The p38/MK2/Hsp25 pathway is required for BMP-2-induced cell migration.

Background: Bone morphogenetic proteins (BMPs) have been shown to participate in the patterning and specification of several tissues and organs during development and to regulate cell growth, differentiation and migration in different cell types. BMP-mediated cell migration requires activation of th...

Descripción completa

Detalles Bibliográficos
Autores: Gamell Fullà, Cristina, Susperregui, Antonio G., Bernard, Ora, Rosa López, José Luis, Ventura Pujol, Francesc
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2011
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/21489
Acceso en línea:https://hdl.handle.net/2445/21489
Access Level:acceso abierto
Palabra clave:Morfogènesi
Proteïnes
Proliferació cel·lular
Regulació cel·lular
Morphogenesis
Proteins
Cell proliferation
Cellular control mechanisms
id ES_19dac542aa59bfcc995c68f019f7e241
oai_identifier_str oai:recercat.cat:2445/21489
network_acronym_str ES
network_name_str España
repository_id_str
spelling The p38/MK2/Hsp25 pathway is required for BMP-2-induced cell migration.Gamell Fullà, CristinaSusperregui, Antonio G.Bernard, OraRosa López, José LuisVentura Pujol, FrancescMorfogènesiProteïnesProliferació cel·lularRegulació cel·lularMorphogenesisProteinsCell proliferationCellular control mechanismsBackground: Bone morphogenetic proteins (BMPs) have been shown to participate in the patterning and specification of several tissues and organs during development and to regulate cell growth, differentiation and migration in different cell types. BMP-mediated cell migration requires activation of the small GTPase Cdc42 and LIMK1 activities. In our earlier report we showed that activation of LIMK1 also requires the activation of PAKs through Cdc42 and PI3K. However, the requirement of additional signaling is not clearly known. Methodology/Principal Findings: Activation of p38 MAPK has been shown to be relevant for a number of BMP-2¿s physiological effects. We report here that BMP-2 regulation of cell migration and actin cytoskeleton remodelling are dependent on p38 activity. BMP-2 treatment of mesenchymal cells results in activation of the p38/MK2/Hsp25 signaling pathway downstream from the BMP receptors. Moreover, chemical inhibition of p38 signaling or genetic ablation of either p38¿ or MK2 blocks the ability to activate the downstream effectors of the pathway and abolishes BMP-2-induction of cell migration. These signaling effects on p38/MK2/Hsp25 do not require the activity of either Cdc42 or PAK, whereas p38/MK2 activities do not significantly modify the BMP-2-dependent activation of LIMK1, measured by either kinase activity or with an antibody raised against phospho-threonine 508 at its activation loop. Finally, phosphorylated Hsp25 colocalizes with the BMP receptor complexes in lamellipodia and overexpression of a phosphorylation mutant form of Hsp25 is able to abolish the migration of cells in response to BMP-2. Conclusions: These results indicate that Cdc42/PAK/LIMK1 and p38/MK2/Hsp25 pathways, acting in parallel and modulating specific actin regulatory proteins, play a critical role in integrating responses during BMP-induced actin reorganization and cell migration.PLoS201220122011info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion12 p.application/pdfapplication/pdfhttps://hdl.handle.net/2445/21489Articles publicats en revistes (Ciències Fisiològiques)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0016477PLoS ONE 6(1): e16477http://dx.doi.org/10.1371/journal.pone.0016477cc-by (c) Gamell et al., 2011http://creativecommons.org/licenses/by/2.5/info:eu-repo/semantics/openAccessoai:recercat.cat:2445/214892026-05-29T05:05:01Z
dc.title.none.fl_str_mv The p38/MK2/Hsp25 pathway is required for BMP-2-induced cell migration.
title The p38/MK2/Hsp25 pathway is required for BMP-2-induced cell migration.
spellingShingle The p38/MK2/Hsp25 pathway is required for BMP-2-induced cell migration.
Gamell Fullà, Cristina
Morfogènesi
Proteïnes
Proliferació cel·lular
Regulació cel·lular
Morphogenesis
Proteins
Cell proliferation
Cellular control mechanisms
title_short The p38/MK2/Hsp25 pathway is required for BMP-2-induced cell migration.
title_full The p38/MK2/Hsp25 pathway is required for BMP-2-induced cell migration.
title_fullStr The p38/MK2/Hsp25 pathway is required for BMP-2-induced cell migration.
title_full_unstemmed The p38/MK2/Hsp25 pathway is required for BMP-2-induced cell migration.
title_sort The p38/MK2/Hsp25 pathway is required for BMP-2-induced cell migration.
dc.creator.none.fl_str_mv Gamell Fullà, Cristina
Susperregui, Antonio G.
Bernard, Ora
Rosa López, José Luis
Ventura Pujol, Francesc
author Gamell Fullà, Cristina
author_facet Gamell Fullà, Cristina
Susperregui, Antonio G.
Bernard, Ora
Rosa López, José Luis
Ventura Pujol, Francesc
author_role author
author2 Susperregui, Antonio G.
Bernard, Ora
Rosa López, José Luis
Ventura Pujol, Francesc
author2_role author
author
author
author
dc.subject.none.fl_str_mv Morfogènesi
Proteïnes
Proliferació cel·lular
Regulació cel·lular
Morphogenesis
Proteins
Cell proliferation
Cellular control mechanisms
topic Morfogènesi
Proteïnes
Proliferació cel·lular
Regulació cel·lular
Morphogenesis
Proteins
Cell proliferation
Cellular control mechanisms
description Background: Bone morphogenetic proteins (BMPs) have been shown to participate in the patterning and specification of several tissues and organs during development and to regulate cell growth, differentiation and migration in different cell types. BMP-mediated cell migration requires activation of the small GTPase Cdc42 and LIMK1 activities. In our earlier report we showed that activation of LIMK1 also requires the activation of PAKs through Cdc42 and PI3K. However, the requirement of additional signaling is not clearly known. Methodology/Principal Findings: Activation of p38 MAPK has been shown to be relevant for a number of BMP-2¿s physiological effects. We report here that BMP-2 regulation of cell migration and actin cytoskeleton remodelling are dependent on p38 activity. BMP-2 treatment of mesenchymal cells results in activation of the p38/MK2/Hsp25 signaling pathway downstream from the BMP receptors. Moreover, chemical inhibition of p38 signaling or genetic ablation of either p38¿ or MK2 blocks the ability to activate the downstream effectors of the pathway and abolishes BMP-2-induction of cell migration. These signaling effects on p38/MK2/Hsp25 do not require the activity of either Cdc42 or PAK, whereas p38/MK2 activities do not significantly modify the BMP-2-dependent activation of LIMK1, measured by either kinase activity or with an antibody raised against phospho-threonine 508 at its activation loop. Finally, phosphorylated Hsp25 colocalizes with the BMP receptor complexes in lamellipodia and overexpression of a phosphorylation mutant form of Hsp25 is able to abolish the migration of cells in response to BMP-2. Conclusions: These results indicate that Cdc42/PAK/LIMK1 and p38/MK2/Hsp25 pathways, acting in parallel and modulating specific actin regulatory proteins, play a critical role in integrating responses during BMP-induced actin reorganization and cell migration.
publishDate 2011
dc.date.none.fl_str_mv 2011
2012
2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/21489
url https://hdl.handle.net/2445/21489
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0016477
PLoS ONE 6(1): e16477
http://dx.doi.org/10.1371/journal.pone.0016477
dc.rights.none.fl_str_mv cc-by (c) Gamell et al., 2011
http://creativecommons.org/licenses/by/2.5/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Gamell et al., 2011
http://creativecommons.org/licenses/by/2.5/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 12 p.
application/pdf
application/pdf
dc.publisher.none.fl_str_mv PLoS
publisher.none.fl_str_mv PLoS
dc.source.none.fl_str_mv Articles publicats en revistes (Ciències Fisiològiques)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869404071462436864
score 15,812455

Similares en LA Referencia