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hal.structure.identifierInterdisciplinary Institute for Neuroscience [Bordeaux] [IINS]
dc.contributor.authorMASSOU, Sophie
hal.structure.identifierInterdisciplinary Institute for Neuroscience [Bordeaux] [IINS]
dc.contributor.authorNUNES VICENTE, Filipe
hal.structure.identifierLaboratoire Photonique, Numérique et Nanosciences [LP2N]
dc.contributor.authorWETZEL, Franziska
hal.structure.identifierInterdisciplinary Institute for Neuroscience [Bordeaux] [IINS]
dc.contributor.authorMEHIDI, Amine
hal.structure.identifierLaboratoire Photonique, Numérique et Nanosciences [LP2N]
dc.contributor.authorSTREHLE, Dan
hal.structure.identifierCentre National de la Recherche Scientifique [CNRS]
dc.contributor.authorLEDUC, Cecile
hal.structure.identifierLaboratoire Jean Perrin [LJP]
dc.contributor.authorVOITURIEZ, Raphaël
hal.structure.identifierInterdisciplinary Institute for Neuroscience [Bordeaux] [IINS]
dc.contributor.authorROSSIER, Olivier
hal.structure.identifierLaboratoire Photonique, Numérique et Nanosciences [LP2N]
dc.contributor.authorNASSOY, Pierre
hal.structure.identifierInterdisciplinary Institute for Neuroscience [Bordeaux] [IINS]
dc.contributor.authorGIANNONE, Grégory
dc.date.accessioned2023-05-12T10:37:33Z
dc.date.available2023-05-12T10:37:33Z
dc.date.issued2020-08
dc.identifier.issn1465-7392
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/181540
dc.description.abstractEnDetection and conversion of mechanical forces into biochemical signals control cell functions during physiological and pathological processes. Mechano-sensing is based on protein deformations and reorganizations, yet the molecular mechanisms in cells are still unclear. Using a cell stretching device compatible with super-resolution microscopy (SRM) and single protein tracking (SPT), we explored the nanoscale deformations and reorganizations of individual proteins inside mechano-sensitive structures. We achieved SRM after live stretching on intermediate filaments, microtubules and integrin adhesions. Simultaneous SPT and stretching showed that while integrins follow the elastic deformation of the substrate, actin filaments and talin also displayed lagged and transient inelastic responses associated with active acto-myosin remodeling and talin deformations. Capturing acute reorganizations of single-molecule during stretching showed that force-dependent vinculin recruitment is delayed and depends on the maturation state of integrin adhesions. Thus, cells respond to external forces by amplifying transiently and locally cytoskeleton displacements enabling protein deformation and recruitment in mechano-sensitive structures.
dc.language.isoen
dc.publisherNature Publishing Group
dc.title.enCell stretching is amplified by active actin remodelling to deform and recruit proteins in mechanosensitive structures
dc.typeArticle de revue
dc.identifier.doi10.1038/s41556-020-0548-2
dc.subject.halSciences du Vivant [q-bio]/Biologie cellulaire/Organisation et fonctions cellulaires [q-bio.SC]
dc.subject.halPhysique [physics]/Physique [physics]/Biophysique [physics.bio-ph]
bordeaux.journalNature Cell Biology
bordeaux.page1011-1023
bordeaux.volume22
bordeaux.hal.laboratoriesLaboratoire Photonique, Numérique et Nanosciences (LP2N) - UMR 5298*
bordeaux.issue8
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionCNRS
bordeaux.peerReviewedoui
hal.identifierhal-03027100
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-03027100v1
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