Activation of the Rac-binding Partner FHOD1 Induces Actin Stress Fibers via a ROCK-dependent Mechanism

Diaphanous related formins (DRFs) are part of the formin protein family that control morphogenesis, embryonic differentiation, cytokinesis, and cell polarity. DRFs organize the cytoskeleton in eukaryotic cells via the interaction with specific members of the Rho family of small GTPases including Rho...

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Detalhes bibliográficos
Autores: Gasteier, Judith, Madrid González, Ricardo, Krautkrämer, Ellen, Schröder, Sebastian, Muranyi, Walter, Benichou, Serge, Fackler, Oliver
Tipo de documento: artigo
Data de publicação:2003
País:España
Recursos:Universidad Complutense de Madrid (UCM)
Repositório:Docta Complutense
Idioma:inglês
OAI Identifier:oai:docta.ucm.es:20.500.14352/98035
Acesso em linha:https://hdl.handle.net/20.500.14352/98035
Access Level:Acceso aberto
Palavra-chave:576
Biología celular (Biología)
2407 Biología Celular
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oai_identifier_str oai:docta.ucm.es:20.500.14352/98035
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spelling Activation of the Rac-binding Partner FHOD1 Induces Actin Stress Fibers via a ROCK-dependent MechanismGasteier, JudithMadrid González, RicardoKrautkrämer, EllenSchröder, SebastianMuranyi, WalterBenichou, SergeFackler, Oliver576Biología celular (Biología)2407 Biología CelularDiaphanous related formins (DRFs) are part of the formin protein family that control morphogenesis, embryonic differentiation, cytokinesis, and cell polarity. DRFs organize the cytoskeleton in eukaryotic cells via the interaction with specific members of the Rho family of small GTPases including Rho, Rac, and Cdc42. This is best understood for Rho, which transmits signals to the actin cytoskeleton through the cooperation of its DRF effector mDia with ROCK (Rho-associated kinase). Here, we show that a constitutive active form of the Rac-interacting DRF FHOD1 (formin homology 2 domain containing 1) associates with F-actin in NIH3T3 cells, resulting in the formation of thick actin fibers. Cytoskeletal changes induced by FHOD1 correlated with the induction of serum response element transcription and were mediated by formin homology domains 1 and 2 of FHOD1. FHOD1-induced effects required the activity of the Rho-ROCK cascade that is targeted at a level downstream of Rho by the DRF. However, when the functional interaction of FHOD1 with individual GTPases was addressed, Rac but not Rho or Cdc42 bound to FHOD1 in cells and induced its recruitment to actin filaments and lamellipodia/membrane ruffles. Furthermore, activated FHOD1 interfered with lamellipodia formation. These results indicate that FHOD1 acts as an effector of Rac in actin rearrangements and transcriptional regulation and may provide a link for the Rac-dependent activation of the Rho cascade.The American Society for Biochemistry and Molecular Biology, Inc.Universidad Complutense de Madrid20032003-01-0120032003-01-01journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/98035reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/980352026-06-02T12:44:21Z
dc.title.none.fl_str_mv Activation of the Rac-binding Partner FHOD1 Induces Actin Stress Fibers via a ROCK-dependent Mechanism
title Activation of the Rac-binding Partner FHOD1 Induces Actin Stress Fibers via a ROCK-dependent Mechanism
spellingShingle Activation of the Rac-binding Partner FHOD1 Induces Actin Stress Fibers via a ROCK-dependent Mechanism
Gasteier, Judith
576
Biología celular (Biología)
2407 Biología Celular
title_short Activation of the Rac-binding Partner FHOD1 Induces Actin Stress Fibers via a ROCK-dependent Mechanism
title_full Activation of the Rac-binding Partner FHOD1 Induces Actin Stress Fibers via a ROCK-dependent Mechanism
title_fullStr Activation of the Rac-binding Partner FHOD1 Induces Actin Stress Fibers via a ROCK-dependent Mechanism
title_full_unstemmed Activation of the Rac-binding Partner FHOD1 Induces Actin Stress Fibers via a ROCK-dependent Mechanism
title_sort Activation of the Rac-binding Partner FHOD1 Induces Actin Stress Fibers via a ROCK-dependent Mechanism
dc.creator.none.fl_str_mv Gasteier, Judith
Madrid González, Ricardo
Krautkrämer, Ellen
Schröder, Sebastian
Muranyi, Walter
Benichou, Serge
Fackler, Oliver
author Gasteier, Judith
author_facet Gasteier, Judith
Madrid González, Ricardo
Krautkrämer, Ellen
Schröder, Sebastian
Muranyi, Walter
Benichou, Serge
Fackler, Oliver
author_role author
author2 Madrid González, Ricardo
Krautkrämer, Ellen
Schröder, Sebastian
Muranyi, Walter
Benichou, Serge
Fackler, Oliver
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 576
Biología celular (Biología)
2407 Biología Celular
topic 576
Biología celular (Biología)
2407 Biología Celular
description Diaphanous related formins (DRFs) are part of the formin protein family that control morphogenesis, embryonic differentiation, cytokinesis, and cell polarity. DRFs organize the cytoskeleton in eukaryotic cells via the interaction with specific members of the Rho family of small GTPases including Rho, Rac, and Cdc42. This is best understood for Rho, which transmits signals to the actin cytoskeleton through the cooperation of its DRF effector mDia with ROCK (Rho-associated kinase). Here, we show that a constitutive active form of the Rac-interacting DRF FHOD1 (formin homology 2 domain containing 1) associates with F-actin in NIH3T3 cells, resulting in the formation of thick actin fibers. Cytoskeletal changes induced by FHOD1 correlated with the induction of serum response element transcription and were mediated by formin homology domains 1 and 2 of FHOD1. FHOD1-induced effects required the activity of the Rho-ROCK cascade that is targeted at a level downstream of Rho by the DRF. However, when the functional interaction of FHOD1 with individual GTPases was addressed, Rac but not Rho or Cdc42 bound to FHOD1 in cells and induced its recruitment to actin filaments and lamellipodia/membrane ruffles. Furthermore, activated FHOD1 interfered with lamellipodia formation. These results indicate that FHOD1 acts as an effector of Rac in actin rearrangements and transcriptional regulation and may provide a link for the Rac-dependent activation of the Rho cascade.
publishDate 2003
dc.date.none.fl_str_mv 2003
2003-01-01
2003
2003-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/98035
url https://hdl.handle.net/20.500.14352/98035
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv The American Society for Biochemistry and Molecular Biology, Inc.
publisher.none.fl_str_mv The American Society for Biochemistry and Molecular Biology, Inc.
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300724

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