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  • Title: Binding of ARF and beta-COP to Golgi membranes: possible regulation by a trimeric G protein.
    Author: Donaldson JG, Kahn RA, Lippincott-Schwartz J, Klausner RD.
    Journal: Science; 1991 Nov 22; 254(5035):1197-9. PubMed ID: 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.
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