Binding of ARF and β-COP to Golgi Membranes: Possible Regulation by a Trimeric G Protein
- 22 November 1991
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 254 (5035) , 1197-1199
- https://doi.org/10.1126/science.1957170
Abstract
The binding of cytosolic coat proteins to organelles may regulate membrane structure and traffic. Evidence is presented that a small guanosine triphosphate (GTP)-binding protein, the adenosine diphosphate ribosylation factor (ARF), reversibly associates with the Golgi apparatus in an energy, GTP, and fungal metabolite brefeldin A (BFA)-sensitive manner similar to, but distinguishable from, the 110-kilodalton cytosolic coat protein beta-COP. Addition of beta gamma subunits of G proteins inhibited the association of both ARF and beta-COP with Golgi membranes that occurred upon incubation with guanosine 5'-O-(3-thiotriphosphate) (GTP-gamma-S). Thus, heterotrimeric G proteins may function to regulate the assembly of coat proteins onto the Golgi membrane.Keywords
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