Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes

Autores
Ambroggio, Ernesto Esteban; Sillibourne, James; Bruno, Antonny; Manneville, Jean-Baptiste; Bruno, Goud
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Arfaptin2 contains a Bin/Amphiphysin/Rvs (BAR) domain and directly interacts with proteins of the Arf/Arl family in their active GTP-bound state. It has been proposed that BAR domains are able to sense membrane curvature and to induce membrane tubulation. We report here that active Arf1 is required for the recruitment of Arfaptin2 to artificial liposomes mimicking the Golgi apparatus lipid composition. The Arf1-dependent recruitment of Arfaptin2 increases with membrane curvature, while the recruitment of Arf1 itself is not sensitive to curvature. At high protein concentrations, the binding of Arfaptin2 induces membrane tubulation. Finally, membrane-bound Arfaptin2 is released from the liposome when ArfGAP1 catalyzes the hydrolysis of GTP to GDP in Arf1. These results show that both Arf1 activation and high membrane curvature are required for efficient recruitment of Arfaptin2 to membranes.
Fil: Ambroggio, Ernesto Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina
Fil: Sillibourne, James. Institute Curie; Francia
Fil: Bruno, Antonny. Université Nice Sophia Antipolis. Laboratoire Jean-alexandre Dieudonné.; Francia
Fil: Manneville, Jean-Baptiste. Institute Curie; Francia
Fil: Bruno, Goud. Institute Curie; Francia
Materia
Arfaptin2
Arf1
Guvs
Tubes
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:11336/480
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomesAmbroggio, Ernesto EstebanSillibourne, JamesBruno, AntonnyManneville, Jean-BaptisteBruno, GoudArfaptin2Arf1GuvsTubeshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Arfaptin2 contains a Bin/Amphiphysin/Rvs (BAR) domain and directly interacts with proteins of the Arf/Arl family in their active GTP-bound state. It has been proposed that BAR domains are able to sense membrane curvature and to induce membrane tubulation. We report here that active Arf1 is required for the recruitment of Arfaptin2 to artificial liposomes mimicking the Golgi apparatus lipid composition. The Arf1-dependent recruitment of Arfaptin2 increases with membrane curvature, while the recruitment of Arf1 itself is not sensitive to curvature. At high protein concentrations, the binding of Arfaptin2 induces membrane tubulation. Finally, membrane-bound Arfaptin2 is released from the liposome when ArfGAP1 catalyzes the hydrolysis of GTP to GDP in Arf1. These results show that both Arf1 activation and high membrane curvature are required for efficient recruitment of Arfaptin2 to membranes.Fil: Ambroggio, Ernesto Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; ArgentinaFil: Sillibourne, James. Institute Curie; FranciaFil: Bruno, Antonny. Université Nice Sophia Antipolis. Laboratoire Jean-alexandre Dieudonné.; FranciaFil: Manneville, Jean-Baptiste. Institute Curie; FranciaFil: Bruno, Goud. Institute Curie; FranciaPublic Library of Science2013-04-29info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/480Ambroggio, Ernesto Esteban; Sillibourne, James; Bruno, Antonny; Manneville, Jean-Baptiste; Bruno, Goud; Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes; Public Library of Science; Plos One; 8; 4; 29-4-2013; 1-61932-6203CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0062963info:eu-repo/semantics/altIdentifier/url/http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0062963info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-23T14:43:17Zoai:ri.conicet.gov.ar:11336/480instacron: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:34982025-12-23 14:43:17.496CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes
title Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes
spellingShingle Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes
Ambroggio, Ernesto Esteban
Arfaptin2
Arf1
Guvs
Tubes
title_short Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes
title_full Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes
title_fullStr Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes
title_full_unstemmed Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes
title_sort Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes
dc.creator.none.fl_str_mv Ambroggio, Ernesto Esteban
Sillibourne, James
Bruno, Antonny
Manneville, Jean-Baptiste
Bruno, Goud
author Ambroggio, Ernesto Esteban
author_facet Ambroggio, Ernesto Esteban
Sillibourne, James
Bruno, Antonny
Manneville, Jean-Baptiste
Bruno, Goud
author_role author
author2 Sillibourne, James
Bruno, Antonny
Manneville, Jean-Baptiste
Bruno, Goud
author2_role author
author
author
author
dc.subject.none.fl_str_mv Arfaptin2
Arf1
Guvs
Tubes
topic Arfaptin2
Arf1
Guvs
Tubes
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Arfaptin2 contains a Bin/Amphiphysin/Rvs (BAR) domain and directly interacts with proteins of the Arf/Arl family in their active GTP-bound state. It has been proposed that BAR domains are able to sense membrane curvature and to induce membrane tubulation. We report here that active Arf1 is required for the recruitment of Arfaptin2 to artificial liposomes mimicking the Golgi apparatus lipid composition. The Arf1-dependent recruitment of Arfaptin2 increases with membrane curvature, while the recruitment of Arf1 itself is not sensitive to curvature. At high protein concentrations, the binding of Arfaptin2 induces membrane tubulation. Finally, membrane-bound Arfaptin2 is released from the liposome when ArfGAP1 catalyzes the hydrolysis of GTP to GDP in Arf1. These results show that both Arf1 activation and high membrane curvature are required for efficient recruitment of Arfaptin2 to membranes.
Fil: Ambroggio, Ernesto Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina
Fil: Sillibourne, James. Institute Curie; Francia
Fil: Bruno, Antonny. Université Nice Sophia Antipolis. Laboratoire Jean-alexandre Dieudonné.; Francia
Fil: Manneville, Jean-Baptiste. Institute Curie; Francia
Fil: Bruno, Goud. Institute Curie; Francia
description Arfaptin2 contains a Bin/Amphiphysin/Rvs (BAR) domain and directly interacts with proteins of the Arf/Arl family in their active GTP-bound state. It has been proposed that BAR domains are able to sense membrane curvature and to induce membrane tubulation. We report here that active Arf1 is required for the recruitment of Arfaptin2 to artificial liposomes mimicking the Golgi apparatus lipid composition. The Arf1-dependent recruitment of Arfaptin2 increases with membrane curvature, while the recruitment of Arf1 itself is not sensitive to curvature. At high protein concentrations, the binding of Arfaptin2 induces membrane tubulation. Finally, membrane-bound Arfaptin2 is released from the liposome when ArfGAP1 catalyzes the hydrolysis of GTP to GDP in Arf1. These results show that both Arf1 activation and high membrane curvature are required for efficient recruitment of Arfaptin2 to membranes.
publishDate 2013
dc.date.none.fl_str_mv 2013-04-29
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/11336/480
Ambroggio, Ernesto Esteban; Sillibourne, James; Bruno, Antonny; Manneville, Jean-Baptiste; Bruno, Goud; Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes; Public Library of Science; Plos One; 8; 4; 29-4-2013; 1-6
1932-6203
CONICET Digital
CONICET
url http://hdl.handle.net/11336/480
identifier_str_mv Ambroggio, Ernesto Esteban; Sillibourne, James; Bruno, Antonny; Manneville, Jean-Baptiste; Bruno, Goud; Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes; Public Library of Science; Plos One; 8; 4; 29-4-2013; 1-6
1932-6203
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0062963
info:eu-repo/semantics/altIdentifier/url/http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0062963
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 Public Library of Science
publisher.none.fl_str_mv Public Library of Science
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 12.952241

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