beta'-COP, a novel subunit of coatomer.
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.
Stenbeck
G
G
Institute of Biochemistry I, University of Heidelberg, Germany.
Harter
C
C
Brecht
A
A
Herrmann
D
D
Lottspeich
F
F
Orci
L
L
Wieland
F T
FT
D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D002213:Capsid / Q000737:chemistry*; D002417:Cattle; D020756:Coatomer Protein; D006224:Cricetinae; D004247:DNA; D006056:Golgi Apparatus / Q000737:chemistry / Q000648:ultrastructure; D007425:Intracellular Membranes / Q000737:chemistry / Q000648:ultrastructure; D008565:Membrane Proteins / Q000737:chemistry*; D008854:Microscopy, Electron; D008869:Microtubule-Associated Proteins / Q000737:chemistry* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D011817:Rabbits
D020756:Coatomer Protein; D008565:Membrane Proteins; D008869:Microtubule-Associated Proteins; D004247:DNA