The formin INF2 regulates basolateral-to-apical transcytosis and lumen formation in association with Cdc42 and MAL2

Transcytosis is a widespread pathway for apical targeting in epithelial cells. MAL2, an essential protein of the machinery for apical transcytosis, functions by shuttling in vesicular carriers between the apical zone and the cell periphery. We have identified INF2, an atypical formin with actin poly...

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Autores: Madrid González, Ricardo, Aranda Gómez, Juan Francisco, Rodríguez Fraticelli, Alejo, Ventimiglia, Leandro, Andrés Delgado, Laura, Shehata, Mona, Fanayan, Susan, Shahheydari, Hamideh, Gómez, Sergio, Jiménez, Alberto, Martín Belmonte, Fernando, Byrne, Jennifer Anne, Alonso, Miguel
Tipo de recurso: artículo
Fecha de publicación:2010
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/99128
Acceso en línea:https://hdl.handle.net/20.500.14352/99128
Access Level:acceso abierto
Palabra clave:577.112
Bioquímica (Biología)
2403 Bioquímica
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spelling The formin INF2 regulates basolateral-to-apical transcytosis and lumen formation in association with Cdc42 and MAL2Madrid González, RicardoAranda Gómez, Juan FranciscoRodríguez Fraticelli, AlejoVentimiglia, LeandroAndrés Delgado, LauraShehata, MonaFanayan, SusanShahheydari, HamidehGómez, SergioJiménez, AlbertoMartín Belmonte, FernandoByrne, Jennifer AnneAlonso, Miguel577.112Bioquímica (Biología)2403 BioquímicaTranscytosis is a widespread pathway for apical targeting in epithelial cells. MAL2, an essential protein of the machinery for apical transcytosis, functions by shuttling in vesicular carriers between the apical zone and the cell periphery. We have identified INF2, an atypical formin with actin polymerization and depolymerization activities, which is a binding partner of MAL2. MAL2-positive vesicular carriers associate with short actin filaments during transcytosis in a process requiring INF2. INF2 binds Cdc42 in a GTP-loaded-dependent manner. Cdc42 and INF2 regulate MAL2 dynamics and are necessary for apical transcytosis and the formation of lateral lumens in hepatoma HepG2 cells. INF2 and MAL2 are also essential for the formation of the central lumen in organotypic cultures of epithelial MDCK cells. Our results reveal a functional mechanism whereby Cdc42, INF2, and MAL2 are sequentially ordered in a pathway dedicated to the regulation of transcytosis and lumen formation.ElsevierUniversidad Complutense de Madrid20102010-01-0120102010-01-01journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/99128reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/991282026-06-02T12:44:21Z
dc.title.none.fl_str_mv The formin INF2 regulates basolateral-to-apical transcytosis and lumen formation in association with Cdc42 and MAL2
title The formin INF2 regulates basolateral-to-apical transcytosis and lumen formation in association with Cdc42 and MAL2
spellingShingle The formin INF2 regulates basolateral-to-apical transcytosis and lumen formation in association with Cdc42 and MAL2
Madrid González, Ricardo
577.112
Bioquímica (Biología)
2403 Bioquímica
title_short The formin INF2 regulates basolateral-to-apical transcytosis and lumen formation in association with Cdc42 and MAL2
title_full The formin INF2 regulates basolateral-to-apical transcytosis and lumen formation in association with Cdc42 and MAL2
title_fullStr The formin INF2 regulates basolateral-to-apical transcytosis and lumen formation in association with Cdc42 and MAL2
title_full_unstemmed The formin INF2 regulates basolateral-to-apical transcytosis and lumen formation in association with Cdc42 and MAL2
title_sort The formin INF2 regulates basolateral-to-apical transcytosis and lumen formation in association with Cdc42 and MAL2
dc.creator.none.fl_str_mv Madrid González, Ricardo
Aranda Gómez, Juan Francisco
Rodríguez Fraticelli, Alejo
Ventimiglia, Leandro
Andrés Delgado, Laura
Shehata, Mona
Fanayan, Susan
Shahheydari, Hamideh
Gómez, Sergio
Jiménez, Alberto
Martín Belmonte, Fernando
Byrne, Jennifer Anne
Alonso, Miguel
author Madrid González, Ricardo
author_facet Madrid González, Ricardo
Aranda Gómez, Juan Francisco
Rodríguez Fraticelli, Alejo
Ventimiglia, Leandro
Andrés Delgado, Laura
Shehata, Mona
Fanayan, Susan
Shahheydari, Hamideh
Gómez, Sergio
Jiménez, Alberto
Martín Belmonte, Fernando
Byrne, Jennifer Anne
Alonso, Miguel
author_role author
author2 Aranda Gómez, Juan Francisco
Rodríguez Fraticelli, Alejo
Ventimiglia, Leandro
Andrés Delgado, Laura
Shehata, Mona
Fanayan, Susan
Shahheydari, Hamideh
Gómez, Sergio
Jiménez, Alberto
Martín Belmonte, Fernando
Byrne, Jennifer Anne
Alonso, Miguel
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 577.112
Bioquímica (Biología)
2403 Bioquímica
topic 577.112
Bioquímica (Biología)
2403 Bioquímica
description Transcytosis is a widespread pathway for apical targeting in epithelial cells. MAL2, an essential protein of the machinery for apical transcytosis, functions by shuttling in vesicular carriers between the apical zone and the cell periphery. We have identified INF2, an atypical formin with actin polymerization and depolymerization activities, which is a binding partner of MAL2. MAL2-positive vesicular carriers associate with short actin filaments during transcytosis in a process requiring INF2. INF2 binds Cdc42 in a GTP-loaded-dependent manner. Cdc42 and INF2 regulate MAL2 dynamics and are necessary for apical transcytosis and the formation of lateral lumens in hepatoma HepG2 cells. INF2 and MAL2 are also essential for the formation of the central lumen in organotypic cultures of epithelial MDCK cells. Our results reveal a functional mechanism whereby Cdc42, INF2, and MAL2 are sequentially ordered in a pathway dedicated to the regulation of transcytosis and lumen formation.
publishDate 2010
dc.date.none.fl_str_mv 2010
2010-01-01
2010
2010-01-01
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/20.500.14352/99128
url https://hdl.handle.net/20.500.14352/99128
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
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
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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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