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γ‐COP, a coat subunit of non‐clathrin‐coated vesicles with homology to Sec21p
Author(s) -
Stenbeck Gudrun,
Schreiner Rupert,
Herrmann Doris,
Auerbach Sylvia,
Lottspeich Friedrich,
Rothman James E.,
Wieland Felix T.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80973-k
Subject(s) - clathrin , vesicle , copi , protein subunit , complementary dna , microbiology and biotechnology , clathrin adaptor proteins , yeast , biology , chemistry , secretory pathway , biochemistry , golgi apparatus , gene , membrane , endoplasmic reticulum
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 .