Search Results - "Guichard, Berengere"

Profilin Interaction with Actin Filament Barbed End Controls Dynamic Instability, Capping, Branching, and Motility by Pernier, Julien, Shekhar, Shashank, Jegou, Antoine, Guichard, Bérengère, Carlier, Marie-France

“…Cell motility and actin homeostasis depend on the control of polarized growth of actin filaments. Profilin, an abundant regulator of actin dynamics, supports…”
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Actin filament oxidation by MICAL1 suppresses protections from cofilin-induced disassembly by Wioland, Hugo, Frémont, Stéphane, Guichard, Bérengère, Echard, Arnaud, Jégou, Antoine, Romet-Lemonne, Guillaume

“…Proteins of the ADF/cofilin family play a central role in the disassembly of actin filaments, and their activity must be tightly regulated in cells. Recently,…”
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Geometrical Constraints Greatly Hinder Formin mDia1 Activity by Suzuki, Emiko L, Chikireddy, Jahnavi, Dmitrieff, Serge, Guichard, Bérengère, Romet-Lemonne, Guillaume, Jégou, Antoine

“…Formins are one of the central players in the assembly of most actin networks in cells. The sensitivity of these processive molecular machines to mechanical…”
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Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork by Richet, Nicolas, Liu, Danni, Legrand, Pierre, Velours, Christophe, Corpet, Armelle, Gaubert, Albane, Bakail, May, Moal-Raisin, Gwenaelle, Guerois, Raphael, Compper, Christel, Besle, Arthur, Guichard, Berengère, Almouzni, Genevieve, Ochsenbein, Françoise

“…MCM2 is a subunit of the replicative helicase machinery shown to interact with histones H3 and H4 during the replication process through its N-terminal domain…”
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Spire and Formin 2 synergize and antagonize in regulating actin assembly in meiosis by a ping-pong mechanism by Montaville, Pierre, Jégou, Antoine, Pernier, Julien, Compper, Christel, Guichard, Bérengère, Mogessie, Binyam, Schuh, Melina, Romet-Lemonne, Guillaume, Carlier, Marie-France

“…In mammalian oocytes, three actin binding proteins, Formin 2 (Fmn2), Spire, and profilin, synergistically organize a dynamic cytoplasmic actin meshwork that…”
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Interactions of Isolated C-terminal Fragments of Neural Wiskott-Aldrich Syndrome Protein (N-WASP) with Actin and Arp2/3 Complex by Gaucher, Jean-François, Maugé, Chloé, Didry, Dominique, Guichard, Bérengère, Renault, Louis, Carlier, Marie-France

“…Wiskott-Aldrich syndrome proteins (WASP) are a family of proteins that all catalyze actin filament branching with the Arp2/3 complex in a variety of…”
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Direct observation of the conformational states of formin mDia1 at actin filament barbed ends and along the filament by Maufront, Julien, Guichard, Bérengère, Cao, Lu-Yan, Cicco, Aurélie Di, Jégou, Antoine, Romet-Lemonne, Guillaume, Bertin, Aurélie

“…The fine regulation of actin polymerization is essential to control cell motility and architecture and to perform essential cellular functions. Formins are key…”
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Using Microfluidics Single Filament Assay to Study Formin Control of Actin Assembly by Romet-Lemonne, Guillaume, Guichard, Bérengère, Jégou, Antoine

“…Formin is a highly processive motor that offers very unique features to control the elongation of actin filaments. When bound to the filament barbed-end, it…”
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Intermittent depolymerization of actin filaments is caused by photo-induced dimerization of actin protomers by Niedermayer, Thomas, Jégou, Antoine, Chièze, Lionel, Guichard, Bérengère, Helfer, Emmanuèle, Romet-Lemonne, Guillaume, Carlier, Marie-France, Lipowsky, Reinhard

“…Actin, one of the most abundant proteins within eukaryotic cells, assembles into long filaments that form intricate cytoskeletal networks and are continuously…”
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Dimeric WH2 domains in Vibrio VopF promote actin filament barbed-end uncapping and assisted elongation by Pernier, Julien, Orban, Jozsef, Avvaru, Balendu Sankara, Jégou, Antoine, Romet-Lemonne, Guillaume, Guichard, Bérengère, Carlier, Marie-France

“…Proteins containing repeats of the WASP homology 2 (WH2) actin-binding module are multifunctional regulators of actin nucleation and assembly. Now biochemical…”
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Modulation of formin processivity by profilin and mechanical tension by Cao, Luyan, Kerleau, Mikael, Suzuki, Emiko L, Wioland, Hugo, Jouet, Sandy, Guichard, Berengere, Lenz, Martin, Romet-Lemonne, Guillaume, Jegou, Antoine

“…Formins are major regulators of actin networks. They enhance actin filament dynamics by remaining processively bound to filament barbed ends. How biochemical…”
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Regeneration of actin filament branches from the same Arp2/3 complex by Ghasemi, Foad, Cao, LuYan, Mladenov, Miroslav, Guichard, Bérengère, Way, Michael, Jégou, Antoine, Romet-Lemonne, Guillaume

“…Branched actin filaments are found in many key cellular structures. Branches are nucleated by the Arp2/3 complex activated by nucleation-promoting factor (NPF)…”
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Spire and Formin 2 Synergize and Antagonize in Regulating Actin Assembly in Meiosis by a Ping-Pong Mechanism: e1001795 by Montaville, Pierre, Jégou, Antoine, Pernier, Julien, Compper, Christel, Guichard, Bérengère, Mogessie, Binyam, Schuh, Melina, Romet-Lemonne, Guillaume, Carlier, Marie-France

“…In mammalian oocytes, three actin binding proteins, Formin 2 (Fmn2), Spire, and profilin, synergistically organize a dynamic cytoplasmic actin meshwork that…”
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ADF/Cofilin Accelerates Actin Dynamics by Severing Filaments and Promoting Their Depolymerization at Both Ends by Wioland, Hugo, Guichard, Berengere, Senju, Yosuke, Myram, Sarah, Lappalainen, Pekka, Jégou, Antoine, Romet-Lemonne, Guillaume

“…Actin-depolymerizing factor (ADF)/cofilins contribute to cytoskeletal dynamics by promoting rapid actin filament disassembly. In the classical view,…”
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occludin and ZO-1 complex, defined by small angle X-ray scattering and NMR, has implications for modulating tight junction permeability by Tash, Brian R, Bewley, Maria C, Russo, Mariano, Keil, Jason M, Griffin, Kathleen A, Sundstrom, Jeffrey M, Antonetti, David A, Tian, Fang, Flanagan, John M

“…Tight junctions (TJs) are dynamic cellular structures that are critical for compartmentalizing environments within tissues and regulating transport of small…”
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