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Accueil > Départements > Biochimie, Biophysique et Biologie Structurale > Christophe LE CLAINCHE & Louis RENAULT : Dynamique du cytosquelette et motilité

Publications de l’équipe


  • M. - F. Carlier et S. Shekhar, « Global treadmilling coordinates actin turnover and controls the size of actin networks », Nature Reviews Molecular Cell Biology, mars 2017.

  • G. Dimchev, A. Steffen, F. Kage, V. Dimchev, J. Pernier, M. - F. Carlier, et K. Rottner, « Efficiency of lamellipodia protrusion is determined by the extent of cytosolic actin assembly », Molecular Biology of the Cell, p. mbc.E16-05-0334, mars 2017.

  • F. Kage, M. Winterhoff, V. Dimchev, J. Mueller, T. Thalheim, A. Freise, S. Brühmann, J. Kollasser, J. Block, G. Dimchev, M. Geyer, H. - J. Schnittler, C. Brakebusch, T. E. B. Stradal, M. - F. Carlier, M. Sixt, J. Käs, J. Faix, et K. Rottner, « FMNL formins boost lamellipodial force generation », Nature Communications, vol. 8, p. 14832, mars 2017.

  • A. Le Dur, T. L. Laï, M. - G. Stinnakre, A. Laisné, N. Chenais, S. Rakotobe, B. Passet, F. Reine, S. Soulier, L. Herzog, G. Tilly, H. Rézaei, V. Béringue, J. - L. Vilotte, et H. Laude, « Divergent prion strain evolution driven by PrP(C) expression level in transgenic mice », Nature Communications, vol. 8, p. 14170, 2017.
    Résumé : Prions induce a fatal neurodegenerative disease in infected host brain based on the refolding and aggregation of the host-encoded prion protein PrP(C) into PrP(Sc). Structurally distinct PrP(Sc) conformers can give rise to multiple prion strains. Constrained interactions between PrP(C) and different PrP(Sc) strains can in turn lead to certain PrP(Sc) (sub)populations being selected for cross-species transmission, or even produce mutation-like events. By contrast, prion strains are generally conserved when transmitted within the same species, or to transgenic mice expressing homologous PrP(C). Here, we compare the strain properties of a representative sheep scrapie isolate transmitted to a panel of transgenic mouse lines expressing varying levels of homologous PrP(C). While breeding true in mice expressing PrP(C) at near physiological levels, scrapie prions evolve consistently towards different strain components in mice beyond a certain threshold of PrP(C) overexpression. Our results support the view that PrP(C) gene dosage can influence prion evolution on homotypic transmission.
    Mots-clés : ACTIN, B3S.

  • T. Motomura, M. Suga, R. Hienerwadel, A. Nakagawa, T. - L. Lai, W. Nitschke, T. Kuma, M. Sugiura, A. Boussac, et J. - R. Shen, « Crystal structure and redox properties of a novel cyanobacterial heme-protein with a His/Cys heme axial ligation and a per-arnt-sim (PAS)-like domain », The Journal of Biological Chemistry, 2017.
    Résumé : Photosystem II (PSII) catalyzes the light-induced water oxidation leading to the generation of dioxygen indispensable for sustaining aerobic life on Earth. The PSII reaction center is composed of D1 and D2 proteins encoded by the psbA and psbD genes, respectively. In cyanobacteria, different psbA genes are present in the genome. The thermophilic cyanobacterium Thermosynechococcus elongatus contains 3 psbA genes, psbA1, psbA2 and psbA3 and a new c-type heme protein, Tll0287, was found to be expressed in a strain expressing the psbA2 gene only, but the structure and function of Tll0287 are unknown. Here we solved the crystal structure of Tll0287 at a 2.0 Å resolution. The overall structure of Tll0287 was found to be similar to some kinases and sensor proteins with a per-arnt-sim (PAS)-like domain, rather than to other c-type cytochromes. The 5(th) and 6(th) axial ligands for the heme were Cys and His, instead of the His/Met or His/His ligand pairs observed for most of the c-type hemes. The redox potential, E1/2, of Tll0287 was -255 ± 20 mV versus normal hydrogen electrode at pH values above 7.5. Below this pH value, the E1/2 increased by ≈57 mV/pH unit at 15°C, suggesting the involvement of a protonatable group with a pKred = 7.2 ± 0.3. Possible functions of Tll0287 as a redox sensor under micro-aerobic conditions or a cytochrome subunit of an H2S-oxidising system, are discussed in view of the environmental conditions in which psbA2 is expressed as well as phylogenetic analysis, structural and sequence homologies.
    Mots-clés : ACTIN, B3S, cytochrome, D1 protein, Heme, His-Cys heme axial coordination, PAS domain, PAS-like domain, photosynthesis, Photosystem II, PS2, Tll0287, x-ray crystallography.

  • S. Shekhar et M. - F. Carlier, « Enhanced Depolymerization of Actin Filaments by ADF/Cofilin and Monomer Funneling by Capping Protein Cooperate to Accelerate Barbed-End Growth », Current biology: CB, 2017.
    Résumé : A living cell's ability to assemble actin filaments in intracellular motile processes is directly dependent on the availability of polymerizable actin monomers, which feed polarized filament growth [1, 2]. Continued generation of the monomer pool by filament disassembly is therefore crucial. Disassemblers like actin depolymerizing factor (ADF)/cofilin and filament cappers like capping protein (CP) are essential agonists of motility [3-8], but the exact molecular mechanisms by which they accelerate actin polymerization at the leading edge and filament turnover has been debated for over two decades [9-12]. Whereas filament fragmentation by ADF/cofilin has long been demonstrated by total internal reflection fluorescence (TIRF) [13, 14], filament depolymerization was only inferred from bulk solution assays [15]. Using microfluidics-assisted TIRF microscopy, we provide the first direct visual evidence of ADF's simultaneous severing and rapid depolymerization of individual filaments. Using a conceptually novel assay to directly visualize ADF's effect on a population of pre-assembled filaments, we demonstrate how ADF's enhanced pointed-end depolymerization causes an increase in polymerizable actin monomers, thus promoting faster barbed-end growth. We further reveal that ADF-enhanced depolymerization synergizes with CP's long-predicted "monomer funneling" [16] and leads to skyrocketing of filament growth rates, close to estimated lamellipodial rates. The "funneling model" hypothesized, on thermodynamic grounds, that at high enough extent of capping, the few non-capped filaments transiently grow much faster [15], an effect proposed to be very important for motility. We provide the first direct microscopic evidence of monomer funneling at the scale of individual filaments. These results significantly enhance our understanding of the turnover of cellular actin networks.
    Mots-clés : ACTIN, B3S, Capping protein.


  • J. V. G. Abella, C. Galloni, J. Pernier, D. J. Barry, S. Kjær, M. - F. Carlier, et M. Way, « Isoform diversity in the Arp2/3 complex determines actin filament dynamics », Nature Cell Biology, vol. 18, nᵒ 1, p. 76-86, 2016.
    Résumé : The Arp2/3 complex consists of seven evolutionarily conserved subunits (Arp2, Arp3 and ARPC1-5) and plays an essential role in generating branched actin filament networks during many different cellular processes. In mammals, however, the ARPC1 and ARPC5 subunits are each encoded by two isoforms that are 67% identical. This raises the possibility that Arp2/3 complexes with different properties may exist.  We found that Arp2/3 complexes containing ARPC1B and ARPC5L are significantly better at promoting actin assembly than those with ARPC1A and ARPC5, both in cells and in vitro. Branched actin networks induced by complexes containing ARPC1B or ARPC5L are also disassembled ∼2-fold slower than those formed by their counterparts. This difference reflects the ability of cortactin to stabilize ARPC1B- and ARPC5L- but not ARPC1A- and ARPC5-containing complexes against coronin-mediated disassembly. Our observations demonstrate that the Arp2/3 complex in higher eukaryotes is actually a family of complexes with different properties.
    Mots-clés : ACTIN, Actin Cytoskeleton, Actin-Related Protein 2, Actin-Related Protein 3, Angiopoietins, Animals, B3S, Cell Line, Cortactin, Humans, Mice, Microfilament Proteins, Protein Isoforms.

  • 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.

  • C. Deville, C. Girard-Blanc, N. Assrir, N. Nhiri, E. Jacquet, F. Bontems, L. Renault, S. Petres, et C. van Heijenoort, « Mutations in actin used for structural studies partially disrupt β-thymosin/WH2 domains interaction », FEBS Letters, vol. 590, nᵒ 20, p. 3690-3699, 2016.
    Mots-clés : ACTIN, B3S, NMR spectroscopy.

  • P. Montaville, S. Kühn, C. Compper, et M. - F. Carlier, « Role of the C-terminal Extension of Formin 2 in Its Activation by Spire Protein and Processive Assembly of Actin Filaments », The Journal of Biological Chemistry, vol. 291, nᵒ 7, p. 3302-3318, 2016.
    Résumé : Formin 2 (Fmn2), a member of the FMN family of formins, plays an important role in early development. This formin cooperates with profilin and Spire, a WASP homology domain 2 (WH2) repeat protein, to stimulate assembly of a dynamic cytoplasmic actin meshwork that facilitates translocation of the meiotic spindle in asymmetric division of mouse oocytes. The kinase-like non-catalytic domain (KIND) of Spire directly interacts with the C-terminal extension of the formin homology domain 2 (FH2) domain of Fmn2, called FSI. This direct interaction is required for the synergy between the two proteins in actin assembly. We have recently demonstrated how Spire, which caps barbed ends via its WH2 domains, activates Fmn2. Fmn2 by itself associates very poorly to filament barbed ends but is rapidly recruited to Spire-capped barbed ends via the KIND domain, and it subsequently displaces Spire from the barbed end to elicit rapid processive assembly from profilin·actin. Here, we address the mechanism by which Spire and Fmn2 compete at barbed ends and the role of FSI in orchestrating this competition as well as in the processivity of Fmn2. We have combined microcalorimetric, fluorescence, and hydrodynamic binding assays, as well as bulk solution and single filament measurements of actin assembly, to show that removal of FSI converts Fmn2 into a Capping Protein. This activity is mimicked by association of KIND to Fmn2. In addition, FSI binds actin at filament barbed ends as a weak capper and plays a role in displacing the WH2 domains of Spire from actin, thus allowing the association of actin-binding regions of FH2 to the barbed end.
    Mots-clés : ACTIN, Actin Cytoskeleton, Animals, B3S, Binding, Competitive, Conserved Sequence, Gene Deletion, Humans, Kinetics, Mice, Microfilament Proteins, Models, Molecular, Molecular Weight, Nuclear Proteins, Peptide Fragments, Protein Conformation, Protein Interaction Domains and Motifs, Protein Multimerization, Recombinant Fusion Proteins, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid.

  • J. Pernier, S. Shekhar, A. Jegou, B. Guichard, et M. - F. Carlier, « Profilin Interaction with Actin Filament Barbed End Controls Dynamic Instability, Capping, Branching, and Motility », Developmental Cell, vol. 36, nᵒ 2, p. 201-214, 2016.
    Mots-clés : ACTIN, Actin Cytoskeleton, Actin-Related Protein 2-3 Complex, Actins, Animals, B3S, Cell Movement, Cytoskeleton, Profilins, Protein Binding, Rabbits.

  • L. Renault, « Intrinsic, Functional, and Structural Properties of β-Thymosins and β-Thymosin/WH2 Domains in the Regulation and Coordination of Actin Self-Assembly Dynamics and Cytoskeleton Remodeling », Vitamins and Hormones, vol. 102, p. 25-54, 2016.
    Résumé : β-Thymosins are a family of heat-stable multifunctional polypeptides that are expressed as small proteins of about 5kDa (~45 amino acids) almost exclusively in multicellular animals. They were first isolated from the thymus. As full-length or truncated polypeptides, they appear to stimulate a broad range of extracellular activities in various signaling pathways, including tissue repair and regeneration, inflammation, cell migration, and immune defense. However, their cell surface receptors and structural mechanisms of regulations in these multiple pathways remain still poorly understood. Besides their extracellular activities, they belong to a larger family of small, intrinsically disordered actin-binding domains called WH2/β-thymosin domains that have been identified in more than 1800 multidomain proteins found in different taxonomic domains of life and involved in various actin-based motile processes including cell morphogenesis, motility, adhesions, tissue development, intracellular trafficking, or pathogen infections. This review briefly surveys the main recent findings to understand how these small, intrinsically disordered but functional domains can interact with many unrelated partners and can thus integrate and coordinate various intracellular activities in actin self-assembly dynamics and cell signaling pathways linked to their cytoskeleton remodeling.
    Mots-clés : ACTIN, Actin Cytoskeleton, Actin-binding proteins, B3S, Functional versatility, Fuzzy complex, Intrinsically disordered, Multifunctionality, Structure–function relationship, Thymosin-β4, WH2 domain, β-Thymosin.

  • S. Shekhar, J. Pernier, et M. - F. Carlier, « Regulators of actin filament barbed ends at a glance », Journal of Cell Science, vol. 129, nᵒ 6, p. 1085-1091, mars 2016.
    Mots-clés : ACTIN, Actin assembly, Actin Cytoskeleton, Actins, Animals, B3S, Capping protein, Cytoskeleton, Filament barbed end, formin, Humans, Motility, profilin.

  • S. Shekhar et M. - F. Carlier, « Single-filament kinetic studies provide novel insights into regulation of actin-based motility », Molecular Biology of the Cell, vol. 27, nᵒ 1, p. 1-6, 2016.
    Résumé : Polarized assembly of actin filaments forms the basis of actin-based motility and is regulated both spatially and temporally. Cells use a variety of mechanisms by which intrinsically slower processes are accelerated, and faster ones decelerated, to match rates observed in vivo. Here we discuss how kinetic studies of individual reactions and cycles that drive actin remodeling have provided a mechanistic and quantitative understanding of such processes. We specifically consider key barbed-end regulators such as capping protein and formins as illustrative examples. We compare and contrast different kinetic approaches, such as the traditional pyrene-polymerization bulk assays, as well as more recently developed single-filament and single-molecule imaging approaches. Recent development of novel biophysical methods for sensing and applying forces will in future allow us to address the very important relationship between mechanical stimulus and kinetics of actin-based motility.
    Mots-clés : ACTIN, Actin Capping Proteins, Actin Cytoskeleton, B3S, Cell Movement, Cytoskeleton, Fetal Proteins, Kinetics, Microfilament Proteins, Models, Molecular, Nuclear Proteins, Profilins, Protein Binding.


  • B. S. Avvaru, J. Pernier, et M. - F. Carlier, « Dimeric WH2 repeats of VopF sequester actin monomers into non-nucleating linear string conformations: An X-ray scattering study », Journal of Structural Biology, vol. 190, nᵒ 2, p. 192-199, 2015.
    Mots-clés : ACTIN, Actin Cytoskeleton, B3S, Bacterial Outer Membrane Proteins, Dimerization, Models, Molecular, Protein Conformation, Protein Structure, Tertiary, SAXS, Scattering, Small Angle, Vibrio cholerae, Virulence Factors, VopF, WH2 domain repeats.

  • M. - F. Carlier, J. Pernier, P. Montaville, S. Shekhar, et S. Kühn, « Control of polarized assembly of actin filaments in cell motility », Cellular and Molecular Life Sciences, vol. 72, nᵒ 16, p. 3051-3067, 2015.
    Mots-clés : ACTIN, Actin Cytoskeleton, Actin-Related Protein 2-3 Complex, B3S, Cell Movement, Cell Polarity, Microfilament Proteins, Models, Biological, Models, Molecular, Optical Imaging, Protein Binding, Protein Conformation.

  • C. Ciobanasu, B. Faivre, et C. Le Clainche, « Reconstituting actomyosin-dependent mechanosensitive protein complexes in vitro », Nature Protocols, vol. 10, nᵒ 1, p. 75-89, 2015.
    Résumé : In many mechanosensitive biological processes, actin-binding proteins (ABPs) sense the force generated by the actomyosin cytoskeleton and respond by recruiting effector proteins. We developed an in vitro assay, with pure proteins, to observe the force-dependent binding of a protein to a cryptic binding site buried in the stretchable domain of an ABP. Here we describe the protocol to study the actomyosin-dependent binding of vinculin to the ABP talin. In this assay, talin is immobilized in 5-μm-diameter disc-shaped islands, which are regularly spaced by 35 μm and micropatterned on a glass coverslip. In response to the force generated by an actomyosin network, talin extension reveals cryptic vinculin-binding sites (VBSs). To follow this reaction, fluorescent proteins are visualized by total internal refection fluorescence (TIRF) microscopy. EGFP-vinculin fluorescence in talin-coated discs reveals the binding of vinculin to stretched talin. Actomyosin structures are visualized by the fluorescence of Alexa Fluor 594-labeled actin. This protocol describes the purification of the proteins, the preparation of the chamber in which talin is coated on a micropatterned surface, and the biochemical conditions to study several kinetic parameters of the actomyosin-dependent binding of vinculin to talin. A stable actomyosin network is used to measure the steady-state dissociation of vinculin from talin under constant force. In the presence of α-actinin-1, actomyosin cables undergo cycles of force application and release, allowing the measurement of vinculin dissociation associated with talin re-folding. Expression and purification of the proteins requires at least 3 weeks. The assay can be completed within 1 d.
    Mots-clés : ACTIN, Actomyosin, B3S, Biomechanical Phenomena, In Vitro Techniques, Mechanotransduction, Cellular, Microscopy, Fluorescence, Multiprotein Complexes, Organic Chemicals, Protein Binding, Talin, Vinculin.

  • I. Herrada, C. Samson, C. Velours, L. Renault, C. Östlund, P. Chervy, D. Puchkov, H. J. Worman, B. Buendia, et S. Zinn-Justin, « Muscular Dystrophy Mutations Impair the Nuclear Envelope Emerin Self-assembly Properties », ACS chemical biology, vol. 10, nᵒ 12, p. 2733-2742, 2015.
    Résumé : More than 100 genetic mutations causing X-linked Emery-Dreifuss muscular dystrophy have been identified in the gene encoding the integral inner nuclear membrane protein emerin. Most mutations are nonsense or frameshift mutations that lead to the absence of emerin in cells. Only very few cases are due to missense or short in-frame deletions. Molecular mechanisms explaining the corresponding emerin variants' loss of function are particularly difficult to identify because of the mostly intrinsically disordered state of the emerin nucleoplasmic region. We now demonstrate that this EmN region can be produced as a disordered monomer, as revealed by nuclear magnetic resonance, but rapidly self-assembles in vitro. Increases in concentration and temperature favor the formation of long curvilinear filaments with diameters of approximately 10 nm, as observed by electron microscopy. Assembly of these filaments can be followed by fluorescence through Thioflavin-T binding and by Fourier-transform Infrared spectrometry through formation of β-structures. Analysis of the assembly properties of five EmN variants reveals that del95-99 and Q133H impact filament assembly capacities. In cells, these variants are located at the nuclear envelope, but the corresponding quantities of emerin-emerin and emerin-lamin proximities are decreased compared to wild-type protein. Furthermore, variant P183H favors EmN aggregation in vitro, and variant P183T provokes emerin accumulation in cytoplasmic foci in cells. Substitution of residue Pro183 might systematically favor oligomerization, leading to emerin aggregation and mislocalization in cells. Our results suggest that emerin self-assembly is necessary for its proper function and that a loss of either the protein itself or its ability to self-assemble causes muscular dystrophy.
    Mots-clés : ACTIN, B3S, Genetic Variation, HeLa Cells, Humans, Hydrophobic and Hydrophilic Interactions, INTGEN, Magnetic Resonance Spectroscopy, Membrane Proteins, Muscular Dystrophies, Nuclear Envelope, Nuclear Proteins, PF, PIM, Proteostasis Deficiencies, Spectroscopy, Fourier Transform Infrared.

  • S. Shekhar, M. Kerleau, S. Kühn, J. Pernier, G. Romet-Lemonne, A. Jégou, et M. - F. Carlier, « Formin and capping protein together embrace the actin filament in a ménage à trois », Nature Communications, vol. 6, p. 8730, nov. 2015.
    Mots-clés : ACTIN, Actin Capping Proteins, Actin Cytoskeleton, Adaptor Proteins, Signal Transducing, Animals, B3S, Humans, Kinetics, Protein Binding, Proteins, Rabbits.
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Sélection de publications entre 2001-2014

# auteur de correspondance, gras : membres de l’équipe

- Carlier MF, Romet-Lemonne G, Jégou A. (2014) Actin filament dynamics using microfluidics.
Methods Enzymol. 540:3-17 PubMed

-  Mueller J, Pfanzelter J, Winkler C, Narita A, Le Clainche C, Nemethova M, Carlier MF, Maeda Y, Welch MD, Ohkawa T, Schmeiser C, Resch GP, Small JV. (2014) Electron tomography and simulation of baculovirus actin comet tails support a tethered filament model of pathogen propulsion.
PLoS Biol. 12(1):e1001765 PubMed

-  Ciobanasu C, Faivre B, Le Clainche C. (2014) Actomyosin-dependent formation of the mechanosensitive talin-vinculin complex reinforces actin anchoring.
Nat Commun. 5:3095 PubMed

- Jiao Y, Walker M, Trinick J, Pernier J, Montaville P, Carlier MF. (2014) Mutagenetic and electron microscopy analysis of actin filament severing by Cordon-Bleu, a WH2 domain protein.
Cytoskeleton (Hoboken).71(3):170-83 PubMed

- Ciobanasu C, Faivre B, Le Clainche C#. (2013) Integrating actin dynamics, mechanotransduction and integrin activation : the multiple functions of actin binding proteins in focal adhesions.
Eur J Cell Biol. 92(10-11), 339-48. Review.

- Renault, L#, Deville, C., van Heijenoort C. (2013) Structural features and interfacial properties of WH2, β-Thymosin domains and other intrinsically disordered domains in the regulation of actin cytoskeleton dynamics.
Cytoskeleton (Hoboken) 70(11):686-705. Review.

- Dias J, Renault L#, Pérez J, Mirande M#. (2013) Small-angle X-ray solution scattering study of the multi-aminoacyl-tRNA synthetase complex reveals an elongated and multi-armed particle.
J Biol Chem. 288(33), 23979-89.

- D. Didry, F.X. Cantrelle, C. Husson, P. Roblin, A. M. Eswara Moorthy, J. Perez, C. Le Clainche, M. Hertzog, E. Guittet, M.F. Carlier, C. van Heijenoort# and L. Renault#. (2012) How a Single Residue in Individual ß-Thymosin/WH2 Domains Controls their Functions in Actin Assembly.
EMBO J. 31(4), 1000-13

- C. Husson, L. Renault, D. Didry, D. Pantaloni, M.F. Carlier #. (2011) Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin filament assembly.
Molecular Cell 43, 464-77.

- C. Le Clainche#, S. Prakash Dwivedi, D. Didry and M.F. Carlier (2010) Vinculin Is a Dually Regulated Actin Filament Barbed End-capping and Side-binding Protein.
J. Biol Chem. 285(30),23420-32.

- Le Clainche C#, Carlier M (2008). Regulation of actin assembly associated with protrusion and adhesion in cell migration.
Physiological Reviews. 88(2):489-513. Review.

- Le Clainche C, Pauly BS, Zhang CX, Engqvist-Goldstein AE, Cunningham K, Drubin DG. (2007) A Hip1R-cortactin complex negatively regulates actin assembly associated with endocytosis.
EMBO J. 26(5), 1199-210.

- Bosch M, Le KH, Bugyi B,Correia JJ, Renault L#, Carlier MF#. (2007) Analysis of the Function of Spire in Actin Assembly and Its Synergy with Formin and Profilin.
Molecular Cell 28(4), 555-568.

- Ghosh A., Praefcke G. J. K., Renault L.#, Wittinghofer A.#, Herrmann C. (2006) How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP.
Nature 440, 101-4.

- Romero S, Le Clainche C, Didry D, Egile C, Pantaloni D, Carlier MF# . (2004) Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis.
Cell 119(3), 419-29.

- C. Le Clainche, D. Pantaloni and M.F. Carlier #. (2003) ATP hydrolysis on Arp2/3 complex causes debranching of dendritic actin arrays.
Proceedings of the National Academy of Sciences of USA 100(11), 6337-42.

- Renault L., Guibert B., Cherfils J. # (2003) Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor.
Nature 426, 525-530.

- Renault L., Kuhlmann J., Henkel A. & Wittinghofer A. # (2001) Structural basis for guanine nucleotide exchange on Ran by the Regulator of Chromosome Condensation (RCC1).
Cell 105, 245-255.

- Pantaloni D, Le Clainche C, Carlier MF# (2001). Mechanism of actin-based motility.
Science 292(5521), 1502-6. Review.

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