Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: a role for ArfGAP1

doi:10.1083/jcb.200108017

Published online 17 December 2001. doi:10.1083/jcb.200108017

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© The Rockefeller University Press, 0021-9525/2001/12/1199 $5.00
The Journal of Cell Biology, Volume 155, Number 7, December 24, 2001 1199-1212

Article

Sorting of Golgi resident proteins into different subpopulations of COPI vesicles : a role for ArfGAP1

Joel Lanoix¹, Joke Ouwendijk¹, Annika Stark¹, Edith Szafer², Dan Cassel², Kurt Dejgaard¹, Matthias Weiss¹ and Tommy Nilsson¹

¹ Cell Biology and Biophysics Programme, European Molecular Biology Laboratory, D-69017 Heidelberg, Germany
² Department of Biology, Technion, Haifa 32000, Israel

Address correspondence to Tommy Nilsson, Cell Biology and Biophysics Programme, EMBL, D-69017 Heidelberg, Germany. Tel.: 49-6221-387-294. Fax: 49-6221-387-306. E-mail: nilsson{at}embl-heidelberg.de

We present evidence for two subpopulations of coatomer proteinI vesicles, both containing high amounts of Golgi resident proteinsbut only minor amounts of anterograde cargo. Early Golgi proteinsp24 ${alpha}$ ₂, ß₁, ${delta}$ ₁, and ${gamma}$ ₃ are shown to be sorted togetherinto vesicles that are distinct from those containing mannosidaseII, a glycosidase of the medial Golgi stack, and GS28, a SNAREprotein of the Golgi stack. Sorting into each vesicle populationis Arf-1 and GTP hydrolysis dependent and is inhibited by aluminumand beryllium fluoride. Using synthetic peptides, we find thatthe cytoplasmic domain of p24ß₁ can bind Arf GTPase-activatingprotein (GAP)1 and cause direct inhibition of ArfGAP1-mediatedGTP hydrolysis on Arf-1 bound to liposomes and Golgi membranes.We propose a two-stage reaction to explain how GTP hydrolysisconstitutes a prerequisite for sorting of resident proteins,yet becomes inhibited in their presence.

Key Words: Golgi; COPI; recycling; p24 proteins; ArfGAP1

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