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Science 22 November 1991:
Vol. 254. no. 5035, pp. 1197 - 1199
DOI: 10.1126/science.1957170
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Articles

Science, Vol 254, Issue 5035, 1197-1199
Copyright © 1991 by American Association for the Advancement of Science

articles

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

JG Donaldson, RA Kahn, J Lippincott-Schwartz, and RD Klausner

Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.

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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