Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures

Autores
Baschieri, Francesco; Dayot, Stéphane; Elkhatib, Nadia; Ly, Nathalie; Capmany, Anahi; Schauer, Kristine; Betz, Timo; Vignjevic, Danijela Matic; Poincloux, Renaud; Montagnac, Guillaume
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
It is generally assumed that cells interrogate the mechanical properties of their environment by pushing and pulling on the extracellular matrix (ECM). For instance, acto-myosin-dependent contraction forces exerted at focal adhesions (FAs) allow the cell to actively probe substrate elasticity. Here, we report that a subset of long-lived and flat clathrin-coated structures (CCSs), also termed plaques, are contractility-independent mechanosensitive signaling platforms. We observed that plaques assemble in response to increasing substrate rigidity and that this is independent of FAs, actin and myosin-II activity. We show that plaque assembly depends on αvβ5 integrin, and is a consequence of frustrated endocytosis whereby αvβ5 tightly engaged with the stiff substrate locally stalls CCS dynamics. We also report that plaques serve as platforms for receptor-dependent signaling and are required for increased Erk activation and cell proliferation on stiff environments. We conclude that CCSs are mechanotransduction structures that sense substrate rigidity independently of cell contractility.
Fil: Baschieri, Francesco. Université Paris Sud; Francia
Fil: Dayot, Stéphane. Université Paris Sud; Francia. Research University; Francia
Fil: Elkhatib, Nadia. Université Paris Sud; Francia
Fil: Ly, Nathalie. Université Paris Sud; Francia
Fil: Capmany, Anahi. Centre National de la Recherche Scientifique; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina. Research University; Francia
Fil: Schauer, Kristine. Research University; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Betz, Timo. University of Münster; Alemania
Fil: Vignjevic, Danijela Matic. Centre National de la Recherche Scientifique; Francia. Research University; Francia
Fil: Poincloux, Renaud. Université de Toulouse; Francia
Fil: Montagnac, Guillaume. Université Paris Sud; Francia
Materia
CLATHRIN-COATED STRUCTURES
SUBSTRATE RIGIDITY
MECHANOTRANSDUCTION
ENDOCYTOSIS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/100397
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/100397
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structuresBaschieri, FrancescoDayot, StéphaneElkhatib, NadiaLy, NathalieCapmany, AnahiSchauer, KristineBetz, TimoVignjevic, Danijela MaticPoincloux, RenaudMontagnac, GuillaumeCLATHRIN-COATED STRUCTURESSUBSTRATE RIGIDITYMECHANOTRANSDUCTIONENDOCYTOSIShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1It is generally assumed that cells interrogate the mechanical properties of their environment by pushing and pulling on the extracellular matrix (ECM). For instance, acto-myosin-dependent contraction forces exerted at focal adhesions (FAs) allow the cell to actively probe substrate elasticity. Here, we report that a subset of long-lived and flat clathrin-coated structures (CCSs), also termed plaques, are contractility-independent mechanosensitive signaling platforms. We observed that plaques assemble in response to increasing substrate rigidity and that this is independent of FAs, actin and myosin-II activity. We show that plaque assembly depends on αvβ5 integrin, and is a consequence of frustrated endocytosis whereby αvβ5 tightly engaged with the stiff substrate locally stalls CCS dynamics. We also report that plaques serve as platforms for receptor-dependent signaling and are required for increased Erk activation and cell proliferation on stiff environments. We conclude that CCSs are mechanotransduction structures that sense substrate rigidity independently of cell contractility.Fil: Baschieri, Francesco. Université Paris Sud; FranciaFil: Dayot, Stéphane. Université Paris Sud; Francia. Research University; FranciaFil: Elkhatib, Nadia. Université Paris Sud; FranciaFil: Ly, Nathalie. Université Paris Sud; FranciaFil: Capmany, Anahi. Centre National de la Recherche Scientifique; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina. Research University; FranciaFil: Schauer, Kristine. Research University; Francia. Centre National de la Recherche Scientifique; FranciaFil: Betz, Timo. University of Münster; AlemaniaFil: Vignjevic, Danijela Matic. Centre National de la Recherche Scientifique; Francia. Research University; FranciaFil: Poincloux, Renaud. Université de Toulouse; FranciaFil: Montagnac, Guillaume. Université Paris Sud; FranciaNature Publishing Group2018-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/100397Baschieri, Francesco; Dayot, Stéphane; Elkhatib, Nadia; Ly, Nathalie; Capmany, Anahi; et al.; Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures; Nature Publishing Group; Nature Communications; 9; 1; 12-20182041-1723CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41467-018-06367-yinfo:eu-repo/semantics/altIdentifier/doi/10.1038/s41467-018-06367-yinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:05:09Zoai:ri.conicet.gov.ar:11336/100397instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:05:10.028CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures
title Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures
spellingShingle Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures
Baschieri, Francesco
CLATHRIN-COATED STRUCTURES
SUBSTRATE RIGIDITY
MECHANOTRANSDUCTION
ENDOCYTOSIS
title_short Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures
title_full Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures
title_fullStr Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures
title_full_unstemmed Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures
title_sort Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures
dc.creator.none.fl_str_mv Baschieri, Francesco
Dayot, Stéphane
Elkhatib, Nadia
Ly, Nathalie
Capmany, Anahi
Schauer, Kristine
Betz, Timo
Vignjevic, Danijela Matic
Poincloux, Renaud
Montagnac, Guillaume
author Baschieri, Francesco
author_facet Baschieri, Francesco
Dayot, Stéphane
Elkhatib, Nadia
Ly, Nathalie
Capmany, Anahi
Schauer, Kristine
Betz, Timo
Vignjevic, Danijela Matic
Poincloux, Renaud
Montagnac, Guillaume
author_role author
author2 Dayot, Stéphane
Elkhatib, Nadia
Ly, Nathalie
Capmany, Anahi
Schauer, Kristine
Betz, Timo
Vignjevic, Danijela Matic
Poincloux, Renaud
Montagnac, Guillaume
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv CLATHRIN-COATED STRUCTURES
SUBSTRATE RIGIDITY
MECHANOTRANSDUCTION
ENDOCYTOSIS
topic CLATHRIN-COATED STRUCTURES
SUBSTRATE RIGIDITY
MECHANOTRANSDUCTION
ENDOCYTOSIS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv It is generally assumed that cells interrogate the mechanical properties of their environment by pushing and pulling on the extracellular matrix (ECM). For instance, acto-myosin-dependent contraction forces exerted at focal adhesions (FAs) allow the cell to actively probe substrate elasticity. Here, we report that a subset of long-lived and flat clathrin-coated structures (CCSs), also termed plaques, are contractility-independent mechanosensitive signaling platforms. We observed that plaques assemble in response to increasing substrate rigidity and that this is independent of FAs, actin and myosin-II activity. We show that plaque assembly depends on αvβ5 integrin, and is a consequence of frustrated endocytosis whereby αvβ5 tightly engaged with the stiff substrate locally stalls CCS dynamics. We also report that plaques serve as platforms for receptor-dependent signaling and are required for increased Erk activation and cell proliferation on stiff environments. We conclude that CCSs are mechanotransduction structures that sense substrate rigidity independently of cell contractility.
Fil: Baschieri, Francesco. Université Paris Sud; Francia
Fil: Dayot, Stéphane. Université Paris Sud; Francia. Research University; Francia
Fil: Elkhatib, Nadia. Université Paris Sud; Francia
Fil: Ly, Nathalie. Université Paris Sud; Francia
Fil: Capmany, Anahi. Centre National de la Recherche Scientifique; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza; Argentina. Research University; Francia
Fil: Schauer, Kristine. Research University; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Betz, Timo. University of Münster; Alemania
Fil: Vignjevic, Danijela Matic. Centre National de la Recherche Scientifique; Francia. Research University; Francia
Fil: Poincloux, Renaud. Université de Toulouse; Francia
Fil: Montagnac, Guillaume. Université Paris Sud; Francia
description It is generally assumed that cells interrogate the mechanical properties of their environment by pushing and pulling on the extracellular matrix (ECM). For instance, acto-myosin-dependent contraction forces exerted at focal adhesions (FAs) allow the cell to actively probe substrate elasticity. Here, we report that a subset of long-lived and flat clathrin-coated structures (CCSs), also termed plaques, are contractility-independent mechanosensitive signaling platforms. We observed that plaques assemble in response to increasing substrate rigidity and that this is independent of FAs, actin and myosin-II activity. We show that plaque assembly depends on αvβ5 integrin, and is a consequence of frustrated endocytosis whereby αvβ5 tightly engaged with the stiff substrate locally stalls CCS dynamics. We also report that plaques serve as platforms for receptor-dependent signaling and are required for increased Erk activation and cell proliferation on stiff environments. We conclude that CCSs are mechanotransduction structures that sense substrate rigidity independently of cell contractility.
publishDate 2018
dc.date.none.fl_str_mv 2018-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/100397
Baschieri, Francesco; Dayot, Stéphane; Elkhatib, Nadia; Ly, Nathalie; Capmany, Anahi; et al.; Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures; Nature Publishing Group; Nature Communications; 9; 1; 12-2018
2041-1723
CONICET Digital
CONICET
url http://hdl.handle.net/11336/100397
identifier_str_mv Baschieri, Francesco; Dayot, Stéphane; Elkhatib, Nadia; Ly, Nathalie; Capmany, Anahi; et al.; Frustrated endocytosis controls contractility-independent mechanotransduction at clathrin-coated structures; Nature Publishing Group; Nature Communications; 9; 1; 12-2018
2041-1723
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41467-018-06367-y
info:eu-repo/semantics/altIdentifier/doi/10.1038/s41467-018-06367-y
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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