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...

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Bibliographic Details
Published in:PloS one 2013-04, Vol.8 (4), p.e62963-e62963
Main Authors: Ambroggio, Ernesto E, Sillibourne, James, Antonny, Bruno, Manneville, Jean-Baptiste, Goud, Bruno
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing - metabolism
ADP-Ribosylation Factor 1 - metabolism
Binding sites
Biology
Cell Membrane - metabolism
Chemistry
Curvature
Experiments
Golgi apparatus
Guanosine triphosphate
Guanosine Triphosphate - metabolism
Humans
Lipid composition
Lipids
Liposomes
Liposomes - metabolism
Materials Science
Membranes
Mimicry
Protein Transport
Proteins
Recruitment
Substrate Specificity
Sucrose
Unilamellar Liposomes - metabolism
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Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0062963