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. 1993 Jul;12(7):2841–2845. doi: 10.1002/j.1460-2075.1993.tb05945.x

beta'-COP, a novel subunit of coatomer.

G Stenbeck 1, C Harter 1, A Brecht 1, D Herrmann 1, F Lottspeich 1, L Orci 1, F T Wieland 1
PMCID: PMC413534  PMID: 8334999

Abstract

Several lines of evidence favour the hypothesis that intracellular biosynthetic protein transport in eukaryotes is mediated by non-clathrin-coated vesicles (for a review see Rothman and Orci, 1992). The vesicles have been isolated and a set of their surface proteins has been characterized as coat proteins (COPs). These COPs exist in the cytosol as a preformed complex, the coatomer, which was prior to this study known to contain six subunits: four (alpha-, beta-, gamma- and delta-COP) with molecular weights between 160 and 58 kDa, and two additional proteins of approximately 36 and 20 kDa, epsilon- and xi-COP. Here we describe a novel subunit of the coatomer complex, beta'-COP. This subunit occurs in amounts stoichiometric to the established COPs both in the coatomer and in nonclathrin-coated vesicles and shows homology to the beta-subunits of trimeric G proteins.

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Selected References

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