Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes.

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...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Ernesto E Ambroggio, James Sillibourne, Bruno Antonny, Jean-Baptiste Manneville, Bruno Goud
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8f67bad387a24eefa2ef9c7fc2dff0a8
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:8f67bad387a24eefa2ef9c7fc2dff0a8
record_format	dspace
spelling	oai:doaj.org-article:8f67bad387a24eefa2ef9c7fc2dff0a82021-11-18T07:47:35ZArf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes.1932-620310.1371/journal.pone.0062963https://doaj.org/article/8f67bad387a24eefa2ef9c7fc2dff0a82013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23638170/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Arfaptin2 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.Ernesto E AmbroggioJames SillibourneBruno AntonnyJean-Baptiste MannevilleBruno GoudPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 4, p e62963 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ernesto E Ambroggio James Sillibourne Bruno Antonny Jean-Baptiste Manneville Bruno Goud Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes.
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.
format	article
author	Ernesto E Ambroggio James Sillibourne Bruno Antonny Jean-Baptiste Manneville Bruno Goud
author_facet	Ernesto E Ambroggio James Sillibourne Bruno Antonny Jean-Baptiste Manneville Bruno Goud
author_sort	Ernesto E Ambroggio
title	Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes.
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.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/8f67bad387a24eefa2ef9c7fc2dff0a8
work_keys_str_mv	AT ernestoeambroggio arf1andmembranecurvaturecooperatetorecruitarfaptin2toliposomes AT jamessillibourne arf1andmembranecurvaturecooperatetorecruitarfaptin2toliposomes AT brunoantonny arf1andmembranecurvaturecooperatetorecruitarfaptin2toliposomes AT jeanbaptistemanneville arf1andmembranecurvaturecooperatetorecruitarfaptin2toliposomes AT brunogoud arf1andmembranecurvaturecooperatetorecruitarfaptin2toliposomes
_version_	1718422987116380160

Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes.

Ejemplares similares