Nesprins are mechanotransducers that discriminate epithelial-mesenchymal transition programs

Detalhes bibliográficos
Autor(a) principal: Déjardin, Théophile
Data de Publicação: 2020
Outros Autores: Carollo, Pietro Salvatore, Sipieter, François, Davidson, Patricia M, Seiler, Cynthia, Cuvelier, Damien, Cadot, Bruno, Sykes, Cecile, Gomes, Edgar, Borghi, Nicolas
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10451/47321
Resumo: © 2020 Déjardin et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
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spelling Nesprins are mechanotransducers that discriminate epithelial-mesenchymal transition programs© 2020 Déjardin et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).LINC complexes are transmembrane protein assemblies that physically connect the nucleoskeleton and cytoskeleton through the nuclear envelope. Dysfunctions of LINC complexes are associated with pathologies such as cancer and muscular disorders. The mechanical roles of LINC complexes are poorly understood. To address this, we used genetically encoded FRET biosensors of molecular tension in a nesprin protein of the LINC complex of fibroblastic and epithelial cells in culture. We exposed cells to mechanical, genetic, and pharmacological perturbations, mimicking a range of physiological and pathological situations. We show that nesprin experiences tension generated by the cytoskeleton and acts as a mechanical sensor of cell packing. Moreover, nesprin discriminates between inductions of partial and complete epithelial-mesenchymal transitions. We identify the implicated mechanisms, which involve α-catenin capture at the nuclear envelope by nesprin upon its relaxation, thereby regulating β-catenin transcription. Our data thus implicate LINC complex proteins as mechanotransducers that fine-tune β-catenin signaling in a manner dependent on the epithelial-mesenchymal transition program.This material is based on work supported by the Centre national de la recherche scientifique (CNRS), Agence nationale de la recherche (ANR; grants ANR-13-JSV5-0007 and ANR-14-CE09-0006), France BioImaging (ANR-10-INBS-04), la Ligue contre le Cancer (REMX17751 to P.M. Davidson), and the Fondation ARC pour la Recherche sur le Cancer (PDF20161205227 to P.M. Davidson). P.S. Carollo has received funding from the European Union’s Horizon 2020 Framework Programme for Research and Innovation (Marie Skłodowska-Curie grant agreement 665850-INSPIRE) and acknowledges the Ecole Doctorale Frontières de l'Innovation en Recherche et Éducation (FIRE) Programme Bettencourt. E.R. Gomes was supported by a European Research Council consolidator grant (617676).Rockefeller University PressRepositório da Universidade de LisboaDéjardin, ThéophileCarollo, Pietro SalvatoreSipieter, FrançoisDavidson, Patricia MSeiler, CynthiaCuvelier, DamienCadot, BrunoSykes, CecileGomes, EdgarBorghi, Nicolas2021-04-09T15:56:24Z20202020-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/47321engJ Cell Biol. 2020 Oct 5;219(10):e2019080360021-952510.1083/jcb.2019080361540-8140info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-08T16:50:10Zoai:repositorio.ul.pt:10451/47321Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:59:24.064369Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Nesprins are mechanotransducers that discriminate epithelial-mesenchymal transition programs
title Nesprins are mechanotransducers that discriminate epithelial-mesenchymal transition programs
spellingShingle Nesprins are mechanotransducers that discriminate epithelial-mesenchymal transition programs
Déjardin, Théophile
title_short Nesprins are mechanotransducers that discriminate epithelial-mesenchymal transition programs
title_full Nesprins are mechanotransducers that discriminate epithelial-mesenchymal transition programs
title_fullStr Nesprins are mechanotransducers that discriminate epithelial-mesenchymal transition programs
title_full_unstemmed Nesprins are mechanotransducers that discriminate epithelial-mesenchymal transition programs
title_sort Nesprins are mechanotransducers that discriminate epithelial-mesenchymal transition programs
author Déjardin, Théophile
author_facet Déjardin, Théophile
Carollo, Pietro Salvatore
Sipieter, François
Davidson, Patricia M
Seiler, Cynthia
Cuvelier, Damien
Cadot, Bruno
Sykes, Cecile
Gomes, Edgar
Borghi, Nicolas
author_role author
author2 Carollo, Pietro Salvatore
Sipieter, François
Davidson, Patricia M
Seiler, Cynthia
Cuvelier, Damien
Cadot, Bruno
Sykes, Cecile
Gomes, Edgar
Borghi, Nicolas
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Repositório da Universidade de Lisboa
dc.contributor.author.fl_str_mv Déjardin, Théophile
Carollo, Pietro Salvatore
Sipieter, François
Davidson, Patricia M
Seiler, Cynthia
Cuvelier, Damien
Cadot, Bruno
Sykes, Cecile
Gomes, Edgar
Borghi, Nicolas
description © 2020 Déjardin et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
publishDate 2020
dc.date.none.fl_str_mv 2020
2020-01-01T00:00:00Z
2021-04-09T15:56:24Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10451/47321
url http://hdl.handle.net/10451/47321
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv J Cell Biol. 2020 Oct 5;219(10):e201908036
0021-9525
10.1083/jcb.201908036
1540-8140
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Rockefeller University Press
publisher.none.fl_str_mv Rockefeller University Press
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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