Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature. Export

@article{citeulike:3267789, abstract = {Protein coats deform flat lipid membranes into buds and capture membrane proteins to form transport vesicles. The assembly/disassembly cycle of the COPI coat on Golgi membranes is coupled to the GTP/GDP cycle of the small G protein Arf1. At the heart of this coupling is the specific interaction of membrane-bound Arf1-GTP with coatomer, a complex of seven proteins that forms the building unit of the COPI coat. Although COPI coat disassembly requires the catalysis of GTP hydrolysis in Arf1 by a specific GTPase-activating protein (ArfGAP1), the precise timing of this reaction during COPI vesicle formation is not known. Using time-resolved assays for COPI dynamics on liposomes of controlled size, we show that the rate of ArfGAP1-catalysed GTP hydrolysis in Arf1 and the rate of COPI disassembly increase over two orders of magnitude as the curvature of the lipid bilayer increases and approaches that of a typical transport vesicle. This leads to a model for COPI dynamics in which GTP hydrolysis in Arf1 is organized temporally and spatially according to the changes in lipid packing induced by the coat.}, address = {Institut de Pharmacologie Mol\'{e}culaire et Cellulaire, CNRS, 660 route des Lucioles, 06560 Valbonne-Sophia-Antipolis, France.}, author = {Bigay, J. and Gounon, P. and Robineau, S. and Antonny, B.}, citeulike-article-id = {3267789}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nature02108}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/14654841}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=14654841}, day = {4}, doi = {10.1038/nature02108}, issn = {1476-4687}, journal = {Nature}, keywords = {arf1, budding, coatomer, conform\_change, curvature, fluo, interactions, lipids, membrane, pinching\_off, regulation, vesicle}, month = {December}, number = {6966}, pages = {563--566}, posted-at = {2008-09-15 09:19:26}, priority = {2}, title = {Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature.}, url = {http://dx.doi.org/10.1038/nature02108}, volume = {426}, year = {2003} }

TY - JOUR ID - citeulike:3267789 L3 - citeulike-article-id:3267789 N2 - Protein coats deform flat lipid membranes into buds and capture membrane proteins to form transport vesicles. The assembly/disassembly cycle of the COPI coat on Golgi membranes is coupled to the GTP/GDP cycle of the small G protein Arf1. At the heart of this coupling is the specific interaction of membrane-bound Arf1-GTP with coatomer, a complex of seven proteins that forms the building unit of the COPI coat. Although COPI coat disassembly requires the catalysis of GTP hydrolysis in Arf1 by a specific GTPase-activating protein (ArfGAP1), the precise timing of this reaction during COPI vesicle formation is not known. Using time-resolved assays for COPI dynamics on liposomes of controlled size, we show that the rate of ArfGAP1-catalysed GTP hydrolysis in Arf1 and the rate of COPI disassembly increase over two orders of magnitude as the curvature of the lipid bilayer increases and approaches that of a typical transport vesicle. This leads to a model for COPI dynamics in which GTP hydrolysis in Arf1 is organized temporally and spatially according to the changes in lipid packing induced by the coat. IS - 6966 JF - Nature SN - 1476-4687 AD - Institut de Pharmacologie Moléculaire et Cellulaire, CNRS, 660 route des Lucioles, 06560 Valbonne-Sophia-Antipolis, France. EP - 566 TI - Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature. VL - 426 SP - 563 KW - arf1 KW - budding KW - coatomer KW - conform_change KW - curvature KW - fluo KW - interactions KW - lipids KW - membrane KW - pinching_off KW - regulation KW - vesicle AU - Bigay, J AU - Gounon, P AU - Robineau, S AU - Antonny, B PY - 2003/12/04/ UR - http://dx.doi.org/10.1038/nature02108 ER -