Rab1 recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion
Rab1 recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion
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DOI：
10.1126/science.289.5478.444
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发表时间：
2000-07-21
期刊：
影响因子：
56.9
通讯作者：
Balch, WE
中科院分区：
文献类型：
--
作者：
Allan, BB;Moyer, BD;Balch, WE
鸟苷三磷酸酶 Rab1 通过与效应分子相互作用调节新合成的蛋白质从内质网到高尔基体的转运，但发生这种情况的分子机制尚不清楚。此处，束缚因子 p115 被证明是直接与激活的 Rab1 结合的 Rab1 效应子。 Rab1在内质网出芽期间招募p115来包裹蛋白复合物II (COPII)囊泡，其中它与一组选定的COPII囊泡相关SNARE（可溶性N-乙基马酰亚胺敏感因子附着蛋白受体）相互作用，形成顺式SNARE复合物，促进靶向高尔基体。我们提出 Rab1 调节的功能效应器-SNARE 复合物的组装定义了一种保守的分子机制来协调亚细胞区室之间的识别。
The guanosine triphosphatase Rab1 regulates the transport of newly synthesized proteins from the endoplasmic reticulum to the Golgi apparatus through interaction with effector molecules, but the molecular mechanisms by which this occurs are unknown. Here, the tethering factor p115 was shown to be a Rab1 effector that binds directly to activated Rab1. Rab1 recruited p115 to coat protein complex II (COPII) vesicles during budding from the endoplasmic reticulum, where it interacted with a select set of COPII vesicle-associated SNAREs (soluble N-ethylmateimide-sensitive factor attachment protein receptors) to form a cis-SNARE complex that promotes targeting to the Golgi apparatus. We propose that Rab1-regulated assembly of functional effector-SNARE complexes defines a conserved molecular mechanism to coordinate recognition between subcellular compartments.