Lipid-packing and membrane curvature for the regulation of protein-membrane interaction of the Arf1/ArfGAP1-mediated trafficking

AMBROGGIO ERNESTO ESTEBAN; JEAN-BAPTISTE MANNEVILLE; BRUNO GOUD; BRUNO ANTONNY

Puerto Natales

Workshop; EMBO Workshop: Current advances in membrane trafficking: Implications for polarity and diseases; 2014

EMBO

The recruitment of coatomer (COPI) by the small G-protein Arf1 (GTP-bound form) to the Golgigenerates highly-curved COPI-coated membrane buds, which give rise to transport vesicles. TheGTPase activating protein for Arf1, ArfGAP1, has been shown to preferentially interact with highlycurved membranes where it promotes fast GTP hydrolysis on Arf1. This adsorption to highlycurved membranes is due to the presence of two adjacent lipid-packing sensor motifs, calledALPS 1 and ALPS 2, in the middle of the ArfGAP1 sequence. Here I will introduce two casesof study: 1-how lipid packing and membrane curvature impacts on the association and activity ofArfGAP1when GTP-Arf1 is associated to low and high-curvature membranes; and 2-how membranecurvature is important and necessary for the recruitment of Arfaptin2, induced by Arf1 activation, tothe surface of liposomes and lipid tubes.