the apical and basal extrusions described to date. These apoptotic corpses are engulfed and eliminated by surrounding follicle cells, which are thus acting as non-professional phagocytes. This study therefore shows the non cell-autonomous impact of an epithelium, via JAK/STAT signaling activation, on cell morphogenesis events leading to apoptotic extrusion. It is likely that the use of high-resolution 3D and 4D imaging, which allows for better spatio-temporal understanding of morphogenetic events, will reveal that cell monosis and lateral extrusion within an epithelium are pertinent for other cases of epithelial cell extrusion as well.
    Mots-clés : BIOCELL, SIGDEV.


  • C. Appenzeller-Herzog, G. Bánhegyi, I. Bogeski, K. J. A. Davies, A. Delaunay-Moisan, H. J. Forman, A. Görlach, T. Kietzmann, F. Laurindo, E. Margittai, A. J. Meyer, J. Riemer, M. Rützler, T. Simmen, R. Sitia, M. B. Toledano, et I. P. Touw, « Transit of H2O2 across the endoplasmic reticulum membrane is not sluggish », Free Radical Biology and Medicine, vol. 94, p. 157-160, 2016.

  • U. Baetz, C. Eisenach, T. Tohge, E. Martinoia, et A. De Angeli, « Vacuolar Chloride Fluxes Impact Ion content and Distribution during Early Salinity Stress », Plant Physiology, p. pp.00183.2016, août 2016.

  • A. Belyy, D. Raoux-Barbot, C. Saveanu, A. Namane, V. Ogryzko, L. Worpenberg, V. David, V. Henriot, S. Fellous, C. Merrifield, E. Assayag, D. Ladant, L. Renault, et U. Mechold, « Actin activates Pseudomonas aeruginosa ExoY nucleotidyl cyclase toxin and ExoY-like effector domains from MARTX toxins », Nature Communications, vol. 7, p. 13582, déc. 2016.
    Mots-clés : ACTIN, B3S, BIOCELL, ENDEXO.

  • I. Damiani, A. Drain, M. Guichard, S. Balzergue, A. Boscari, J. - C. Boyer, V. Brunaud, S. Cottaz, C. Rancurel, M. Da Rocha, C. Fizames, S. Fort, I. Gaillard, V. Maillol, E. G. J. Danchin, H. Rouached, E. Samain, Y. - H. Su, J. Thouin, B. Touraine, A. Puppo, J. - M. Frachisse, N. Pauly, et H. Sentenac, « Nod Factor Effects on Root Hair-Specific Transcriptome of Medicago truncatula: Focus on Plasma Membrane Transport Systems and Reactive Oxygen Species Networks », Frontiers in Plant Science, vol. 7, juin 2016.
    Mots-clés : BIOCELL, deep-RNA sequencing, legume-rhizobium symbiosis, Medicago truncatula, MINION, Nod factors (lipochitooligosaccharides), plasma membrane transport systems, Reactive Oxygen Species, root hairs.

  • T. Delerue, F. Khosrobakhsh, M. Daloyau, L. J. Emorine, A. Dedieu, C. J. Herbert, N. Bonnefoy, L. Arnauné-Pelloquin, et P. Belenguer, « Loss of Msp1p in Schizosaccharomyces pombe induces a ROS-dependent nuclear mutator phenotype that affects mitochondrial fission genes », FEBS Letters, vol. 590, nᵒ 20, p. 3544-3558, 2016.
    Mots-clés : BIOCELL, BIOMIT, mitochondrial DNA, mitochondrial fission and fusion, Schizosaccharomyces pombe.

  • A. De Angeli, S. Thomine, et J. - M. Frachisse, « Anion Channel Blockage by ATP as a Means for Membranes to Perceive the Energy Status of the Cell », Molecular Plant, vol. 9, nᵒ 3, p. 320-322, 2016.
    Mots-clés : Adenosine Triphosphate, Arabidopsis, BIOCELL, Cell Membrane, Energy Metabolism, MINION.

  • A. Guimier, C.  T. Gordon, F. Godard, G. Ravenscroft, M. Oufadem, C. Vasnier, C. Rambaud, P. Nitschke, C. Bole-Feysot, C. Masson, S. Dauger, C. Longman, N.  G. Laing, B. Kugener, D. Bonnet, P. Bouvagnet, S. Di Filippo, V. Probst, R. Redon, P. Charron, A. Rötig, S. Lyonnet, A. Dautant, L. de Pontual, J. - P. di Rago, A. Delahodde, et J. Amiel, « Biallelic PPA2 Mutations Cause Sudden Unexpected Cardiac Arrest in Infancy », American Journal of Human Genetics, vol. 99, nᵒ 3, p. 666-673, 2016.

  • S. Hanzén, K. Vielfort, J. Yang, F. Roger, V. Andersson, S. Zamarbide-Forés, R. Andersson, L. Malm, G. Palais, B. Biteau, B. Liu, M. B. Toledano, M. Molin, et T. Nyström, « Lifespan Control by Redox-Dependent Recruitment of Chaperones to Misfolded Proteins », Cell, vol. 166, nᵒ 1, p. 140-151, 2016.
    Résumé : Caloric restriction (CR) extends the lifespan of flies, worms, and yeast by counteracting age-related oxidation of H2O2-scavenging peroxiredoxins (Prxs). Here, we show that increased dosage of the major cytosolic Prx in yeast, Tsa1, extends lifespan in an Hsp70 chaperone-dependent and CR-independent manner without increasing H2O2 scavenging or genome stability. We found that Tsa1 and Hsp70 physically interact and that hyperoxidation of Tsa1 by H2O2 is required for the recruitment of the Hsp70 chaperones and the Hsp104 disaggregase to misfolded and aggregated proteins during aging, but not heat stress. Tsa1 counteracted the accumulation of ubiquitinated aggregates during aging and the reduction of hyperoxidized Tsa1 by sulfiredoxin facilitated clearance of H2O2-generated aggregates. The data reveal a conceptually new role for H2O2 signaling in proteostasis and lifespan control and shed new light on the selective benefits endowed to eukaryotic peroxiredoxins by their reversible hyperoxidation.
    Mots-clés : Animals, BIOCELL, Caloric Restriction, Genomic Instability, Heat-Shock Proteins, HSP70 Heat-Shock Proteins, Humans, Hydrogen Peroxide, Longevity, Oxidation-Reduction, Peroxidases, Protein Aggregates, Protein Folding, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Signal Transduction, SOC.

  • Y. Jaillais et G. Vert, « Brassinosteroid signaling and BRI1 dynamics went underground », Current Opinion in Plant Biology, vol. 33, p. 92-100, 2016.

  • A. Johnson et G. Vert, « Unraveling K63 Polyubiquitination Networks by Sensor-Based Proteomics », Plant Physiology, vol. 171, nᵒ 3, p. 1808-1820, 2016.

  • D. J. Klionsky, K. Abdelmohsen, A. Abe, M. J. Abedin, H. Abeliovich, A. Acevedo Arozena, H. Adachi, C. M. Adams, P. D. Adams, K. Adeli, P. J. Adhihetty, S. G. Adler, G. Agam, R. Agarwal, M. K. Aghi, M. Agnello, P. Agostinis, P. V. Aguilar, J. Aguirre-Ghiso, E. M. Airoldi, S. Ait-Si-Ali, T. Akematsu, E. T. Akporiaye, M. Al-Rubeai, G. M. Albaiceta, C. Albanese, D. Albani, M. L. Albert, J. Aldudo, H. Algül, M. Alirezaei, I. Alloza, A. Almasan, M. Almonte-Beceril, E. S. Alnemri, C. Alonso, N. Altan-Bonnet, D. C. Altieri, S. Alvarez, L. Alvarez-Erviti, S. Alves, G. Amadoro, A. Amano, C. Amantini, S. Ambrosio, I. Amelio, A. O. Amer, M. Amessou, A. Amon, Z. An, F. A. Anania, S. U. Andersen, U. P. Andley, C. K. Andreadi, N. Andrieu-Abadie, A. Anel, D. K. Ann, S. Anoopkumar-Dukie, M. Antonioli, H. Aoki, N. Apostolova, S. Aquila, K. Aquilano, K. Araki, E. Arama, A. Aranda, J. Araya, A. Arcaro, E. Arias, H. Arimoto, A. R. Ariosa, J. L. Armstrong, T. Arnould, I. Arsov, K. Asanuma, V. Askanas, E. Asselin, R. Atarashi, S. S. Atherton, J. D. Atkin, L. D. Attardi, P. Auberger, G. Auburger, L. Aurelian, R. Autelli, L. Avagliano, M. L. Avantaggiati, L. Avrahami, S. Awale, N. Azad, T. Bachetti, J. M. Backer, D. - H. Bae, J. - S. Bae, O. - N. Bae, S. H. Bae, E. H. Baehrecke, S. - H. Baek, S. Baghdiguian, A. Bagniewska-Zadworna, H. Bai, J. Bai, X. - Y. Bai, Y. Bailly, K. N. Balaji, W. Balduini, A. Ballabio, R. Balzan, R. Banerjee, G. Bánhegyi, H. Bao, B. Barbeau, M. D. Barrachina, E. Barreiro, B. Bartel, A. Bartolomé, D. C. Bassham, M. T. Bassi, R. C. Bast, A. Basu, M. T. Batista, H. Batoko, M. Battino, K. Bauckman, B. L. Baumgarner, K. U. Bayer, R. Beale, J. - F. Beaulieu, G. R. Beck, C. Becker, J. D. Beckham, P. - A. Bédard, P. J. Bednarski, T. J. Begley, C. Behl, C. Behrends, G. M. Behrens, K. E. Behrns, E. Bejarano, A. Belaid, F. Belleudi, G. Bénard, G. Berchem, D. Bergamaschi, M. Bergami, B. Berkhout, L. Berliocchi, A. Bernard, M. Bernard, F. Bernassola, A. Bertolotti, A. S. Bess, S. Besteiro, S. Bettuzzi, S. Bhalla, S. Bhattacharyya, S. K. Bhutia, C. Biagosch, M. W. Bianchi, M. Biard-Piechaczyk, V. Billes, C. Bincoletto, B. Bingol, S. W. Bird, M. Bitoun, I. Bjedov, C. Blackstone, L. Blanc, G. A. Blanco, H. K. Blomhoff, E. Boada-Romero, S. Böckler, M. Boes, K. Boesze-Battaglia, L. H. Boise, A. Bolino, A. Boman, P. Bonaldo, M. Bordi, J. Bosch, L. M. Botana, J. Botti, G. Bou, M. Bouché, M. Bouchecareilh, M. - J. Boucher, M. E. Boulton, S. G. Bouret, P. Boya, M. Boyer-Guittaut, P. V. Bozhkov, N. Brady, V. M. Braga, C. Brancolini, G. H. Braus, J. M. Bravo-San Pedro, L. A. Brennan, E. H. Bresnick, P. Brest, D. Bridges, M. - A. Bringer, M. Brini, G. C. Brito, B. Brodin, P. S. Brookes, E. J. Brown, K. Brown, H. E. Broxmeyer, A. Bruhat, P. C. Brum, J. H. Brumell, N. Brunetti-Pierri, R. J. Bryson-Richardson, S. Buch, A. M. Buchan, H. Budak, D. V. Bulavin, S. J. Bultman, G. Bultynck, V. Bumbasirevic, Y. Burelle, R. E. Burke, M. Burmeister, P. Bütikofer, L. Caberlotto, K. Cadwell, M. Cahova, D. Cai, J. Cai, Q. Cai, S. Calatayud, N. Camougrand, M. Campanella, G. R. Campbell, M. Campbell, S. Campello, R. Candau, I. Caniggia, L. Cantoni, L. Cao, A. B. Caplan, M. Caraglia, C. Cardinali, S. M. Cardoso, J. S. Carew, L. A. Carleton, C. R. Carlin, S. Carloni, S. R. Carlsson, D. Carmona-Gutierrez, L. A. Carneiro, O. Carnevali, S. Carra, A. Carrier, B. Carroll, C. Casas, J. Casas, G. Cassinelli, P. Castets, S. Castro-Obregon, G. Cavallini, I. Ceccherini, F. Cecconi, A. I. Cederbaum, V. Ceña, S. Cenci, C. Cerella, D. Cervia, S. Cetrullo, H. Chaachouay, H. - J. Chae, A. S. Chagin, C. - Y. Chai, G. Chakrabarti, G. Chamilos, E. Y. Chan, M. T. Chan, D. Chandra, P. Chandra, C. - P. Chang, R. C. - C. Chang, T. Y. Chang, J. C. Chatham, S. Chatterjee, S. Chauhan, Y. Che, M. E. Cheetham, R. Cheluvappa, C. - J. Chen, G. Chen, G. - C. Chen, G. Chen, H. Chen, J. W. Chen, J. - K. Chen, M. Chen, M. Chen, P. Chen, Q. Chen, Q. Chen, S. - D. Chen, S. Chen, S. S. - L. Chen, W. Chen, W. - J. Chen, W. Q. Chen, W. Chen, X. Chen, Y. - H. Chen, Y. - G. Chen, Y. Chen, Y. Chen, Y. Chen, Y. - J. Chen, Y. - Q. Chen, Y. Chen, Z. Chen, Z. Chen, A. Cheng, C. H. Cheng, H. Cheng, H. Cheong, S. Cherry, J. Chesney, C. H. A. Cheung, E. Chevet, H. C. Chi, S. - G. Chi, F. Chiacchiera, H. - L. Chiang, R. Chiarelli, M. Chiariello, M. Chieppa, L. - S. Chin, M. Chiong, G. N. Chiu, D. - H. Cho, S. - G. Cho, W. C. Cho, Y. - Y. Cho, Y. - S. Cho, A. M. Choi, E. - J. Choi, E. - K. Choi, J. Choi, M. E. Choi, S. - I. Choi, T. - F. Chou, S. Chouaib, D. Choubey, V. Choubey, K. - C. Chow, K. Chowdhury, C. T. Chu, T. - H. Chuang, T. Chun, H. Chung, T. Chung, Y. - L. Chung, Y. - J. Chwae, V. Cianfanelli, R. Ciarcia, I. A. Ciechomska, M. R. Ciriolo, M. Cirone, S. Claerhout, M. J. Clague, J. Clària, P. G. Clarke, R. Clarke, E. Clementi, C. Cleyrat, M. Cnop, E. M. Coccia, T. Cocco, P. Codogno, J. Coers, E. E. Cohen, D. Colecchia, L. Coletto, N. S. Coll, E. Colucci-Guyon, S. Comincini, M. Condello, K. L. Cook, G. H. Coombs, C. D. Cooper, J. M. Cooper, I. Coppens, M. T. Corasaniti, M. Corazzari, R. Corbalan, E. Corcelle-Termeau, M. D. Cordero, C. Corral-Ramos, O. Corti, A. Cossarizza, P. Costelli, S. Costes, S. L. Cotman, A. Coto-Montes, S. Cottet, E. Couve, L. R. Covey, L. A. Cowart, J. S. Cox, F. P. Coxon, C. B. Coyne, M. S. Cragg, R. J. Craven, T. Crepaldi, J. L. Crespo, A. Criollo, V. Crippa, M. T. Cruz, A. M. Cuervo, J. M. Cuezva, T. Cui, P. R. Cutillas, M. J. Czaja, M. F. Czyzyk-Krzeska, R. K. Dagda, U. Dahmen, C. Dai, W. Dai, Y. Dai, K. N. Dalby, L. Dalla Valle, G. Dalmasso, M. D'Amelio, M. Damme, A. Darfeuille-Michaud, C. Dargemont, V. M. Darley-Usmar, S. Dasarathy, B. Dasgupta, S. Dash, C. R. Dass, H. M. Davey, L. M. Davids, D. Dávila, R. J. Davis, T. M. Dawson, V. L. Dawson, P. Daza, J. de Belleroche, P. de Figueiredo, R. C. B. Q. de Figueiredo, J. de la Fuente, L. De Martino, A. De Matteis, G. R. De Meyer, A. De Milito, M. De Santi, W. de Souza, V. De Tata, D. De Zio, J. Debnath, R. Dechant, J. - P. Decuypere, S. Deegan, B. Dehay, B. Del Bello, D. P. Del Re, R. Delage-Mourroux, L. M. Delbridge, L. Deldicque, E. Delorme-Axford, Y. Deng, J. Dengjel, M. Denizot, P. Dent, C. J. Der, V. Deretic, B. Derrien, E. Deutsch, T. P. Devarenne, R. J. Devenish, S. Di Bartolomeo, N. Di Daniele, F. Di Domenico, A. Di Nardo, S. Di Paola, A. Di Pietro, L. Di Renzo, A. DiAntonio, G. Díaz-Araya, I. Díaz-Laviada, M. T. Diaz-Meco, J. Diaz-Nido, C. A. Dickey, R. C. Dickson, M. Diederich, P. Digard, I. Dikic, S. P. Dinesh-Kumar, C. Ding, W. - X. Ding, Z. Ding, L. Dini, J. H. Distler, A. Diwan, M. Djavaheri-Mergny, K. Dmytruk, R. C. Dobson, V. Doetsch, K. Dokladny, S. Dokudovskaya, M. Donadelli, X. C. Dong, X. Dong, Z. Dong, T. M. Donohue, K. S. Doran, G. D'Orazi, G. W. Dorn, V. Dosenko, S. Dridi, L. Drucker, J. Du, L. - L. Du, L. Du, A. du Toit, P. Dua, L. Duan, P. Duann, V. K. Dubey, M. R. Duchen, M. A. Duchosal, H. Duez, I. Dugail, V. I. Dumit, M. C. Duncan, E. A. Dunlop, W. A. Dunn, N. Dupont, L. Dupuis, R. V. Durán, T. M. Durcan, S. Duvezin-Caubet, U. Duvvuri, V. Eapen, D. Ebrahimi-Fakhari, A. Echard, L. Eckhart, C. L. Edelstein, A. L. Edinger, L. Eichinger, T. Eisenberg, A. Eisenberg-Lerner, N. T. Eissa, W. S. El-Deiry, V. El-Khoury, Z. Elazar, H. Eldar-Finkelman, C. J. Elliott, E. Emanuele, U. Emmenegger, N. Engedal, A. - M. Engelbrecht, S. Engelender, J. M. Enserink, R. Erdmann, J. Erenpreisa, R. Eri, J. L. Eriksen, A. Erman, R. Escalante, E. - L. Eskelinen, L. Espert, L. Esteban-Martínez, T. J. Evans, M. Fabri, G. Fabrias, C. Fabrizi, A. Facchiano, N. J. Færgeman, A. Faggioni, W. D. Fairlie, C. Fan, D. Fan, J. Fan, S. Fang, M. Fanto, A. Fanzani, T. Farkas, M. Faure, F. B. Favier, H. Fearnhead, M. Federici, E. Fei, T. C. Felizardo, H. Feng, Y. Feng, Y. Feng, T. A. Ferguson, Á. F. Fernández, M. G. Fernandez-Barrena, J. C. Fernandez-Checa, A. Fernández-López, M. E. Fernandez-Zapico, O. Feron, E. Ferraro, C. V. Ferreira-Halder, L. Fesus, R. Feuer, F. C. Fiesel, E. C. Filippi-Chiela, G. Filomeni, G. M. Fimia, J. H. Fingert, S. Finkbeiner, T. Finkel, F. Fiorito, P. B. Fisher, M. Flajolet, F. Flamigni, O. Florey, S. Florio, R. A. Floto, M. Folini, C. Follo, E. A. Fon, F. Fornai, F. Fortunato, A. Fraldi, R. Franco, A. Francois, A. François, L. B. Frankel, I. D. Fraser, N. Frey, D. G. Freyssenet, C. Frezza, S. L. Friedman, D. E. Frigo, D. Fu, J. M. Fuentes, J. Fueyo, Y. Fujitani, Y. Fujiwara, M. Fujiya, M. Fukuda, S. Fulda, C. Fusco, B. Gabryel, M. Gaestel, P. Gailly, M. Gajewska, S. Galadari, G. Galili, I. Galindo, M. F. Galindo, G. Galliciotti, L. Galluzzi, L. Galluzzi, V. Galy, N. Gammoh, S. Gandy, A. K. Ganesan, S. Ganesan, I. G. Ganley, M. Gannagé, F. - B. Gao, F. Gao, J. - X. Gao, L. García Nannig, E. García Véscovi, M. Garcia-Macía, C. Garcia-Ruiz, A. D. Garg, P. K. Garg, R. Gargini, N. C. Gassen, D. Gatica, E. Gatti, J. Gavard, E. Gavathiotis, L. Ge, P. Ge, S. Ge, P. - W. Gean, V. Gelmetti, A. A. Genazzani, J. Geng, P. Genschik, L. Gerner, J. E. Gestwicki, D. A. Gewirtz, S. Ghavami, E. Ghigo, D. Ghosh, A. M. Giammarioli, F. Giampieri, C. Giampietri, A. Giatromanolaki, D. J. Gibbings, L. Gibellini, S. B. Gibson, V. Ginet, A. Giordano, F. Giorgini, E. Giovannetti, S. E. Girardin, S. Gispert, S. Giuliano, C. L. Gladson, A. Glavic, M. Gleave, N. Godefroy, R. M. Gogal, K. Gokulan, G. H. Goldman, D. Goletti, M. S. Goligorsky, A. V. Gomes, L. C. Gomes, H. Gomez, C. Gomez-Manzano, R. Gómez-Sánchez, D. A. Gonçalves, E. Goncu, Q. Gong, C. Gongora, C. B. Gonzalez, P. Gonzalez-Alegre, P. Gonzalez-Cabo, R. A. González-Polo, I. S. Goping, C. Gorbea, N. V. Gorbunov, D. R. Goring, A. M. Gorman, S. M. Gorski, S. Goruppi, S. Goto-Yamada, C. Gotor, R. A. Gottlieb, I. Gozes, D. Gozuacik, Y. Graba, M. Graef, G. E. Granato, G. D. Grant, S. Grant, G. L. Gravina, D. R. Green, A. Greenhough, M. T. Greenwood, B. Grimaldi, F. Gros, C. Grose, J. - F. Groulx, F. Gruber, P. Grumati, T. Grune, J. - L. Guan, K. - L. Guan, B. Guerra, C. Guillen, K. Gulshan, J. Gunst, C. Guo, L. Guo, M. Guo, W. Guo, X. - G. Guo, A. A. Gust, Å. B. Gustafsson, E. Gutierrez, M. G. Gutierrez, H. - S. Gwak, A. Haas, J. E. Haber, S. Hadano, M. Hagedorn, D. R. Hahn, A. J. Halayko, A. Hamacher-Brady, K. Hamada, A. Hamai, A. Hamann, M. Hamasaki, I. Hamer, Q. Hamid, E. M. Hammond, F. Han, W. Han, J. T. Handa, J. A. Hanover, M. Hansen, M. Harada, L. Harhaji-Trajkovic, J. W. Harper, A. H. Harrath, A. L. Harris, J. Harris, U. Hasler, P. Hasselblatt, K. Hasui, R. G. Hawley, T. S. Hawley, C. He, C. Y. He, F. He, G. He, R. - R. He, X. - H. He, Y. - W. He, Y. - Y. He, J. K. Heath, M. - J. Hébert, R. A. Heinzen, G. V. Helgason, M. Hensel, E. P. Henske, C. Her, P. K. Herman, A. Hernández, C. Hernandez, S. Hernández-Tiedra, C. Hetz, P. R. Hiesinger, K. Higaki, S. Hilfiker, B. G. Hill, J. A. Hill, W. D. Hill, K. Hino, D. Hofius, P. Hofman, G. U. Höglinger, J. Höhfeld, M. K. Holz, Y. Hong, D. A. Hood, J. J. Hoozemans, T. Hoppe, C. Hsu, C. - Y. Hsu, L. - C. Hsu, D. Hu, G. Hu, H. - M. Hu, H. Hu, M. C. Hu, Y. - C. Hu, Z. - W. Hu, F. Hua, Y. Hua, C. Huang, H. - L. Huang, K. - H. Huang, K. - Y. Huang, S. Huang, S. Huang, W. - P. Huang, Y. - R. Huang, Y. Huang, Y. Huang, T. B. Huber, P. Huebbe, W. - K. Huh, J. J. Hulmi, G. M. Hur, J. H. Hurley, Z. Husak, S. N. Hussain, S. Hussain, J. J. Hwang, S. Hwang, T. I. Hwang, A. Ichihara, Y. Imai, C. Imbriano, M. Inomata, T. Into, V. Iovane, J. L. Iovanna, R. V. Iozzo, N. Y. Ip, J. E. Irazoqui, P. Iribarren, Y. Isaka, A. J. Isakovic, H. Ischiropoulos, J. S. Isenberg, M. Ishaq, H. Ishida, I. Ishii, J. E. Ishmael, C. Isidoro, K. - I. Isobe, E. Isono, S. Issazadeh-Navikas, K. Itahana, E. Itakura, A. I. Ivanov, A. K. V. Iyer, J. M. Izquierdo, Y. Izumi, V. Izzo, M. Jäättelä, N. Jaber, D. J. Jackson, W. T. Jackson, T. G. Jacob, T. S. Jacques, C. Jagannath, A. Jain, N. R. Jana, B. K. Jang, A. Jani, B. Janji, P. R. Jannig, P. J. Jansson, S. Jean, M. Jendrach, J. - H. Jeon, N. Jessen, E. - B. Jeung, K. Jia, L. Jia, H. Jiang, H. Jiang, L. Jiang, T. Jiang, X. Jiang, X. Jiang, X. Jiang, Y. Jiang, Y. Jiang, A. Jiménez, C. Jin, H. Jin, L. Jin, M. Jin, S. Jin, U. K. Jinwal, E. - K. Jo, T. Johansen, D. E. Johnson, G. V. Johnson, J. D. Johnson, E. Jonasch, C. Jones, L. A. Joosten, J. Jordan, A. - M. Joseph, B. Joseph, A. M. Joubert, D. Ju, J. Ju, H. - F. Juan, K. Juenemann, G. Juhász, H. S. Jung, J. U. Jung, Y. - K. Jung, H. Jungbluth, M. J. Justice, B. Jutten, N. O. Kaakoush, K. Kaarniranta, A. Kaasik, T. Kabuta, B. Kaeffer, K. Kågedal, A. Kahana, S. Kajimura, O. Kakhlon, M. Kalia, D. V. Kalvakolanu, Y. Kamada, K. Kambas, V. O. Kaminskyy, H. H. Kampinga, M. Kandouz, C. Kang, R. Kang, T. - C. Kang, T. Kanki, T. - D. Kanneganti, H. Kanno, A. G. Kanthasamy, M. Kantorow, M. Kaparakis-Liaskos, O. Kapuy, V. Karantza, M. R. Karim, P. Karmakar, A. Kaser, S. Kaushik, T. Kawula, A. M. Kaynar, P. - Y. Ke, Z. - J. Ke, J. H. Kehrl, K. E. Keller, J. K. Kemper, A. K. Kenworthy, O. Kepp, A. Kern, S. Kesari, D. Kessel, R. Ketteler, I. do C. Kettelhut, B. Khambu, M. M. Khan, V. K. Khandelwal, S. Khare, J. G. Kiang, A. A. Kiger, A. Kihara, A. L. Kim, C. H. Kim, D. R. Kim, D. - H. Kim, E. K. Kim, H. Y. Kim, H. - R. Kim, J. - S. Kim, J. H. Kim, J. C. Kim, J. H. Kim, K. W. Kim, M. D. Kim, M. - M. Kim, P. K. Kim, S. W. Kim, S. - Y. Kim, Y. - S. Kim, Y. Kim, A. Kimchi, A. C. Kimmelman, T. Kimura, J. S. King, K. Kirkegaard, V. Kirkin, L. A. Kirshenbaum, S. Kishi, Y. Kitajima, K. Kitamoto, Y. Kitaoka, K. Kitazato, R. A. Kley, W. T. Klimecki, M. Klinkenberg, J. Klucken, H. Knævelsrud, E. Knecht, L. Knuppertz, J. - L. Ko, S. Kobayashi, J. C. Koch, C. Koechlin-Ramonatxo, U. Koenig, Y. H. Koh, K. Köhler, S. D. Kohlwein, M. Koike, M. Komatsu, E. Kominami, D. Kong, H. J. Kong, E. G. Konstantakou, B. T. Kopp, T. Korcsmaros, L. Korhonen, V. I. Korolchuk, N. V. Koshkina, Y. Kou, M. I. Koukourakis, C. Koumenis, A. L. Kovács, T. Kovács, W. J. Kovacs, D. Koya, C. Kraft, D. Krainc, H. Kramer, T. Kravic-Stevovic, W. Krek, C. Kretz-Remy, R. Krick, M. Krishnamurthy, J. Kriston-Vizi, G. Kroemer, M. C. Kruer, R. Kruger, N. T. Ktistakis, K. Kuchitsu, C. Kuhn, A. P. Kumar, A. Kumar, A. Kumar, D. Kumar, D. Kumar, R. Kumar, S. Kumar, M. Kundu, H. - J. Kung, A. Kuno, S. - H. Kuo, J. Kuret, T. Kurz, T. Kwok, T. K. Kwon, Y. T. Kwon, I. Kyrmizi, A. R. La Spada, F. Lafont, T. Lahm, A. Lakkaraju, T. Lam, T. Lamark, S. Lancel, T. H. Landowski, D. J. R. Lane, J. D. Lane, C. Lanzi, P. Lapaquette, L. R. Lapierre, J. Laporte, J. Laukkarinen, G. W. Laurie, S. Lavandero, L. Lavie, M. J. LaVoie, B. Y. K. Law, H. K. - W. Law, K. B. Law, R. Layfield, P. A. Lazo, L. Le Cam, K. G. Le Roch, H. Le Stunff, V. Leardkamolkarn, M. Lecuit, B. - H. Lee, C. - H. Lee, E. F. Lee, G. M. Lee, H. - J. Lee, H. Lee, J. K. Lee, J. Lee, J. - H. Lee, J. H. Lee, M. Lee, M. - S. Lee, P. J. Lee, S. W. Lee, S. - J. Lee, S. - J. Lee, S. Y. Lee, S. H. Lee, S. S. Lee, S. - J. Lee, S. Lee, Y. - R. Lee, Y. J. Lee, Y. H. Lee, C. Leeuwenburgh, S. Lefort, R. Legouis, J. Lei, Q. - Y. Lei, D. A. Leib, G. Leibowitz, I. Lekli, S. D. Lemaire, J. J. Lemasters, M. K. Lemberg, A. Lemoine, S. Leng, G. Lenz, P. Lenzi, L. O. Lerman, D. Lettieri Barbato, J. I. - J. Leu, H. Y. Leung, B. Levine, P. A. Lewis, F. Lezoualc'h, C. Li, F. Li, F. - J. Li, J. Li, K. Li, L. Li, M. Li, M. Li, Q. Li, R. Li, S. Li, W. Li, W. Li, X. Li, Y. Li, J. Lian, C. Liang, Q. Liang, Y. Liao, J. Liberal, P. P. Liberski, P. Lie, A. P. Lieberman, H. J. Lim, K. - L. Lim, K. Lim, R. T. Lima, C. - S. Lin, C. - F. Lin, F. Lin, F. Lin, F. - C. Lin, K. Lin, K. - H. Lin, P. - H. Lin, T. Lin, W. - W. Lin, Y. - S. Lin, Y. Lin, R. Linden, D. Lindholm, L. M. Lindqvist, P. Lingor, A. Linkermann, L. A. Liotta, M. M. Lipinski, V. A. Lira, M. P. Lisanti, P. B. Liton, B. Liu, C. Liu, C. - F. Liu, F. Liu, H. - J. Liu, J. Liu, J. - J. Liu, J. - L. Liu, K. Liu, L. Liu, L. Liu, Q. Liu, R. - Y. Liu, S. Liu, S. Liu, W. Liu, X. - D. Liu, X. Liu, X. - H. Liu, X. Liu, X. Liu, X. Liu, Y. Liu, Y. Liu, Z. Liu, Z. Liu, J. P. Liuzzi, G. Lizard, M. Ljujic, I. J. Lodhi, S. E. Logue, B. L. Lokeshwar, Y. C. Long, S. Lonial, B. Loos, C. López-Otín, C. López-Vicario, M. Lorente, P. L. Lorenzi, P. Lõrincz, M. Los, M. T. Lotze, P. E. Lovat, B. Lu, B. Lu, J. Lu, Q. Lu, S. - M. Lu, S. Lu, Y. Lu, F. Luciano, S. Luckhart, J. M. Lucocq, P. Ludovico, A. Lugea, N. W. Lukacs, J. J. Lum, A. H. Lund, H. Luo, J. Luo, S. Luo, C. Luparello, T. Lyons, J. Ma, Y. Ma, Y. Ma, Z. Ma, J. Machado, G. M. Machado-Santelli, F. Macian, G. C. MacIntosh, J. P. MacKeigan, K. F. Macleod, J. D. MacMicking, L. A. MacMillan-Crow, F. Madeo, M. Madesh, J. Madrigal-Matute, A. Maeda, T. Maeda, G. Maegawa, E. Maellaro, H. Maes, M. Magariños, K. Maiese, T. K. Maiti, L. Maiuri, M. C. Maiuri, C. G. Maki, R. Malli, W. Malorni, A. Maloyan, F. Mami-Chouaib, N. Man, J. D. Mancias, E. - M. Mandelkow, M. A. Mandell, A. A. Manfredi, S. N. Manié, C. Manzoni, K. Mao, Z. Mao, Z. - W. Mao, P. Marambaud, A. M. Marconi, Z. Marelja, G. Marfe, M. Margeta, E. Margittai, M. Mari, F. V. Mariani, C. Marin, S. Marinelli, G. Mariño, I. Markovic, R. Marquez, A. M. Martelli, S. Martens, K. R. Martin, S. J. Martin, S. Martin, M. A. Martin-Acebes, P. Martín-Sanz, C. Martinand-Mari, W. Martinet, J. Martinez, N. Martinez-Lopez, U. Martinez-Outschoorn, M. Martínez-Velázquez, M. Martinez-Vicente, W. K. Martins, H. Mashima, J. A. Mastrianni, G. Matarese, P. Matarrese, R. Mateo, S. Matoba, N. Matsumoto, T. Matsushita, A. Matsuura, T. Matsuzawa, M. P. Mattson, S. Matus, N. Maugeri, C. Mauvezin, A. Mayer, D. Maysinger, G. D. Mazzolini, M. K. McBrayer, K. McCall, C. McCormick, G. M. McInerney, S. C. McIver, S. McKenna, J. J. McMahon, I. A. McNeish, F. Mechta-Grigoriou, J. P. Medema, D. L. Medina, K. Megyeri, M. Mehrpour, J. L. Mehta, Y. Mei, U. - C. Meier, A. J. Meijer, A. Meléndez, G. Melino, S. Melino, E. J. T. de Melo, M. A. Mena, M. D. Meneghini, J. A. Menendez, R. Menezes, L. Meng, L. - H. Meng, S. Meng, R. Menghini, A. S. Menko, R. F. Menna-Barreto, M. B. Menon, M. A. Meraz-Ríos, G. Merla, L. Merlini, A. M. Merlot, A. Meryk, S. Meschini, J. N. Meyer, M. - T. Mi, C. - Y. Miao, L. Micale, S. Michaeli, C. Michiels, A. R. Migliaccio, A. S. Mihailidou, D. Mijaljica, K. Mikoshiba, E. Milan, L. Miller-Fleming, G. B. Mills, I. G. Mills, G. Minakaki, B. A. Minassian, X. - F. Ming, F. Minibayeva, E. A. Minina, J. D. Mintern, S. Minucci, A. Miranda-Vizuete, C. H. Mitchell, S. Miyamoto, K. Miyazawa, N. Mizushima, K. Mnich, B. Mograbi, S. Mohseni, L. F. Moita, M. Molinari, M. Molinari, A. B. Møller, B. Mollereau, F. Mollinedo, M. Mongillo, M. M. Monick, S. Montagnaro, C. Montell, D. J. Moore, M. N. Moore, R. Mora-Rodriguez, P. I. Moreira, E. Morel, M. B. Morelli, S. Moreno, M. J. Morgan, A. Moris, Y. Moriyasu, J. L. Morrison, L. A. Morrison, E. Morselli, J. Moscat, P. L. Moseley, S. Mostowy, E. Motori, D. Mottet, J. C. Mottram, C. E. - H. Moussa, V. E. Mpakou, H. Mukhtar, J. M. Mulcahy Levy, S. Muller, R. Muñoz-Moreno, C. Muñoz-Pinedo, C. Münz, M. E. Murphy, J. T. Murray, A. Murthy, I. U. Mysorekar, I. R. Nabi, M. Nabissi, G. A. Nader, Y. Nagahara, Y. Nagai, K. Nagata, A. Nagelkerke, P. Nagy, S. R. Naidu, S. Nair, H. Nakano, H. Nakatogawa, M. Nanjundan, G. Napolitano, N. I. Naqvi, R. Nardacci, D. P. Narendra, M. Narita, A. C. Nascimbeni, R. Natarajan, L. C. Navegantes, S. T. Nawrocki, T. Y. Nazarko, V. Y. Nazarko, T. Neill, L. M. Neri, M. G. Netea, R. T. Netea-Maier, B. M. Neves, P. A. Ney, I. P. Nezis, H. T. Nguyen, H. P. Nguyen, A. - S. Nicot, H. Nilsen, P. Nilsson, M. Nishimura, I. Nishino, M. Niso-Santano, H. Niu, R. A. Nixon, V. C. Njar, T. Noda, A. A. Noegel, E. M. Nolte, E. Norberg, K. K. Norga, S. K. Noureini, S. Notomi, L. Notterpek, K. Nowikovsky, N. Nukina, T. Nürnberger, V. B. O'Donnell, T. O'Donovan, P. J. O'Dwyer, I. Oehme, C. L. Oeste, M. Ogawa, B. Ogretmen, Y. Ogura, Y. J. Oh, M. Ohmuraya, T. Ohshima, R. Ojha, K. Okamoto, T. Okazaki, F. J. Oliver, K. Ollinger, S. Olsson, D. P. Orban, P. Ordonez, I. Orhon, L. Orosz, E. J. O'Rourke, H. Orozco, A. L. Ortega, E. Ortona, L. D. Osellame, J. Oshima, S. Oshima, H. D. Osiewacz, T. Otomo, K. Otsu, J. - H. J. Ou, T. F. Outeiro, D. - Y. Ouyang, H. Ouyang, M. Overholtzer, M. A. Ozbun, P. H. Ozdinler, B. Ozpolat, C. Pacelli, P. Paganetti, G. Page, G. Pages, U. Pagnini, B. Pajak, S. C. Pak, K. Pakos-Zebrucka, N. Pakpour, Z. Palková, F. Palladino, K. Pallauf, N. Pallet, M. Palmieri, S. R. Paludan, C. Palumbo, S. Palumbo, O. Pampliega, H. Pan, W. Pan, T. Panaretakis, A. Pandey, A. Pantazopoulou, Z. Papackova, D. L. Papademetrio, I. Papassideri, A. Papini, N. Parajuli, J. Pardo, V. V. Parekh, G. Parenti, J. - I. Park, J. Park, O. K. Park, R. Parker, R. Parlato, J. B. Parys, K. R. Parzych, J. - M. Pasquet, B. Pasquier, K. B. Pasumarthi, D. Patschan, C. Patterson, S. Pattingre, S. Pattison, A. Pause, H. Pavenstädt, F. Pavone, Z. Pedrozo, F. J. Peña, M. A. Peñalva, M. Pende, J. Peng, F. Penna, J. M. Penninger, A. Pensalfini, S. Pepe, G. J. Pereira, P. C. Pereira, V. Pérez-de la Cruz, M. E. Pérez-Pérez, D. Pérez-Rodríguez, D. Pérez-Sala, C. Perier, A. Perl, D. H. Perlmutter, I. Perrotta, S. Pervaiz, M. Pesonen, J. E. Pessin, G. J. Peters, M. Petersen, I. Petrache, B. J. Petrof, G. Petrovski, J. M. Phang, M. Piacentini, M. Pierdominici, P. Pierre, V. Pierrefite-Carle, F. Pietrocola, F. X. Pimentel-Muiños, M. Pinar, B. Pineda, R. Pinkas-Kramarski, M. Pinti, P. Pinton, B. Piperdi, J. M. Piret, L. C. Platanias, H. W. Platta, E. D. Plowey, S. Pöggeler, M. Poirot, P. Polčic, A. Poletti, A. H. Poon, H. Popelka, B. Popova, I. Poprawa, S. M. Poulose, J. Poulton, S. K. Powers, T. Powers, M. Pozuelo-Rubio, K. Prak, R. Prange, M. Prescott, M. Priault, S. Prince, R. L. Proia, T. Proikas-Cezanne, H. Prokisch, V. J. Promponas, K. Przyklenk, R. Puertollano, S. Pugazhenthi, L. Puglielli, A. Pujol, J. Puyal, D. Pyeon, X. Qi, W. - B. Qian, Z. - H. Qin, Y. Qiu, Z. Qu, J. Quadrilatero, F. Quinn, N. Raben, H. Rabinowich, F. Radogna, M. J. Ragusa, M. Rahmani, K. Raina, S. Ramanadham, R. Ramesh, A. Rami, S. Randall-Demllo, F. Randow, H. Rao, V. A. Rao, B. B. Rasmussen, T. M. Rasse, E. A. Ratovitski, P. - E. Rautou, S. K. Ray, B. Razani, B. H. Reed, F. Reggiori, M. Rehm, A. S. Reichert, T. Rein, D. J. Reiner, E. Reits, J. Ren, X. Ren, M. Renna, J. E. Reusch, J. L. Revuelta, L. Reyes, A. R. Rezaie, R. I. Richards, D. R. Richardson, C. Richetta, M. A. Riehle, B. H. Rihn, Y. Rikihisa, B. E. Riley, G. Rimbach, M. R. Rippo, K. Ritis, F. Rizzi, E. Rizzo, P. J. Roach, J. Robbins, M. Roberge, G. Roca, M. C. Roccheri, S. Rocha, C. M. Rodrigues, C. I. Rodríguez, S. R. de Cordoba, N. Rodriguez-Muela, J. Roelofs, V. V. Rogov, T. T. Rohn, B. Rohrer, D. Romanelli, L. Romani, P. S. Romano, M. I. G. Roncero, J. L. Rosa, A. Rosello, K. V. Rosen, P. Rosenstiel, M. Rost-Roszkowska, K. A. Roth, G. Roué, M. Rouis, K. M. Rouschop, D. T. Ruan, D. Ruano, D. C. Rubinsztein, E. B. Rucker, A. Rudich, E. Rudolf, R. Rudolf, M. A. Ruegg, C. Ruiz-Roldan, A. A. Ruparelia, P. Rusmini, D. W. Russ, G. L. Russo, G. Russo, R. Russo, T. E. Rusten, V. Ryabovol, K. M. Ryan, S. W. Ryter, D. M. Sabatini, M. Sacher, C. Sachse, M. N. Sack, J. Sadoshima, P. Saftig, R. Sagi-Eisenberg, S. Sahni, P. Saikumar, T. Saito, T. Saitoh, K. Sakakura, M. Sakoh-Nakatogawa, Y. Sakuraba, M. Salazar-Roa, P. Salomoni, A. K. Saluja, P. M. Salvaterra, R. Salvioli, A. Samali, A. M. Sanchez, J. A. Sánchez-Alcázar, R. Sanchez-Prieto, M. Sandri, M. A. Sanjuan, S. Santaguida, L. Santambrogio, G. Santoni, C. N. Dos Santos, S. Saran, M. Sardiello, G. Sargent, P. Sarkar, S. Sarkar, M. R. Sarrias, M. M. Sarwal, C. Sasakawa, M. Sasaki, M. Sass, K. Sato, M. Sato, J. Satriano, N. Savaraj, S. Saveljeva, L. Schaefer, U. E. Schaible, M. Scharl, H. M. Schatzl, R. Schekman, W. Scheper, A. Schiavi, H. M. Schipper, H. Schmeisser, J. Schmidt, I. Schmitz, B. E. Schneider, E. M. Schneider, J. L. Schneider, E. A. Schon, M. J. Schönenberger, A. H. Schönthal, D. F. Schorderet, B. Schröder, S. Schuck, R. J. Schulze, M. Schwarten, T. L. Schwarz, S. Sciarretta, K. Scotto, A. I. Scovassi, R. A. Screaton, M. Screen, H. Seca, S. Sedej, L. Segatori, N. Segev, P. O. Seglen, J. M. Seguí-Simarro, J. Segura-Aguilar, E. Seki, C. Sell, I. Seiliez, C. F. Semenkovich, G. L. Semenza, U. Sen, A. L. Serra, A. Serrano-Puebla, H. Sesaki, T. Setoguchi, C. Settembre, J. J. Shacka, A. N. Shajahan-Haq, I. M. Shapiro, S. Sharma, H. She, C. - K. J. Shen, C. - C. Shen, H. - M. Shen, S. Shen, W. Shen, R. Sheng, X. Sheng, Z. - H. Sheng, T. G. Shepherd, J. Shi, Q. Shi, Q. Shi, Y. Shi, S. Shibutani, K. Shibuya, Y. Shidoji, J. - J. Shieh, C. - M. Shih, Y. Shimada, S. Shimizu, D. W. Shin, M. L. Shinohara, M. Shintani, T. Shintani, T. Shioi, K. Shirabe, R. Shiri-Sverdlov, O. Shirihai, G. C. Shore, C. - W. Shu, D. Shukla, A. A. Sibirny, V. Sica, C. J. Sigurdson, E. M. Sigurdsson, P. S. Sijwali, B. Sikorska, W. A. Silveira, S. Silvente-Poirot, G. A. Silverman, J. Simak, T. Simmet, A. K. Simon, H. - U. Simon, C. Simone, M. Simons, A. Simonsen, R. Singh, S. V. Singh, S. K. Singh, D. Sinha, S. Sinha, F. A. Sinicrope, A. Sirko, K. Sirohi, B. J. Sishi, A. Sittler, P. M. Siu, E. Sivridis, A. Skwarska, R. Slack, I. Slaninová, N. Slavov, S. S. Smaili, K. S. Smalley, D. R. Smith, S. J. Soenen, S. A. Soleimanpour, A. Solhaug, K. Somasundaram, J. H. Son, A. Sonawane, C. Song, F. Song, H. K. Song, J. - X. Song, W. Song, K. Y. Soo, A. K. Sood, T. W. Soong, V. Soontornniyomkij, M. Sorice, F. Sotgia, D. R. Soto-Pantoja, A. Sotthibundhu, M. J. Sousa, H. P. Spaink, P. N. Span, A. Spang, J. D. Sparks, P. G. Speck, S. A. Spector, C. D. Spies, W. Springer, D. S. Clair, A. Stacchiotti, B. Staels, M. T. Stang, D. T. Starczynowski, P. Starokadomskyy, C. Steegborn, J. W. Steele, L. Stefanis, J. Steffan, C. M. Stellrecht, H. Stenmark, T. M. Stepkowski, S. T. Stern, C. Stevens, B. R. Stockwell, V. Stoka, Z. Storchova, B. Stork, V. Stratoulias, D. J. Stravopodis, P. Strnad, A. M. Strohecker, A. - L. Ström, P. Stromhaug, J. Stulik, Y. - X. Su, Z. Su, C. S. Subauste, S. Subramaniam, C. M. Sue, S. W. Suh, X. Sui, S. Sukseree, D. Sulzer, F. - L. Sun, J. Sun, J. Sun, S. - Y. Sun, Y. Sun, Y. Sun, Y. Sun, V. Sundaramoorthy, J. Sung, H. Suzuki, K. Suzuki, N. Suzuki, T. Suzuki, Y. J. Suzuki, M. S. Swanson, C. Swanton, K. Swärd, G. Swarup, S. T. Sweeney, P. W. Sylvester, Z. Szatmari, E. Szegezdi, P. W. Szlosarek, H. Taegtmeyer, M. Tafani, E. Taillebourg, S. W. Tait, K. Takacs-Vellai, Y. Takahashi, S. Takáts, G. Takemura, N. Takigawa, N. J. Talbot, E. Tamagno, J. Tamburini, C. - P. Tan, L. Tan, M. L. Tan, M. Tan, Y. - J. Tan, K. Tanaka, M. Tanaka, D. Tang, D. Tang, G. Tang, I. Tanida, K. Tanji, B. A. Tannous, J. A. Tapia, I. Tasset-Cuevas, M. Tatar, I. Tavassoly, N. Tavernarakis, A. Taylor, G. S. Taylor, G. A. Taylor, J. P. Taylor, M. J. Taylor, E. V. Tchetina, A. R. Tee, F. Teixeira-Clerc, S. Telang, T. Tencomnao, B. - B. Teng, R. - J. Teng, F. Terro, G. Tettamanti, A. L. Theiss, A. E. Theron, K. J. Thomas, M. P. Thomé, P. G. Thomes, A. Thorburn, J. Thorner, T. Thum, M. Thumm, T. L. Thurston, L. Tian, A. Till, J. P. - Y. Ting, V. I. Titorenko, L. Toker, S. Toldo, S. A. Tooze, I. Topisirovic, M. L. Torgersen, L. Torosantucci, A. Torriglia, M. R. Torrisi, C. Tournier, R. Towns, V. Trajkovic, L. H. Travassos, G. Triola, D. N. Tripathi, D. Trisciuoglio, R. Troncoso, I. P. Trougakos, A. C. Truttmann, K. - J. Tsai, M. P. Tschan, Y. - H. Tseng, T. Tsukuba, A. Tsung, A. S. Tsvetkov, S. Tu, H. - Y. Tuan, M. Tucci, D. A. Tumbarello, B. Turk, V. Turk, R. F. Turner, A. A. Tveita, S. C. Tyagi, M. Ubukata, Y. Uchiyama, A. Udelnow, T. Ueno, M. Umekawa, R. Umemiya-Shirafuji, B. R. Underwood, C. Ungermann, R. P. Ureshino, R. Ushioda, V. N. Uversky, N. L. Uzcátegui, T. Vaccari, M. I. Vaccaro, L. Váchová, H. Vakifahmetoglu-Norberg, R. Valdor, E. M. Valente, F. Vallette, A. M. Valverde, G. Van den Berghe, L. Van Den Bosch, G. R. van den Brink, F. G. van der Goot, I. J. van der Klei, L. J. van der Laan, W. G. van Doorn, M. van Egmond, K. L. van Golen, L. Van Kaer, M. van Lookeren Campagne, P. Vandenabeele, W. Vandenberghe, I. Vanhorebeek, I. Varela-Nieto, M. H. Vasconcelos, R. Vasko, D. G. Vavvas, I. Vega-Naredo, G. Velasco, A. D. Velentzas, P. D. Velentzas, T. Vellai, E. Vellenga, M. H. Vendelbo, K. Venkatachalam, N. Ventura, S. Ventura, P. S. Veras, M. Verdier, B. G. Vertessy, A. Viale, M. Vidal, H. L. A. Vieira, R. D. Vierstra, N. Vigneswaran, N. Vij, M. Vila, M. Villar, V. H. Villar, J. Villarroya, C. Vindis, G. Viola, M. T. Viscomi, G. Vitale, D. T. Vogl, O. V. Voitsekhovskaja, C. von Haefen, K. von Schwarzenberg, D. E. Voth, V. Vouret-Craviari, K. Vuori, J. M. Vyas, C. Waeber, C. L. Walker, M. J. Walker, J. Walter, L. Wan, X. Wan, B. Wang, C. Wang, C. - Y. Wang, C. Wang, C. Wang, C. Wang, D. Wang, F. Wang, F. Wang, G. Wang, H. - J. Wang, H. Wang, H. - G. Wang, H. Wang, H. - D. Wang, J. Wang, J. Wang, M. Wang, M. - Q. Wang, P. - Y. Wang, P. Wang, R. C. Wang, S. Wang, T. - F. Wang, X. Wang, X. - J. Wang, X. - W. Wang, X. Wang, X. Wang, Y. Wang, Y. Wang, Y. Wang, Y. - J. Wang, Y. Wang, Y. Wang, Y. T. Wang, Y. Wang, Z. - N. Wang, P. Wappner, C. Ward, D. M. V. Ward, G. Warnes, H. Watada, Y. Watanabe, K. Watase, T. E. Weaver, C. D. Weekes, J. Wei, T. Weide, C. C. Weihl, G. Weindl, S. N. Weis, L. Wen, X. Wen, Y. Wen, B. Westermann, C. M. Weyand, A. R. White, E. White, J. L. Whitton, A. J. Whitworth, J. Wiels, F. Wild, M. E. Wildenberg, T. Wileman, D. S. Wilkinson, S. Wilkinson, D. Willbold, C. Williams, K. Williams, P. R. Williamson, K. F. Winklhofer, S. S. Witkin, S. E. Wohlgemuth, T. Wollert, E. J. Wolvetang, E. Wong, G. W. Wong, R. W. Wong, V. K. W. Wong, E. A. Woodcock, K. L. Wright, C. Wu, D. Wu, G. S. Wu, J. Wu, J. Wu, M. Wu, M. Wu, S. Wu, W. K. Wu, Y. Wu, Z. Wu, C. P. Xavier, R. J. Xavier, G. - X. Xia, T. Xia, W. Xia, Y. Xia, H. Xiao, J. Xiao, S. Xiao, W. Xiao, C. - M. Xie, Z. Xie, Z. Xie, M. Xilouri, Y. Xiong, C. Xu, C. Xu, F. Xu, H. Xu, H. Xu, J. Xu, J. Xu, J. Xu, L. Xu, X. Xu, Y. Xu, Y. Xu, Z. - X. Xu, Z. Xu, Y. Xue, T. Yamada, A. Yamamoto, K. Yamanaka, S. Yamashina, S. Yamashiro, B. Yan, B. Yan, X. Yan, Z. Yan, Y. Yanagi, D. - S. Yang, J. - M. Yang, L. Yang, M. Yang, P. - M. Yang, P. Yang, Q. Yang, W. Yang, W. Y. Yang, X. Yang, Y. Yang, Y. Yang, Z. Yang, Z. Yang, M. - C. Yao, P. J. Yao, X. Yao, Z. Yao, Z. Yao, L. S. Yasui, M. Ye, B. Yedvobnick, B. Yeganeh, E. S. Yeh, P. L. Yeyati, F. Yi, L. Yi, X. - M. Yin, C. K. Yip, Y. - M. Yoo, Y. H. Yoo, S. - Y. Yoon, K. - I. Yoshida, T. Yoshimori, K. H. Young, H. Yu, J. J. Yu, J. - T. Yu, J. Yu, L. Yu, W. H. Yu, X. - F. Yu, Z. Yu, J. Yuan, Z. - M. Yuan, B. Y. Yue, J. Yue, Z. Yue, D. N. Zacks, E. Zacksenhaus, N. Zaffaroni, T. Zaglia, Z. Zakeri, V. Zecchini, J. Zeng, M. Zeng, Q. Zeng, A. S. Zervos, D. D. Zhang, F. Zhang, G. Zhang, G. - C. Zhang, H. Zhang, H. Zhang, H. Zhang, H. Zhang, J. Zhang, J. Zhang, J. Zhang, J. Zhang, J. - P. Zhang, L. Zhang, L. Zhang, L. Zhang, L. Zhang, M. - Y. Zhang, X. Zhang, X. D. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, Y. Zhang, M. Zhao, W. - L. Zhao, X. Zhao, Y. G. Zhao, Y. Zhao, Y. Zhao, Y. - X. Zhao, Z. Zhao, Z. J. Zhao, D. Zheng, X. - L. Zheng, X. Zheng, B. Zhivotovsky, Q. Zhong, G. - Z. Zhou, G. Zhou, H. Zhou, S. - F. Zhou, X. - J. Zhou, H. Zhu, H. Zhu, W. - G. Zhu, W. Zhu, X. - F. Zhu, Y. Zhu, S. - M. Zhuang, X. Zhuang, E. Ziparo, C. E. Zois, T. Zoladek, W. - X. Zong, A. Zorzano, et S. M. Zughaier, « Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) », Autophagy, vol. 12, nᵒ 1, p. 1-222, 2016.
    Mots-clés : Animals, autolysosome, autophagosome, Autophagy, BIOCELL, Biological Assay, chaperone-mediated autophagy, Computer Simulation, flux, Humans, LC3, lysosome, macroautophagy, OTOFAG, phagophore, stress, vacuole.

  • A. Lalève, C. Vallières, M. - P. Golinelli-Cohen, C. Bouton, Z. Song, G. Pawlik, S. M. Tindall, S. V. Avery, J. Clain, et B. Meunier, « The antimalarial drug primaquine targets Fe–S cluster proteins and yeast respiratory growth », Redox Biology, vol. 7, p. 21-29, 2016.
    Mots-clés : Aconitase, Aconitate Hydratase, Antimalarials, ATP-Binding Cassette Transporters, BIOCELL, BIOMIT, Cytochrome-B(5) Reductase, Gene Expression Regulation, Fungal, Gene Knockout Techniques, Malaria, Mitochondria, Molecular Chaperones, oxidative stress, Primaquine, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sod2, Superoxide Dismutase, Yeast model.

  • C. Lefebvre, C. Largeau, X. Michelet, C. Fourrage, X. Maniere, I. Matic, R. Legouis, et E. Culetto, « The ESCRT-II proteins are involved in shaping the sarcoplasmic reticulum in C. elegans », Journal of Cell Science, vol. 129, nᵒ 7, p. 1490-1499, avr. 2016.

  • M. Malartre, « Regulatory mechanisms of EGFR signalling during Drosophila eye development », Cellular and Molecular Life Sciences, vol. 73, nᵒ 9, p. 1825-1843, 2016.
    Mots-clés : Activators, Animals, BIOCELL, Cell Cycle Checkpoints, Combinatorial signalling, Drosophila, Drosophila Proteins, EGFR, Endoplasmic Reticulum, Eye, Inhibitors, Ommatidia, Photoreceptors, Receptor, Epidermal Growth Factor, Retina, SIGDEV, Signal Transduction, Transcription Factors.

  • M. M. Marquès-Bueno, A. K. Morao, A. Cayrel, M. P. Platre, M. Barberon, E. Caillieux, V. Colot, Y. Jaillais, F. Roudier, et G. Vert, « A versatile Multisite Gateway-compatible promoter and transgenic line collection for cell type-specific functional genomics in Arabidopsis », The Plant Journal, vol. 85, nᵒ 2, p. 320-333, 2016.
    Mots-clés : Arabidopsis, Arabidopsis Proteins, BIOCELL, BREAK lines, Gene Expression Regulation, Plant, Genomics, INTACT, LINE UP lines, Plants, Genetically Modified, Promoter Regions, Genetic, RED TIDE lines, SAND lines, UBINET.

  • C. J. Merrifield, « Erratum: Actin puts the squeeze on Drosophila glue secretion », Nature Cell Biology, vol. 18, nᵒ 3, p. 347-347, févr. 2016.

  • C. J. Merrifield, « Actin puts the squeeze on Drosophila glue secretion », Nature Cell Biology, vol. 18, nᵒ 2, p. 142-144, janv. 2016.
    Mots-clés : Actomyosin, Animals, BIOCELL, Carrier Proteins, Drosophila melanogaster, Drosophila Proteins, ENDEXO, Exocytosis, Glue Proteins, Drosophila, Membrane Proteins, Salivary Glands, Secretory Vesicles.

  • J. Montagne, « A Wacky Bridge to mTORC1 Dimerization », Developmental Cell, vol. 36, nᵒ 2, p. 129-130, 2016.
    Mots-clés : Animals, BIOCELL, Carrier Proteins, DNA Helicases, Drosophila melanogaster, Drosophila Proteins, METABO, TOR Serine-Threonine Kinases.

  • C. T. Nguyen, A. Agorio, M. Jossier, S. Depré, S. Thomine, et S. Filleur, « Characterization of the Chloride Channel-Like, AtCLCg, Involved in Chloride Tolerance in Arabidopsis thaliana », Plant and Cell Physiology, vol. 57, nᵒ 4, p. 764-775, 2016.
    Mots-clés : Arabidopsis, Arabidopsis Proteins, Arabidopsis thaliana, BIOCELL, Chloride channel (CLC), Chloride Channels, Mesophyll Cells, MINION, NaCl stress, Osmotic Pressure, Salt-Tolerance, Sodium Chloride, Stress, Physiological, Vacuolar membrane.

  • J. Ostojić, C. Panozzo, A. Bourand-Plantefol, C. J. Herbert, G. Dujardin, et N. Bonnefoy, « Ribosome recycling defects modify the balance between the synthesis and assembly of specific subunits of the oxidative phosphorylation complexes in yeast mitochondria », Nucleic Acids Research, vol. 44, nᵒ 12, p. 5785-5797, juill. 2016.

  • L. Pitayu, E. Baruffini, C. Rodier, A. Rötig, T. Lodi, et A. Delahodde, « Combined use of Saccharomyces cerevisiae, Caenorhabditis elegans and patient fibroblasts leads to the identification of clofilium tosylate as a potential therapeutic chemical against POLG-related diseases », Human Molecular Genetics, vol. 25, nᵒ 4, p. 715-727, 2016.
    Résumé : Mitochondria are organelles that have their own DNA (mitochondrial DNA, mtDNA) whose maintenance is necessary for the majority of ATP production in eukaryotic cells. Defects in mtDNA maintenance or integrity are responsible for numerous diseases. The DNA polymerase γ (POLG) ensures proper mtDNA replication and repair. Mutations in POLG are a major cause of mitochondrial disorders including hepatic insufficiency, Alpers syndrome, progressive external ophthalmoplegia, sensory neuropathy and ataxia. Mutations in POLG are also associated with parkinsonism. To date, no effective therapy is available. Based on the conservation of mitochondrial function from yeast to human, we used Saccharomyces cerevisiae and Caenorhabditis elegans as first pass filters to identify a chemical that suppresses mtDNA instability in cultured fibroblasts of a POLG-deficient patient. We showed that this unsuspected compound, clofilium tosylate (CLO), belonging to a class of anti-arrhythmic agents, prevents mtDNA loss of all yeast mitochondrial polymerase mutants tested, improves behavior and mtDNA content of polg-1-deficient worms and increases mtDNA content of quiescent POLG-deficient fibroblasts. Furthermore, the mode of action of the drug seems conserved as CLO increases POLG steady-state level in yeast and human cells. Two other anti-arrhythmic agents (FDA-approved) sharing common pharmacological properties and chemical structure also show potential benefit for POLG deficiency in C. elegans. Our findings provide evidence of the first mtDNA-stabilizing compound that may be an effective pharmacological alternative for the treatment of POLG-related diseases.
    Mots-clés : Animals, BIOCELL, Caenorhabditis elegans, DNA Polymerase I, DNA Replication, DNA, Mitochondrial, DNA-Directed DNA Polymerase, FDMITO, Fibroblasts, Humans, Mitochondrial Diseases, Mutation, Phenotype, Primary Cell Culture, Quaternary Ammonium Compounds, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins.

  • C. H. Sellem, J. - P. di Rago, J. - P. Lasserre, S. H. Ackerman, et A. Sainsard-Chanet, « Regulation of Aerobic Energy Metabolism in Podospora anserina by Two Paralogous Genes Encoding Structurally Different c-Subunits of ATP Synthase », PLOS Genetics, vol. 12, nᵒ 7, p. e1006161, juill. 2016.
    Mots-clés : BIOCELL, DBG, DSMC, FDMITO.

  • Z. Song, A. Laleve, C. Vallières, J. E. McGeehan, R. E. Lloyd, et B. Meunier, « Human Mitochondrial Cytochrome b Variants Studied in Yeast: Not All Are Silent Polymorphisms », Human Mutation, vol. 37, nᵒ 9, p. 933-941, 2016.
    Résumé : Variations in mitochondrial DNA (mtDNA) cytochrome b (mt-cyb) are frequently found within the healthy population, but also occur within a spectrum of mitochondrial and common diseases. mt-cyb encodes the core subunit (MT-CYB) of complex III, a central component of the oxidative phosphorylation system that drives cellular energy production and homeostasis. Despite significant efforts, most mt-cyb variations identified are not matched with corresponding biochemical data, so their functional and pathogenic consequences in humans remain elusive. While human mtDNA is recalcitrant to genetic manipulation, it is possible to introduce human-associated point mutations into yeast mtDNA. Using this system, we reveal direct links between human mt-cyb variations in key catalytic domains of MT-CYB and significant changes to complex III activity or drug sensitivity. Strikingly, m.15257G>A (p.Asp171Asn) increased the sensitivity of yeast to the antimalarial drug atovaquone, and m.14798T>C (p.Phe18Leu) enhanced the sensitivity of yeast to the antidepressant drug clomipramine. We demonstrate that while a small number of mt-cyb variations had no functional effect, others have the capacity to alter complex III properties, suggesting they could play a wider role in human health and disease than previously thought. This compendium of new mt-cyb-biochemical relationships in yeast provides a resource for future investigations in humans.
    Mots-clés : Atovaquone, BIOCELL, BIOMIT, clomipramine, mitochondrial DNA, MT-CYB, Yeast model.

  • M. B. Toledano et B. HUANG, « Microbial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological Roles », Molecules and Cells, vol. 39, nᵒ 1, p. 31-39, janv. 2016.
    Mots-clés : bacteria, Bacterial Proteins, BIOCELL, Catalysis, chaperone, Free Radical Scavengers, Fungal Proteins, H2O2 scavenging, H2O2 signaling, Hydrogen Peroxide, Molecular Chaperones, Mutation, Peroxiredoxins, Signal Transduction, SOC, Yeasts.

  • M. Wild, J. - M. Davière, T. Regnault, L. Sakvarelidze-Achard, E. Carrera, I. Lopez Diaz, A. Cayrel, G. Dubeaux, G. Vert, et P. Achard, « Tissue-Specific Regulation of Gibberellin Signaling Fine-Tunes Arabidopsis Iron-Deficiency Responses », Developmental Cell, vol. 37, nᵒ 2, p. 190-200, 2016.
    Mots-clés : Arabidopsis, Arabidopsis Proteins, Arabidopsis thaliana, Basic Helix-Loop-Helix Transcription Factors, BIOCELL, DELLA, FIT, Gene Expression Regulation, Plant, Gibberellins, Iron, iron deficiency, Plant Growth Regulators, Plant Roots, root epidermis, UBINET.

  • Z. Yi, M. Manil-Ségalen, L. Sago, A. Glatigny, V. Redeker, R. Legouis, et M. - H. Mucchielli-Giorgi, « SAFER, an Analysis Method of Quantitative Proteomic Data, Reveals New Interactors of the C. elegans Autophagic Protein LGG-1 », Journal of Proteome Research, vol. 15, nᵒ 5, p. 1515-1523, 2016.
    Résumé : Affinity purifications followed by mass spectrometric analysis are used to identify protein-protein interactions. Because quantitative proteomic data are noisy, it is necessary to develop statistical methods to eliminate false-positives and identify true partners. We present here a novel approach for filtering false interactors, named "SAFER" for mass Spectrometry data Analysis by Filtering of Experimental Replicates, which is based on the reproducibility of the replicates and the fold-change of the protein intensities between bait and control. To identify regulators or targets of autophagy, we characterized the interactors of LGG1, a ubiquitin-like protein involved in autophagosome formation in C. elegans. LGG-1 partners were purified by affinity, analyzed by nanoLC-MS/MS mass spectrometry, and quantified by a label-free proteomic approach based on the mass spectrometric signal intensity of peptide precursor ions. Because the selection of confident interactions depends on the method used for statistical analysis, we compared SAFER with several statistical tests and different scoring algorithms on this set of data. We show that SAFER recovers high-confidence interactors that have been ignored by the other methods and identified new candidates involved in the autophagy process. We further validated our method on a public data set and conclude that SAFER notably improves the identification of protein interactors.
    Mots-clés : atg-8/LC3, Autophagy, BIM, BIOCELL, C. elegans, DBG, label free mass spectrometry, OTOFAG, PF, proteomics, SICAPS, statistical methodology.


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