Binding of ARF and beta-COP to Golgi membranes: possible regulation by a trimeric G protein - PubMed (original) (raw)

. 1991 Nov 22;254(5035):1197-9.

doi: 10.1126/science.1957170.

Affiliations

• PMID: 1957170
• DOI: 10.1126/science.1957170

Binding of ARF and beta-COP to Golgi membranes: possible regulation by a trimeric G protein

J G Donaldson et al. Science. 1991.

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.

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