拉布
对接(动物)
生物
囊泡转运蛋白
高尔基体
小泡
细胞生物学
膜泡运输蛋白质类
囊泡融合
分泌物
转运蛋白
生物化学
酵母
GTP酶
酿酒酵母
突触小泡
液泡蛋白分选
膜
内质网
医学
护理部
作者
Morten Søgaard,Katsuko Tani,R.Ruby Ye,Scott Geromanos,Paul Tempst,Tomas Kirchhausen,James E. Rothman,Thomas Söllner
出处
期刊:Cell
[Elsevier]
日期:1994-09-01
卷期号:78 (6): 937-948
被引量:501
标识
DOI:10.1016/0092-8674(94)90270-4
摘要
Rab proteins are generally required for transport vesicle docking. We have exploited yeast secretion mutants to demonstrate that a rab protein is required for v-SNAREs and t-SNAREs to assemble. The absence of the rab protein in the docking complex suggests that, in a broad sense, rab proteins participate in a reaction catalyzing SNARE complex assembly. In so doing, rab proteins could help impart an additional layer of specificity to vesicle docking. This mechanism likely involves the Sec1 homolog Sly1, which we identified in isolated docking complexes. We also report the identification of a novel v-SNARE (Ykt6p) component of the yeast ER-Golgi docking complex that has a CAAX box and is predicted to be lipid anchored. The surprising finding that docking complexes can contain many distinct species of SNAREs (Sed5p, Bos1p, Sec22p, Ykt6p, and likely Bet1p, p28, and p14) suggests that multimeric interactions are features of the fusion machinery, and may also improve the fidelity of vesicle targeting.
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