Control of MT1-MMP transport by atypical PKC during breast-cancer progression

Autores
Rossé, Carine; Lodillinsky, Catalina; Fuhrmann, Laetitia; Nourieh, Maya; Monteiro, Pedro; Irondelle, Marie; Lagoutte, Emilie; Vacher, Sophie; Waharte, François; Paul Gilloteaux, Perrine; Romao, Maryse; Sengmanivong, Lucie; Linch, Mark; Van Lint, Johan; Raposo, Graça; Vincent Salomon, Anne; Bièche, Ivan; Parker, Peter J.; Chavrier, Philippe
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Dissemination of carcinoma cells requires the pericellular degradation of the extracellular matrix, which is mediated by membrane type 1-matrix metalloproteinase (MT1-MMP). In this article, we report a co–up-regulation and colocalization of MT1-MMP and atypical protein kinase C iota (aPKCι) in hormone receptor-negative breast tumors in association with a higher risk of metastasis. Silencing of aPKC in invasive breast-tumor cell lines impaired the delivery of MT1-MMP from late endocytic storage compartments to the surface and inhibited matrix degradation and invasion. We provide evidence that aPKCι, in association with MT1-MMP–containing endosomes, phosphorylates cortactin, which is present in F-actin–rich puncta on MT1-MMP–positive endosomes and regulates cortactin association with the membrane scission protein dynamin-2. Thus, cell line-based observations and clinical data reveal the concerted activity of aPKC, cortactin, and dynamin-2, which control the trafficking of MT1-MMP from late endosome to the plasma membrane and play an important role in the invasive potential of breast-cancer cells. membrane traffic actin cytoskeleton multi-vesicular body MMP14
Fil: Rossé, Carine. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Lodillinsky, Catalina. Institute Curie; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Fuhrmann, Laetitia. Institute Curie; Francia
Fil: Nourieh, Maya. Institute Curie; Francia
Fil: Monteiro, Pedro. Institute Curie; Francia. Universite Pierre et Marie Curie; Francia. Universite de Paris Vi; Francia
Fil: Irondelle, Marie. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Lagoutte, Emilie. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Vacher, Sophie. Institute Curie; Francia
Fil: Waharte, François. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Paul Gilloteaux, Perrine. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Romao, Maryse. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Sengmanivong, Lucie. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Linch, Mark. Cancer Research UK London Research Institute; Reino Unido
Fil: Van Lint, Johan. Katholikie Universiteit Leuven; Bélgica
Fil: Raposo, Graça. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Vincent Salomon, Anne. Institute Curie; Francia. Katholikie Universiteit Leuven; Bélgica
Fil: Bièche, Ivan. Institute Curie; Francia
Fil: Parker, Peter J.. Cancer Research UK London Research Institute; Reino Unido. King’s College London; Reino Unido
Fil: Chavrier, Philippe. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Materia
Breast cancer
Tumor invasion
MT1-MMP
Atypical PKC
Membrane traffic
Actin cytoskeleton
Multi vesicular body
MMP14
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/16981
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/16981
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Control of MT1-MMP transport by atypical PKC during breast-cancer progressionRossé, CarineLodillinsky, CatalinaFuhrmann, LaetitiaNourieh, MayaMonteiro, PedroIrondelle, MarieLagoutte, EmilieVacher, SophieWaharte, FrançoisPaul Gilloteaux, PerrineRomao, MaryseSengmanivong, LucieLinch, MarkVan Lint, JohanRaposo, GraçaVincent Salomon, AnneBièche, IvanParker, Peter J.Chavrier, PhilippeBreast cancerTumor invasionMT1-MMPAtypical PKCMembrane trafficActin cytoskeletonMulti vesicular bodyMMP14https://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Dissemination of carcinoma cells requires the pericellular degradation of the extracellular matrix, which is mediated by membrane type 1-matrix metalloproteinase (MT1-MMP). In this article, we report a co–up-regulation and colocalization of MT1-MMP and atypical protein kinase C iota (aPKCι) in hormone receptor-negative breast tumors in association with a higher risk of metastasis. Silencing of aPKC in invasive breast-tumor cell lines impaired the delivery of MT1-MMP from late endocytic storage compartments to the surface and inhibited matrix degradation and invasion. We provide evidence that aPKCι, in association with MT1-MMP–containing endosomes, phosphorylates cortactin, which is present in F-actin–rich puncta on MT1-MMP–positive endosomes and regulates cortactin association with the membrane scission protein dynamin-2. Thus, cell line-based observations and clinical data reveal the concerted activity of aPKC, cortactin, and dynamin-2, which control the trafficking of MT1-MMP from late endosome to the plasma membrane and play an important role in the invasive potential of breast-cancer cells. membrane traffic actin cytoskeleton multi-vesicular body MMP14Fil: Rossé, Carine. Institute Curie; Francia. Centre National de la Recherche Scientifique; FranciaFil: Lodillinsky, Catalina. Institute Curie; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Fuhrmann, Laetitia. Institute Curie; FranciaFil: Nourieh, Maya. Institute Curie; FranciaFil: Monteiro, Pedro. Institute Curie; Francia. Universite Pierre et Marie Curie; Francia. Universite de Paris Vi; FranciaFil: Irondelle, Marie. Institute Curie; Francia. Centre National de la Recherche Scientifique; FranciaFil: Lagoutte, Emilie. Institute Curie; Francia. Centre National de la Recherche Scientifique; FranciaFil: Vacher, Sophie. Institute Curie; FranciaFil: Waharte, François. Institute Curie; Francia. Centre National de la Recherche Scientifique; FranciaFil: Paul Gilloteaux, Perrine. Institute Curie; Francia. Centre National de la Recherche Scientifique; FranciaFil: Romao, Maryse. Institute Curie; Francia. Centre National de la Recherche Scientifique; FranciaFil: Sengmanivong, Lucie. Institute Curie; Francia. Centre National de la Recherche Scientifique; FranciaFil: Linch, Mark. Cancer Research UK London Research Institute; Reino UnidoFil: Van Lint, Johan. Katholikie Universiteit Leuven; BélgicaFil: Raposo, Graça. Institute Curie; Francia. Centre National de la Recherche Scientifique; FranciaFil: Vincent Salomon, Anne. Institute Curie; Francia. Katholikie Universiteit Leuven; BélgicaFil: Bièche, Ivan. Institute Curie; FranciaFil: Parker, Peter J.. Cancer Research UK London Research Institute; Reino Unido. King’s College London; Reino UnidoFil: Chavrier, Philippe. Institute Curie; Francia. Centre National de la Recherche Scientifique; FranciaNational Academy of Sciences2014-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/16981Rossé, Carine; Lodillinsky, Catalina; Fuhrmann, Laetitia; Nourieh, Maya; Monteiro, Pedro; et al.; Control of MT1-MMP transport by atypical PKC during breast-cancer progression; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 111; 18; 5-2014; 1872-18790027-8424enginfo:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.1400749111info:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/111/18/E1872.fullinfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4020077/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:34:32Zoai:ri.conicet.gov.ar:11336/16981instacron: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:34982025-09-29 09:34:33.134CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Control of MT1-MMP transport by atypical PKC during breast-cancer progression
title Control of MT1-MMP transport by atypical PKC during breast-cancer progression
spellingShingle Control of MT1-MMP transport by atypical PKC during breast-cancer progression
Rossé, Carine
Breast cancer
Tumor invasion
MT1-MMP
Atypical PKC
Membrane traffic
Actin cytoskeleton
Multi vesicular body
MMP14
title_short Control of MT1-MMP transport by atypical PKC during breast-cancer progression
title_full Control of MT1-MMP transport by atypical PKC during breast-cancer progression
title_fullStr Control of MT1-MMP transport by atypical PKC during breast-cancer progression
title_full_unstemmed Control of MT1-MMP transport by atypical PKC during breast-cancer progression
title_sort Control of MT1-MMP transport by atypical PKC during breast-cancer progression
dc.creator.none.fl_str_mv Rossé, Carine
Lodillinsky, Catalina
Fuhrmann, Laetitia
Nourieh, Maya
Monteiro, Pedro
Irondelle, Marie
Lagoutte, Emilie
Vacher, Sophie
Waharte, François
Paul Gilloteaux, Perrine
Romao, Maryse
Sengmanivong, Lucie
Linch, Mark
Van Lint, Johan
Raposo, Graça
Vincent Salomon, Anne
Bièche, Ivan
Parker, Peter J.
Chavrier, Philippe
author Rossé, Carine
author_facet Rossé, Carine
Lodillinsky, Catalina
Fuhrmann, Laetitia
Nourieh, Maya
Monteiro, Pedro
Irondelle, Marie
Lagoutte, Emilie
Vacher, Sophie
Waharte, François
Paul Gilloteaux, Perrine
Romao, Maryse
Sengmanivong, Lucie
Linch, Mark
Van Lint, Johan
Raposo, Graça
Vincent Salomon, Anne
Bièche, Ivan
Parker, Peter J.
Chavrier, Philippe
author_role author
author2 Lodillinsky, Catalina
Fuhrmann, Laetitia
Nourieh, Maya
Monteiro, Pedro
Irondelle, Marie
Lagoutte, Emilie
Vacher, Sophie
Waharte, François
Paul Gilloteaux, Perrine
Romao, Maryse
Sengmanivong, Lucie
Linch, Mark
Van Lint, Johan
Raposo, Graça
Vincent Salomon, Anne
Bièche, Ivan
Parker, Peter J.
Chavrier, Philippe
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Breast cancer
Tumor invasion
MT1-MMP
Atypical PKC
Membrane traffic
Actin cytoskeleton
Multi vesicular body
MMP14
topic Breast cancer
Tumor invasion
MT1-MMP
Atypical PKC
Membrane traffic
Actin cytoskeleton
Multi vesicular body
MMP14
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Dissemination of carcinoma cells requires the pericellular degradation of the extracellular matrix, which is mediated by membrane type 1-matrix metalloproteinase (MT1-MMP). In this article, we report a co–up-regulation and colocalization of MT1-MMP and atypical protein kinase C iota (aPKCι) in hormone receptor-negative breast tumors in association with a higher risk of metastasis. Silencing of aPKC in invasive breast-tumor cell lines impaired the delivery of MT1-MMP from late endocytic storage compartments to the surface and inhibited matrix degradation and invasion. We provide evidence that aPKCι, in association with MT1-MMP–containing endosomes, phosphorylates cortactin, which is present in F-actin–rich puncta on MT1-MMP–positive endosomes and regulates cortactin association with the membrane scission protein dynamin-2. Thus, cell line-based observations and clinical data reveal the concerted activity of aPKC, cortactin, and dynamin-2, which control the trafficking of MT1-MMP from late endosome to the plasma membrane and play an important role in the invasive potential of breast-cancer cells. membrane traffic actin cytoskeleton multi-vesicular body MMP14
Fil: Rossé, Carine. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Lodillinsky, Catalina. Institute Curie; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Fuhrmann, Laetitia. Institute Curie; Francia
Fil: Nourieh, Maya. Institute Curie; Francia
Fil: Monteiro, Pedro. Institute Curie; Francia. Universite Pierre et Marie Curie; Francia. Universite de Paris Vi; Francia
Fil: Irondelle, Marie. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Lagoutte, Emilie. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Vacher, Sophie. Institute Curie; Francia
Fil: Waharte, François. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Paul Gilloteaux, Perrine. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Romao, Maryse. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Sengmanivong, Lucie. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Linch, Mark. Cancer Research UK London Research Institute; Reino Unido
Fil: Van Lint, Johan. Katholikie Universiteit Leuven; Bélgica
Fil: Raposo, Graça. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Vincent Salomon, Anne. Institute Curie; Francia. Katholikie Universiteit Leuven; Bélgica
Fil: Bièche, Ivan. Institute Curie; Francia
Fil: Parker, Peter J.. Cancer Research UK London Research Institute; Reino Unido. King’s College London; Reino Unido
Fil: Chavrier, Philippe. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia
description Dissemination of carcinoma cells requires the pericellular degradation of the extracellular matrix, which is mediated by membrane type 1-matrix metalloproteinase (MT1-MMP). In this article, we report a co–up-regulation and colocalization of MT1-MMP and atypical protein kinase C iota (aPKCι) in hormone receptor-negative breast tumors in association with a higher risk of metastasis. Silencing of aPKC in invasive breast-tumor cell lines impaired the delivery of MT1-MMP from late endocytic storage compartments to the surface and inhibited matrix degradation and invasion. We provide evidence that aPKCι, in association with MT1-MMP–containing endosomes, phosphorylates cortactin, which is present in F-actin–rich puncta on MT1-MMP–positive endosomes and regulates cortactin association with the membrane scission protein dynamin-2. Thus, cell line-based observations and clinical data reveal the concerted activity of aPKC, cortactin, and dynamin-2, which control the trafficking of MT1-MMP from late endosome to the plasma membrane and play an important role in the invasive potential of breast-cancer cells. membrane traffic actin cytoskeleton multi-vesicular body MMP14
publishDate 2014
dc.date.none.fl_str_mv 2014-05
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/11336/16981
Rossé, Carine; Lodillinsky, Catalina; Fuhrmann, Laetitia; Nourieh, Maya; Monteiro, Pedro; et al.; Control of MT1-MMP transport by atypical PKC during breast-cancer progression; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 111; 18; 5-2014; 1872-1879
0027-8424
url http://hdl.handle.net/11336/16981
identifier_str_mv Rossé, Carine; Lodillinsky, Catalina; Fuhrmann, Laetitia; Nourieh, Maya; Monteiro, Pedro; et al.; Control of MT1-MMP transport by atypical PKC during breast-cancer progression; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 111; 18; 5-2014; 1872-1879
0027-8424
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.1400749111
info:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/111/18/E1872.full
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4020077/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv National Academy of Sciences
publisher.none.fl_str_mv National Academy of Sciences
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 13.070432

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