A role for Yip1p in COPII vesicle biogenesis

被引:63
作者
Heidtman, M
Chen, CZ
Collins, RN
Barlowe, C [1 ]
机构
[1] Dartmouth Coll Sch Med, Dept Biochem, Hanover, NH 03755 USA
[2] Cornell Univ, Ctr Vet Med, Dept Mol Med, Ithaca, NY 14853 USA
关键词
ER; Golgi; vesicles; coat proteins; trafficking;
D O I
10.1083/jcb.200306118
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Yeast Ypt1p-interacting protein (Yip1p) belongs to a conserved family of transmembrane proteins that interact with Rab GTPases. We encountered Yip1p as a constituent of ER-derived transport vesicles, leading us to hypothesize a direct role for this protein in transport through the early secretory pathway. Using a cell-free assay that recapitulates protein transport from the ER to the Golgi complex, we find that affinity-purified antibodies directed against the hydrophilic amino terminus of Yip1p potently inhibit transport. Surprisingly, inhibition is specific to the COPII-dependent budding stage. In support of this in vitro observation, strains bearing the temperature-sensitive yip1-4 allele accumulate ER membranes at a nonpermissive temperature, with no apparent accumulation of vesicle intermediates. Genetic interaction analyses of the yip1-4 mutation corroborate a function in ER budding. Finally, ordering experiments show that preincubation of ER membranes with COPII proteins decreases sensitivity to anti-Yip1p antibodies, indicating an early requirement for Yip1p in vesicle formation. We propose that Yip1p has a previously unappreciated role in COPII vesicle biogenesis.
引用
收藏
页码:57 / 69
页数:13
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