Cargando…

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

Detalles Bibliográficos
Autores principales: Ambroggio, Ernesto E., Sillibourne, James, Antonny, Bruno, Manneville, Jean-Baptiste, Goud, Bruno
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3639266/
https://www.ncbi.nlm.nih.gov/pubmed/23638170
http://dx.doi.org/10.1371/journal.pone.0062963
_version_ 1782475931614445568
author Ambroggio, Ernesto E.
Sillibourne, James
Antonny, Bruno
Manneville, Jean-Baptiste
Goud, Bruno
author_facet Ambroggio, Ernesto E.
Sillibourne, James
Antonny, Bruno
Manneville, Jean-Baptiste
Goud, Bruno
author_sort Ambroggio, Ernesto E.
collection PubMed
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 Online
Article
Text
id pubmed-3639266
institution National Center for Biotechnology Information
language English
publishDate 2013
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-36392662013-05-01 Arf1 and Membrane Curvature Cooperate to Recruit Arfaptin2 to Liposomes Ambroggio, Ernesto E. Sillibourne, James Antonny, Bruno Manneville, Jean-Baptiste Goud, Bruno PLoS One Research Article 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. Public Library of Science 2013-04-29 /pmc/articles/PMC3639266/ /pubmed/23638170 http://dx.doi.org/10.1371/journal.pone.0062963 Text en © 2013 Ambroggio et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Ambroggio, Ernesto E.
Sillibourne, James
Antonny, Bruno
Manneville, Jean-Baptiste
Goud, Bruno
Arf1 and Membrane Curvature Cooperate to Recruit Arfaptin2 to Liposomes
title 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_short Arf1 and Membrane Curvature Cooperate to Recruit Arfaptin2 to Liposomes
title_sort arf1 and membrane curvature cooperate to recruit arfaptin2 to liposomes
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3639266/
https://www.ncbi.nlm.nih.gov/pubmed/23638170
http://dx.doi.org/10.1371/journal.pone.0062963
work_keys_str_mv AT ambroggioernestoe arf1andmembranecurvaturecooperatetorecruitarfaptin2toliposomes
AT sillibournejames arf1andmembranecurvaturecooperatetorecruitarfaptin2toliposomes
AT antonnybruno arf1andmembranecurvaturecooperatetorecruitarfaptin2toliposomes
AT mannevillejeanbaptiste arf1andmembranecurvaturecooperatetorecruitarfaptin2toliposomes
AT goudbruno arf1andmembranecurvaturecooperatetorecruitarfaptin2toliposomes