A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein beta-adaptin

T Serafini; G Stenbeck; A Brecht; F Lottspeich; L Orci; J E Rothman; F T Wieland

doi:10.1038/349215a0

A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein beta-adaptin

Nature. 1991 Jan 17;349(6306):215-20. doi: 10.1038/349215a0.

Authors

T Serafini¹, G Stenbeck, A Brecht, F Lottspeich, L Orci, J E Rothman, F T Wieland

Affiliation

¹ Department of Biochemistry, Stanford University, California 94305.

PMID: 1898984
DOI: 10.1038/349215a0

Abstract

Four high-molecular-weight proteins form the main subunits of the coat of Golgi-derived (non-clathrin) coated vesicles. One of these coat proteins, beta-COP, is identical to a Golgi-associated protein of relative mass 110,000 (110K) that shares homology with the adaptin proteins of clathrin-coated vesicles. This connection, and the comparable molecular weights of the coat proteins of Golgi-derived and clathrin-coated vesicles, indicates that they may be structurally related. The identification of beta-COP as the 110K protein explains the blocking of secretion by the drug brefeldin A.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Adaptor Protein Complex beta Subunits
Amino Acid Sequence
Animals
Cell Fractionation / methods
Clathrin / chemistry*
Coated Pits, Cell-Membrane / chemistry*
Coated Pits, Cell-Membrane / ultrastructure
Golgi Apparatus / chemistry*
Membrane Proteins / chemistry*
Membrane Proteins / isolation & purification
Microscopy, Immunoelectron
Molecular Sequence Data
Proteins / chemistry*
Proteins / isolation & purification
Sequence Homology, Nucleic Acid

Substances

Adaptor Protein Complex beta Subunits
Clathrin
Membrane Proteins
Proteins