BETA'-COP, A NOVEL SUBUNIT OF COATOMER
BETA'-COP, A NOVEL SUBUNIT OF COATOMER
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DOI：
10.1002/j.1460-2075.1993.tb05945.x
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发表时间：
1993-07-01
期刊：
影响因子：
11.4
通讯作者：
WIELAND, FT
中科院分区：
文献类型：
--
作者：
STENBECK, G;HARTER, C;WIELAND, FT
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 non-clathrin-coated vesicles and shows homology to the beta-subunits of trimeric G proteins.
