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Accueil > Publications

Publications Départements Biologie Cellulaire

2017



  • 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.


  • 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.


  • 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.


  • 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.


  • 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.

2016



  • 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. 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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. 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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. 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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, « 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.


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


  • 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.

2015



  • A. Aubusson-Fleury, J. Cohen, et M. Lemullois, « Ciliary heterogeneity within a single cell: The Paramecium model », in Methods in Cell Biology, vol. 127, Elsevier, 2015, p. 457-485.


  • A. Aznar, N. W. G. Chen, S. Thomine, et A. Dellagi, « Immunity to plant pathogens and iron homeostasis », Plant Science, vol. 240, p. 90-97, 2015.
    Mots-clés : BIOCELL, Homeostasis, Iron, MINION, Pathogen, Phenolics, plant defense, Plant Diseases, Plant Immunity, Reactive Oxygen Species, Siderophores.


  • C. Berrier, R. Peyronnet, J. - M. Betton, G. Ephritikhine, H. Barbier-Brygoo, J. - M. Frachisse, et A. Ghazi, « Channel characteristics of VDAC-3 from Arabidopsis thaliana », Biochemical and Biophysical Research Communications, vol. 459, nᵒ 1, p. 24-28, 2015.
    Mots-clés : Arabidopsis, Arabidopsis Proteins, BIOCELL, Cell-free synthesis, Cell-Free System, Channel, Electrophysiological Phenomena, Escherichia coli, Lipid Bilayers, MINION, Protein Engineering, Recombinant Proteins, VDAC, Voltage-Dependent Anion Channels.

  • S. Boukhenouna, H. Mazon, G. Branlant, C. Jacob, M. B. Toledano, et S. Rahuel-Clermont, « Evidence that glutathione and the glutathione system efficiently recycle 1-cys sulfiredoxin in vivo », Antioxidants & Redox Signaling, vol. 22, nᵒ 9, p. 731-743, 2015.
    Résumé : AIMS: Typical 2-Cys peroxiredoxins (2-Cys Prxs) are Cys peroxidases that undergo inactivation by hyperoxidation of the catalytic Cys, a modification reversed by ATP-dependent reduction by sulfiredoxin (Srx). Such an attribute is thought to provide regulation of 2-Cys Prxs functions. The initial steps of the Srx catalytic mechanism lead to a Prx/Srx thiolsulfinate intermediate that must be reduced to regenerate Srx. In Saccharomyces cerevisiae Srx, the thiolsulfinate is resolved by an extra Cys (Cys48) that is absent in mammalian, plant, and cyanobacteria Srxs (1-Cys Srxs). We have addressed the mechanism of reduction of 1-Cys Srxs using S. cerevisiae Srx mutants lacking Cys48 as a model. RESULTS: We have tested the recycling of Srx by glutathione (GSH) by a combination of in vitro steady-state and single-turnover kinetic analyses, using enzymatic coupled assays, Prx fluorescence, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and reverse-phase chromatography coupled to mass spectrometry. We demonstrate that GSH reacts directly with the thiolsulfinate intermediate, by following saturation kinetics with an apparent dissociation constant of 34 μM, while producing S-glutathionylated Srx as a catalytic intermediate which is efficiently reduced by the glutaredoxin/glutathione reductase system. Total cellular depletion of GSH impacted the recycling of Srx, confirming in vivo that GSH is the physiologic reducer of 1-Cys Srx. INNOVATION: Our study suggests that GSH binds to the thiolsulfinate complex, thus allowing non-rate limiting reduction. Such a structural recognition of GSH enables an efficient catalytic reduction, even at very low GSH cellular levels. CONCLUSION: This study provides both in vitro and in vivo evidence of the role of GSH as the primary reducer of 1-Cys Srxs.
    Mots-clés : BIOCELL, Glutathione, Oxidoreductases Acting on Sulfur Group Donors, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, SOC.


  • E. M. Bruch, S. Thomine, L. C. Tabares, et S. Un, « Variations in Mn(II) speciation among organisms: what makes D. radiodurans different. », Metallomics, vol. 7, nᵒ 1, p. 136-144, 2015.
    Mots-clés : B3S, BHFMR, BIOCELL, Deinococcus, Escherichia coli, Manganese, MINION, Nuclear Magnetic Resonance, Biomolecular, Nucleic Acids, Phosphates, Saccharomyces cerevisiae, Water.


  • E. M. Bruch, M. T. Warner, S. Thomine, L. C. Tabares, et S. Un, « Pulse Electron Double Resonance Detected Multinuclear NMR Spectra of Distant and Low Sensitivity Nuclei and Its Application to the Structure of Mn(II) Centers in Organisms », The Journal of Physical Chemistry B, vol. 119, nᵒ 43, p. 13515-13523, oct. 2015.
    Mots-clés : B3S, BHFMR, BIOCELL, Deinococcus, Electron Spin Resonance Spectroscopy, Escherichia coli, Manganese, MINION, Models, Molecular, Molecular Structure, Nuclear Magnetic Resonance, Biomolecular, Organometallic Compounds, Quantum Theory.


  • R. Cossard, M. Esposito, C. H. Sellem, L. Pitayu, C. Vasnier, A. Ã. ¨s Delahodde, et E. P. Dassa, « Caenorhabditis elegans expressing the Saccharomyces cerevisiae NADH alternative dehydrogenase Ndi1p, as a tool to identify new genes involved in complex I related diseases », Frontiers in Genetics, vol. 6, juin 2015.
    Mots-clés : BIOCELL, Caenorhabditis elegans, complex I, embryonic lethality, FDMITO, Ndi1p, RNAi screening.


  • A. Delaunay-Moisan et C. Appenzeller-Herzog, « The antioxidant machinery of the endoplasmic reticulum: Protection and signaling », Free Radical Biology and Medicine, vol. 83, p. 341-351, 2015.
    Mots-clés : Animals, Antioxidants, BIOCELL, Endoplasmic Reticulum, Ero1, Glutathione, H(2)O(2), Humans, Hydrogen Peroxide, NADPH oxidase, Oxidation-Reduction, Oxidative folding, PDI, Reactive Oxygen Species, Redox homeostasis, Redox signaling, Signal Transduction, SOC, UPR.


  • G. Dubeaux, E. Zelazny, et G. Vert, « Getting to the root of plant iron uptake and cell-cell transport: Polarity matters! », Communicative & Integrative Biology, vol. 8, nᵒ 3, p. e1038441, mai 2015.
    Mots-clés : BIOCELL, Endocytosis, Iron, metals, plant nutrition, polarity, UBINET.


  • D. Garrido, T. Rubin, M. Poidevin, B. Maroni, A. Le Rouzic, J. - P. Parvy, et J. Montagne, « Fatty Acid Synthase Cooperates with Glyoxalase 1 to Protect against Sugar Toxicity », PLOS Genetics, vol. 11, nᵒ 2, p. e1004995, févr. 2015.


  • X. Gaume, A. - M. Tassin, I. Ugrinova, F. Mongelard, K. Monier, et P. Bouvet, « Centrosomal nucleolin is required for microtubule network organization », Cell Cycle, vol. 14, nᵒ 6, p. 902-919, mars 2015.

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