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TRAPP 复合物在膜运输中的作用:通过共同的 Rab 汇聚

TRAPP complexes in membrane traffic: convergence through a common Rab.

机构信息

Department of Cell Biology, The Johns Hopkins School of Medicine, Baltimore, Maryland 21205, USA.

出版信息

Nat Rev Mol Cell Biol. 2010 Nov;11(11):759-63. doi: 10.1038/nrm2999.

Abstract

Transport protein particle (TRAPP; also known as trafficking protein particle), a multimeric guanine nucleotide-exchange factor for the yeast GTPase Ypt1 and its mammalian homologue, RAB1, regulates multiple membrane trafficking pathways. TRAPP complexes exist in three forms, each of which activates Ypt1 or RAB1 through a common core of subunits and regulates complex localization through distinct subunits. Whereas TRAPPI and TRAPPII tether coated vesicles during endoplasmic reticulum to Golgi and intra-Golgi traffic, respectively, TRAPPIII has recently been shown to be required for autophagy. These advances illustrate how the TRAPP complexes link Ypt1 and RAB1 activation to distinct membrane-tethering events.

摘要

转运蛋白颗粒 (TRAPP;也称为运输蛋白颗粒),是酵母 GTPase Ypt1 及其哺乳动物同源物 RAB1 的多聚体鸟苷酸交换因子,调节多种膜运输途径。TRAPP 复合物有三种形式,每种形式都通过共同的核心亚基激活 Ypt1 或 RAB1,并通过不同的亚基调节复合物的定位。虽然 TRAPPI 和 TRAPPII 分别在内质网到高尔基体和高尔基体内部运输过程中固定有被包被的囊泡,但最近表明 TRAPPIII 对于自噬是必需的。这些进展说明了 TRAPP 复合物如何将 Ypt1 和 RAB1 的激活与不同的膜固定事件联系起来。

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