beta′-COP, a novel subunit of coatomer.
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TL;DR: A novel subunit of the coatomers complex, beta′‐COP, 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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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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Mechanisms of intracellular protein transport.
TL;DR: In this article, the authors uncovered the general protein apparatus used by all eukaryotes for intracellular transport, including secretion and endocytosis, and for triggered exocytotic of hormones and neurotransmitters.
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COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum.
Charles Barlowe,Lelio Orci,Tom Yeung,Midori Hosobuchi,Susan Hamamoto,Nina R. Salama,M F Rexach,Mariella Ravazzola,Mylène Amherdt,Randy Schekman +9 more
TL;DR: In vitro synthesis of endoplasmic reticulum-derived transport vesicles has been reconstituted with washed membranes and three soluble proteins and it is proposed that the coat structures be called COPI and COPII.
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Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum
François Letourneur,Erin C. Gaynor,Silke Hennecke,Corinne Démollière,Rainer Duden,Scott D. Emr,Howard Riezman,Pierre Cosson +7 more
TL;DR: It is suggested that coatomer plays an essential role in retrograde Golgi-to-ER transport and retrieval of dilysine-tagged proteins back to the ER.
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