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Your search keyword '"Gonzalez Rodriguez, David"' showing total 3 results
Start Over Author "Gonzalez Rodriguez, David" Topic actomyosin
3 results on '"Gonzalez Rodriguez, David"'

1. Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation.

Author

Stefani C, Gonzalez-Rodriguez D, Senju Y, Doye A, Efimova N, Janel S, Lipuma J, Tsai MC, Hamaoui D, Maddugoda MP, Cochet-Escartin O, Prévost C, Lafont F, Svitkina T, Lappalainen P, Bassereau P, and Lemichez E

Subjects
Actin Cytoskeleton chemistry, Actin Cytoskeleton genetics, Actin Cytoskeleton metabolism, Actomyosin chemistry, Actomyosin genetics, Cytoskeletal Proteins chemistry, Cytoskeletal Proteins genetics, Human Umbilical Vein Endothelial Cells chemistry, Human Umbilical Vein Endothelial Cells metabolism, Humans, Nonmuscle Myosin Type IIA chemistry, Nonmuscle Myosin Type IIA genetics, Surface Tension, Actomyosin metabolism, Cytoskeletal Proteins metabolism, Nonmuscle Myosin Type IIA metabolism
Abstract

Transendothelial cell macroaperture (TEM) tunnels control endothelium barrier function and are triggered by several toxins from pathogenic bacteria that provoke vascular leakage. Cellular dewetting theory predicted that a line tension of uncharacterized origin works at TEM boundaries to limit their widening. Here, by conducting high-resolution microscopy approaches we unveil the presence of an actomyosin cable encircling TEMs. We develop a theoretical cellular dewetting framework to interpret TEM physical parameters that are quantitatively determined by laser ablation experiments. This establishes the critical role of ezrin and non-muscle myosin II (NMII) in the progressive implementation of line tension. Mechanistically, fluorescence-recovery-after-photobleaching experiments point for the upstream role of ezrin in stabilizing actin filaments at the edges of TEMs, thereby favouring their crosslinking by NMIIa. Collectively, our findings ascribe to ezrin and NMIIa a critical function of enhancing line tension at the cell boundary surrounding the TEMs by promoting the formation of an actomyosin ring.

Published
2017
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2. Transcellular tunnel dynamics: Control of cellular dewetting by actomyosin contractility and I-BAR proteins.

Author

Lemichez E, Gonzalez-Rodriguez D, Bassereau P, and Brochard-Wyart F

Subjects
Animals, Disease, Humans, Actomyosin metabolism, Endothelial Cells metabolism, Proteins metabolism, Wettability
Abstract

Dewetting is the spontaneous withdrawal of a liquid film from a non-wettable surface by nucleation and growth of dry patches. Two recent reports now propose that the principles of dewetting explain the physical phenomena underpinning the opening of transendothelial cell macroaperture (TEM) tunnels, referred to as cellular dewetting. This was discovered by studying a group of bacterial toxins endowed with the property of corrupting actomyosin cytoskeleton contractility. For both liquid and cellular dewetting, the growth of holes is governed by a competition between surface forces and line tension. We also discuss how the dynamics of TEM opening and closure represent remarkable systems to investigate actin cytoskeleton regulation by sensors of plasma membrane curvature and investigate the impact on membrane tension and the role of TEM in vascular dysfunctions., (Copyright © 2013 Soçiété Française des Microscopies and Soçiété de Biologie Cellulaire de France.)

Published
2013
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3. Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation

Author

Stefani, Caroline, Gonzalez-Rodriguez, David, Senju, Yosuke, Doye, Anne, Efimova, Nadia, Janel, Sébastien, Lipuma, Justine, Tsai, Meng Chen, Hamaoui, Daniel, Maddugoda, Madhavi P., Cochet-Escartin, Olivier, Prévost, Coline, Lafont, Frank, Svitkina, Tatyana, Lappalainen, Pekka, Bassereau, Patricia, Lemichez, Emmanuel, Institute of Biotechnology, Pekka Lappalainen / Principal Investigator, Centre méditerranéen de médecine moléculaire (C3M), Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), Université Nice Sophia Antipolis - Faculté de Médecine (UNS UFR Médecine), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA), Laboratoire de Chimie et Physique - Approche Multi-échelle des Milieux Complexes (LCP-A2MC), Université de Lorraine (UL), Helsingin yliopisto = Helsingfors universitet = University of Helsinki, University of Pennsylvania, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Sorbonne Université (SU), Laboratoire Physico-Chimie Curie [Institut Curie] (PCC), Institut Curie [Paris]-Institut de Chimie du CNRS (INC)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Université Nice Sophia Antipolis (... - 2019) (UNS), University of Helsinki, University of Pennsylvania [Philadelphia], Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), and COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Université Côte d'Azur (UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
DYNAMICS, F-ACTIN, MIGRATION, Nonmuscle Myosin Type IIA, Science, MYOSIN-II, Actomyosin, macromolecular substances, STRESS FIBERS, Article, Actin Cytoskeleton, Cytoskeletal Proteins, PHENOTYPIC HETEROGENEITY, EPITHELIAL CLOSURE, CELLS, Human Umbilical Vein Endothelial Cells, Humans, Surface Tension, 1182 Biochemistry, cell and molecular biology, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, ACTIN POLYMERIZATION, STAPHYLOCOCCUS-AUREUS
Abstract

Transendothelial cell macroaperture (TEM) tunnels control endothelium barrier function and are triggered by several toxins from pathogenic bacteria that provoke vascular leakage. Cellular dewetting theory predicted that a line tension of uncharacterized origin works at TEM boundaries to limit their widening. Here, by conducting high-resolution microscopy approaches we unveil the presence of an actomyosin cable encircling TEMs. We develop a theoretical cellular dewetting framework to interpret TEM physical parameters that are quantitatively determined by laser ablation experiments. This establishes the critical role of ezrin and non-muscle myosin II (NMII) in the progressive implementation of line tension. Mechanistically, fluorescence-recovery-after-photobleaching experiments point for the upstream role of ezrin in stabilizing actin filaments at the edges of TEMs, thereby favouring their crosslinking by NMIIa. Collectively, our findings ascribe to ezrin and NMIIa a critical function of enhancing line tension at the cell boundary surrounding the TEMs by promoting the formation of an actomyosin ring., Holes in endothelial barriers, called transendothelial cell macroapertures (TEMs), are predicted to be limited by line tension of unknown origin. Here the authors identify an actomyosin cable encircling TEMs and establish a role for ezrin in stabilising F-actin bundles, allowing their crosslinking by non-muscle myosin IIa.

Published
2017
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