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J Biol Chem, Vol. 273, Issue 27, 17269-17277, July 3, 1998

Rab2 Protein Enhances Coatomer Recruitment to Pre-Golgi Intermediates

Ellen J. TisdaleDagger and Michael R. Jackson

From the Dagger  Department of Pharmacology, Wayne State University School of Medicine, Detroit, Michigan 48201 and the R. W. Johnson Pharmaceutical Research Institute, San Diego, California 92121

The Rab2 protein is a resident of pre-Golgi intermediates and required for vesicular transport in the early secretory pathway. We have previously shown that a peptide corresponding to the amino terminus of Rab2 (residues 2-14) arrests protein traffic prior to a rate-limiting event in VSV-G movement through pre-Golgi structures (Tisdale, E. J., and Balch, W. E. (1996) J. Biol. Chem. 271, 29372-29379). To determine the mechanism by which this peptide inhibits transport, we investigated the effect of the Rab2 peptide on the distribution of the beta -COP subunit of coatomer because COPI partially localizes to pre-Golgi intermediates. We found that the peptide caused a dramatic change in the distribution of pre-Golgi intermediates containing beta -COP. A quantitative binding assay was employed to measure recruitment of beta -COP to membrane when incubated with the Rab2 (13-mer). Peptide-treated microsomes showed a 25-70% increase in the level of membrane-associated beta -COP. The enhanced recruitment of coatomer to membrane was specific to the Rab2 (13-mer) and required guanosine 5'-3-O-(thio)triphosphate, ADP ribosylation factor, and protein kinase C-like activity. The ability to enhance beta -COP membrane binding was not limited to the peptide. Similarly, the addition of recombinant Rab2 protein to the assay promoted beta -COP membrane association. Our results suggest that the Rab2 peptide causes the persistent recruitment of COPI to pre-Golgi intermediates which ultimately arrests protein transport due to the inability of membranes to uncoat.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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