rdf:type |
|
lifeskim:mentions |
umls-concept:C0010222,
umls-concept:C0023779,
umls-concept:C0184967,
umls-concept:C0453946,
umls-concept:C0528008,
umls-concept:C0596901,
umls-concept:C1423774,
umls-concept:C1522408,
umls-concept:C1705944,
umls-concept:C1707798,
umls-concept:C1880352
|
pubmed:issue |
6966
|
pubmed:dateCreated |
2003-12-5
|
pubmed:abstractText |
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.
|
pubmed:commentsCorrections |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
1476-4687
|
pubmed:author |
|
pubmed:issnType |
Electronic
|
pubmed:day |
4
|
pubmed:volume |
426
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
563-6
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:14654841-ADP-Ribosylation Factors,
pubmed-meshheading:14654841-Animals,
pubmed-meshheading:14654841-COP-Coated Vesicles,
pubmed-meshheading:14654841-Coat Protein Complex I,
pubmed-meshheading:14654841-GTPase-Activating Proteins,
pubmed-meshheading:14654841-Golgi Apparatus,
pubmed-meshheading:14654841-Guanosine Triphosphate,
pubmed-meshheading:14654841-Hydrolysis,
pubmed-meshheading:14654841-Intracellular Membranes,
pubmed-meshheading:14654841-Kinetics,
pubmed-meshheading:14654841-Lipid Bilayers,
pubmed-meshheading:14654841-Lipid Metabolism,
pubmed-meshheading:14654841-Lipids,
pubmed-meshheading:14654841-Liposomes,
pubmed-meshheading:14654841-Models, Biological,
pubmed-meshheading:14654841-Rabbits,
pubmed-meshheading:14654841-Time Factors
|
pubmed:year |
2003
|
pubmed:articleTitle |
Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature.
|
pubmed:affiliation |
Institut de Pharmacologie Moléculaire et Cellulaire, CNRS, 660 route des Lucioles, 06560 Valbonne-Sophia-Antipolis, France.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|