一种源自高尔基体的非网格蛋白包被囊泡的外壳亚基，与网格蛋白包被囊泡外壳蛋白β-衔接蛋白具有同源性。

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

作者信息

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

机构信息

Department of Biochemistry, Stanford University, California 94305.

出版信息

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

DOI:10.1038/349215a0

PMID:1898984

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.

摘要

四种高分子量蛋白质构成了高尔基体衍生（非网格蛋白）被膜小泡衣被的主要亚基。这些衣被蛋白之一，β-COP，与一种相对分子质量为110,000（110K）的高尔基体相关蛋白相同，该蛋白与网格蛋白包被小泡的衔接蛋白具有同源性。这种联系，以及高尔基体衍生的和网格蛋白包被小泡的衣被蛋白相当的分子量，表明它们可能在结构上相关。将β-COP鉴定为110K蛋白解释了药物布雷菲德菌素A对分泌的阻断作用。