ER-bound PTP1B is targeted to newly forming cell-matrix adhesions

Autores
Hernandez, Mariana Vanesa; Davies Sala, María Georgina; Balsamo, Janne; Lilien, Jack; Arregui, Carlos Oscar
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Here, we define the mechanism through which protein tyrosine phosphatase 1B (PTP1B) is targeted to cell-matrix adhesion sites. Green fluorescent protein (GFP)-labeled PTP1B bearing the substrate-trapping mutation D181A was found in punctate structures in lamellae. The puncta co-localized with focal adhesion kinase (FAK) and Src, and defined the distal tips of cell-matrix adhesion sites identified with paxillin and vinculin. PTP1B is largely associated with the external face of the endoplasmic reticulum (ER) and the puncta develop from ER projections over cell-matrix adhesion sites, a process dependent on microtubules. Deletion of the ER-targeting sequence resulted in cytosolic localization and altered the distribution of PTP1B at cell-matrix foci, whereas mutations disrupting interactions with Src homology 3 (SH3) domains, and the insulin and cadherin receptors had no effect. PTP1B recognizes substrates within forming adhesion foci as revealed by its preferential association with paxillin as opposed to zyxin-containing foci. Our results suggest that PTP1B targets to immature cell-matrix foci in newly forming lamellae by dynamic extensions of the ER and contributes to the maturation of these sites.
Fil: Hernandez, Mariana Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Davies Sala, María Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Balsamo, Janne. University of Iowa; Estados Unidos
Fil: Lilien, Jack. University of Iowa; Estados Unidos
Fil: Arregui, Carlos Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Materia
FOSFATASA DE TIROSINA PTP1B
ADESION CELULA-MATRIZ
RETICULO ENDOPLASMATICO
SEÑALIZACION DE INTEGRINAS
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:11336/41566
Acceder
id CONICETDig_ed75a292311a1781ba3f2a28e419ac49
oai_identifier_str oai:ri.conicet.gov.ar:11336/41566
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling ER-bound PTP1B is targeted to newly forming cell-matrix adhesionsHernandez, Mariana VanesaDavies Sala, María GeorginaBalsamo, JanneLilien, JackArregui, Carlos OscarFOSFATASA DE TIROSINA PTP1BADESION CELULA-MATRIZRETICULO ENDOPLASMATICOSEÑALIZACION DE INTEGRINAShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Here, we define the mechanism through which protein tyrosine phosphatase 1B (PTP1B) is targeted to cell-matrix adhesion sites. Green fluorescent protein (GFP)-labeled PTP1B bearing the substrate-trapping mutation D181A was found in punctate structures in lamellae. The puncta co-localized with focal adhesion kinase (FAK) and Src, and defined the distal tips of cell-matrix adhesion sites identified with paxillin and vinculin. PTP1B is largely associated with the external face of the endoplasmic reticulum (ER) and the puncta develop from ER projections over cell-matrix adhesion sites, a process dependent on microtubules. Deletion of the ER-targeting sequence resulted in cytosolic localization and altered the distribution of PTP1B at cell-matrix foci, whereas mutations disrupting interactions with Src homology 3 (SH3) domains, and the insulin and cadherin receptors had no effect. PTP1B recognizes substrates within forming adhesion foci as revealed by its preferential association with paxillin as opposed to zyxin-containing foci. Our results suggest that PTP1B targets to immature cell-matrix foci in newly forming lamellae by dynamic extensions of the ER and contributes to the maturation of these sites.Fil: Hernandez, Mariana Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Davies Sala, María Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Balsamo, Janne. University of Iowa; Estados UnidosFil: Lilien, Jack. University of Iowa; Estados UnidosFil: Arregui, Carlos Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaCompany of Biologists2006-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/41566Hernandez, Mariana Vanesa; Davies Sala, María Georgina; Balsamo, Janne; Lilien, Jack; Arregui, Carlos Oscar; ER-bound PTP1B is targeted to newly forming cell-matrix adhesions; Company of Biologists; Journal of Cell Science; 119; 7; 4-2006; 1233-12430021-95331477-9137CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://jcs.biologists.org/content/119/7/1233.longinfo:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.02846info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-12T09:38:09Zoai:ri.conicet.gov.ar:11336/41566instacron: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:34982025-11-12 09:38:09.843CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
title ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
spellingShingle ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
Hernandez, Mariana Vanesa
FOSFATASA DE TIROSINA PTP1B
ADESION CELULA-MATRIZ
RETICULO ENDOPLASMATICO
SEÑALIZACION DE INTEGRINAS
title_short ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
title_full ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
title_fullStr ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
title_full_unstemmed ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
title_sort ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
dc.creator.none.fl_str_mv Hernandez, Mariana Vanesa
Davies Sala, María Georgina
Balsamo, Janne
Lilien, Jack
Arregui, Carlos Oscar
author Hernandez, Mariana Vanesa
author_facet Hernandez, Mariana Vanesa
Davies Sala, María Georgina
Balsamo, Janne
Lilien, Jack
Arregui, Carlos Oscar
author_role author
author2 Davies Sala, María Georgina
Balsamo, Janne
Lilien, Jack
Arregui, Carlos Oscar
author2_role author
author
author
author
dc.subject.none.fl_str_mv FOSFATASA DE TIROSINA PTP1B
ADESION CELULA-MATRIZ
RETICULO ENDOPLASMATICO
SEÑALIZACION DE INTEGRINAS
topic FOSFATASA DE TIROSINA PTP1B
ADESION CELULA-MATRIZ
RETICULO ENDOPLASMATICO
SEÑALIZACION DE INTEGRINAS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Here, we define the mechanism through which protein tyrosine phosphatase 1B (PTP1B) is targeted to cell-matrix adhesion sites. Green fluorescent protein (GFP)-labeled PTP1B bearing the substrate-trapping mutation D181A was found in punctate structures in lamellae. The puncta co-localized with focal adhesion kinase (FAK) and Src, and defined the distal tips of cell-matrix adhesion sites identified with paxillin and vinculin. PTP1B is largely associated with the external face of the endoplasmic reticulum (ER) and the puncta develop from ER projections over cell-matrix adhesion sites, a process dependent on microtubules. Deletion of the ER-targeting sequence resulted in cytosolic localization and altered the distribution of PTP1B at cell-matrix foci, whereas mutations disrupting interactions with Src homology 3 (SH3) domains, and the insulin and cadherin receptors had no effect. PTP1B recognizes substrates within forming adhesion foci as revealed by its preferential association with paxillin as opposed to zyxin-containing foci. Our results suggest that PTP1B targets to immature cell-matrix foci in newly forming lamellae by dynamic extensions of the ER and contributes to the maturation of these sites.
Fil: Hernandez, Mariana Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Davies Sala, María Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Balsamo, Janne. University of Iowa; Estados Unidos
Fil: Lilien, Jack. University of Iowa; Estados Unidos
Fil: Arregui, Carlos Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
description Here, we define the mechanism through which protein tyrosine phosphatase 1B (PTP1B) is targeted to cell-matrix adhesion sites. Green fluorescent protein (GFP)-labeled PTP1B bearing the substrate-trapping mutation D181A was found in punctate structures in lamellae. The puncta co-localized with focal adhesion kinase (FAK) and Src, and defined the distal tips of cell-matrix adhesion sites identified with paxillin and vinculin. PTP1B is largely associated with the external face of the endoplasmic reticulum (ER) and the puncta develop from ER projections over cell-matrix adhesion sites, a process dependent on microtubules. Deletion of the ER-targeting sequence resulted in cytosolic localization and altered the distribution of PTP1B at cell-matrix foci, whereas mutations disrupting interactions with Src homology 3 (SH3) domains, and the insulin and cadherin receptors had no effect. PTP1B recognizes substrates within forming adhesion foci as revealed by its preferential association with paxillin as opposed to zyxin-containing foci. Our results suggest that PTP1B targets to immature cell-matrix foci in newly forming lamellae by dynamic extensions of the ER and contributes to the maturation of these sites.
publishDate 2006
dc.date.none.fl_str_mv 2006-04
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/11336/41566
Hernandez, Mariana Vanesa; Davies Sala, María Georgina; Balsamo, Janne; Lilien, Jack; Arregui, Carlos Oscar; ER-bound PTP1B is targeted to newly forming cell-matrix adhesions; Company of Biologists; Journal of Cell Science; 119; 7; 4-2006; 1233-1243
0021-9533
1477-9137
CONICET Digital
CONICET
url http://hdl.handle.net/11336/41566
identifier_str_mv Hernandez, Mariana Vanesa; Davies Sala, María Georgina; Balsamo, Janne; Lilien, Jack; Arregui, Carlos Oscar; ER-bound PTP1B is targeted to newly forming cell-matrix adhesions; Company of Biologists; Journal of Cell Science; 119; 7; 4-2006; 1233-1243
0021-9533
1477-9137
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://jcs.biologists.org/content/119/7/1233.long
info:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.02846
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Company of Biologists
publisher.none.fl_str_mv Company of Biologists
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 12.976206

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