共 31 条
TRAPP stimulates guanine nucleotide exchange on Ypt1p
被引:160
作者:

Wang, W
论文数: 0 引用数: 0
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机构:
Yale Univ, Sch Med, Howard Hughes Med Inst, Boyer Ctr Mol Med,Dept Cell Biol, New Haven, CT 06519 USA Yale Univ, Sch Med, Howard Hughes Med Inst, Boyer Ctr Mol Med,Dept Cell Biol, New Haven, CT 06519 USA

Sacher, M
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h-index: 0
机构:
Yale Univ, Sch Med, Howard Hughes Med Inst, Boyer Ctr Mol Med,Dept Cell Biol, New Haven, CT 06519 USA Yale Univ, Sch Med, Howard Hughes Med Inst, Boyer Ctr Mol Med,Dept Cell Biol, New Haven, CT 06519 USA

Ferro-Novick, S
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机构:
Yale Univ, Sch Med, Howard Hughes Med Inst, Boyer Ctr Mol Med,Dept Cell Biol, New Haven, CT 06519 USA Yale Univ, Sch Med, Howard Hughes Med Inst, Boyer Ctr Mol Med,Dept Cell Biol, New Haven, CT 06519 USA
机构:
[1] Yale Univ, Sch Med, Howard Hughes Med Inst, Boyer Ctr Mol Med,Dept Cell Biol, New Haven, CT 06519 USA
关键词:
exchange factor;
small GTPase;
secretion;
ER-to-Golgi;
tethering factor;
D O I:
10.1083/jcb.151.2.289
中图分类号:
Q2 [细胞生物学];
学科分类号:
071009 ;
090102 ;
摘要:
TRAPP, a novel complex that resides on early Golgi, mediates the targeting of ER-to-Golgi vesicles to the Golgi apparatus. Previous studies have shown that YPT1, which encodes the small OTP-binding protein that regulates membrane traffic at this stage of the secretory pathway, interacts genetically with BET3 and BET5. Bet3p and Bet5p are 2 of the 10 identified subunits of TRAPP. Here we show that TRAPP preferentially binds to the nucleotide-free form of Ypt1p. Mutants with defects in several TRAPP subunits are temperature-sensitive in their ability to displace GDP from Ypt1p. Furthermore, the purified TRAPP complex accelerates nucleotide exchange on Ypt1p. Our findings imply that Ypt1p, which is present on ER-to-Golgi transport vesicles, is activated at the Golgi once it interacts with TRAPP.
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页码:289 / 295
页数:7
相关论文
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