Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes

• Published in: PloS one Vol. 8; no. 4; p. e62963
• Main Authors: Ambroggio, Ernesto E, Sillibourne, James, Antonny, Bruno, Manneville, Jean-Baptiste, Goud, Bruno
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 29-04-2013; Public Library of Science (PLoS)
• 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
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0062963

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.