TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion

被引:244
作者
Sacher, M
Jiang, Y
Barrowman, J
Scarpa, A
Burston, J
Zhang, L
Schieltz, D
Yates, JR
Abeliovich, H
Ferro-Novick, S
机构
[1] Yale Univ, Sch Med, Howard Hughes Med Inst, New Haven, CT 06510 USA
[2] Yale Univ, Sch Med, Dept Cell Biol, New Haven, CT 06510 USA
[3] Univ Washington, Dept Mol Biotechnol, Seattle, WA 98195 USA
关键词
membrane traffic; novel complex; vesicle targeting and fusion;
D O I
10.1093/emboj/17.9.2494
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We previously identified BET3 by its genetic interactions with BET1, a gene whose SNARE-like product acts in endoplasmic reticulum (ER)-to-Golgi transport. To gain insight into the function of Bet3p, we added three c-myc tags to its C-terminus and immunopurified this protein front a clarified detergent extract. Here we report that Bet3p is a member of a large complex (similar to 800 kDa) that me call TRAPP (transport protein particle). We propose that TRAPP plays a key role in the targeting and/or fusion of ER-to-Golgi transport vesicles with their acceptor compartment. The localization of Bet3p to the cis-Golgi complex, as well as biochemical studies showing that Bet3p functions on this compartment, support this hypothesis. TRAPP contains at least nine other constituents, Ave of which have been identified and shown to be highly conserved novel proteins.
引用
收藏
页码:2494 / 2503
页数:10
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