A COAT SUBUNIT OF GOLGI-DERIVED NON-CLATHRIN-COATED VESICLES WITH HOMOLOGY TO THE CLATHRIN-COATED VESICLE COAT PROTEIN BETA-ADAPTIN

被引:312
作者
SERAFINI, T
STENBECK, G
BRECHT, A
LOTTSPEICH, F
ORCI, L
ROTHMAN, JE
WIELAND, FT
机构
[1] PRINCETON UNIV,DEPT MOLEC BIOL,PRINCETON,NJ 08544
[2] UNIV HEIDELBERG,INST BIOCHEM 1,W-6900 HEIDELBERG,GERMANY
[3] MAX PLANCK INST BIOCHEM,GENZENTRUM,W-8033 MARTINSRIED,GERMANY
[4] UNIV GENEVA,DEPT MORPHOL,CH-1211 GENEVA 4,SWITZERLAND
关键词
D O I
10.1038/349215a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
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页码:214 / 220
页数:7
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