γ-COP, a coat subunit of non-clathrin-coated vesicles with homology to Sec21p Journal Article


Authors: Stenbeck, G.; Schreiner, R.; Herrmann, D.; Auerbach, S.; Lottspeich, F.; Rothman, J. E.; Wieland, F. T.
Article Title: γ-COP, a coat subunit of non-clathrin-coated vesicles with homology to Sec21p
Abstract: Constitutive secretory transport in eukaryotes is likely to be mediated by non-clathrin-coated vesicles, which have been isolated and characterized [(1989) Cell 58, 329-336; (1991) Nature 349, 215-220]. They contain a set of coat proteins (COPs) which are also likely to exist in a preformed cytosolic complex named coatomer [(1991) Nature 349, 248-250]. From peptide sequence and cDNA structure comparisons evidence is presented that one of the subunits of coatomer, γ-COP, is a true constituent of non-clathrin-coated vesicles, and that γ-COP is related to sec 21, a secretory mutant of the yeast Saccharomyces cervisiae. © 1992.
Keywords: animal; membrane proteins; cloning, molecular; endoplasmic reticulum; amino acid sequence; molecular sequence data; sequence homology, amino acid; brain; saccharomyces cerevisiae; base sequence; cattle; biological transport; golgi complex; clathrin; fungal proteins; vesicular transport; coated vesicle; endosomes; secretory protein; fungus mutant; golgi apparatus; coat protein; golgi; coatomer; priority journal; article; support, non-u.s. gov't; coat protein γ-cop; sec21
Journal Title: FEBS Letters
Volume: 314
Issue: 2
ISSN: 0014-5793
Publisher: Wiley Blackwell  
Date Published: 1992-12-14
Start Page: 195
End Page: 198
Language: English
DOI: 10.1016/0014-5793(92)80973-k
PUBMED: 1360908
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 30 July 2019 -- Source: Scopus
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  1. James E Rothman
    120 Rothman