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 |