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. 1993 Jul;12(7):2847–2853. doi: 10.1002/j.1460-2075.1993.tb05946.x

A 102 kDa subunit of a Golgi-associated particle has homology to beta subunits of trimeric G proteins.

K J Harrison-Lavoie 1, V A Lewis 1, G M Hynes 1, K S Collison 1, E Nutland 1, K R Willison 1
PMCID: PMC413536  PMID: 8335000

Abstract

We have identified a 102 kDa protein, p102, which is found on the cytoplasmic face of Golgi membranes, exocytic transport vesicles and in the cytosol. A monoclonal antibody that cross-reacts with p102 is able to immunoprecipitate a 500-600 kDa protein complex containing p102 and additional subunits. The composition of this p102-containing protein complex resembles that of the Golgi coatomer complex, which constitutes the coat of non-clathrin coated vesicles. One of the subunits of the p102 complex reacts with a monoclonal antibody that detects beta-COP, a subunit of the Golgi coatomer complex. Like beta-COP, p102 exists in a brefeldin A-sensitive association with Golgi membranes. The sequence of p102 contains an N-terminal domain composed of six repeats which are similar to those found in the beta subunit of trimeric G proteins and other regulatory proteins. We suggest that p102 may be involved in regulating membrane traffic in the constitutive exocytic pathway.

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