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活性HOPS复合物的纯化揭示了其对磷酸肌醇和SNARE蛋白Vam7p的亲和力。

Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p.

作者信息

Stroupe Christopher, Collins Kevin M, Fratti Rutilio A, Wickner William

机构信息

Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755-3844, USA.

出版信息

EMBO J. 2006 Apr 19;25(8):1579-89. doi: 10.1038/sj.emboj.7601051. Epub 2006 Apr 6.

Abstract

Coupling of Rab GTPase activation and SNARE complex assembly during membrane fusion is poorly understood. The homotypic fusion and vacuole protein sorting (HOPS) complex links these two processes: it is an effector for the vacuolar Rab GTPase Ypt7p and is required for vacuolar SNARE complex assembly. We now report that pure, active HOPS complex binds phosphoinositides and the PX domain of the vacuolar SNARE protein Vam7p. These binding interactions support HOPS complex association with the vacuole and explain its enrichment at the same microdomains on docked vacuoles as phosphoinositides, Ypt7p, Vam7p, and the other SNARE proteins. Concentration of the HOPS complex at these microdomains may be a key factor for coupling Rab GTPase activation to SNARE complex assembly.

摘要

膜融合过程中Rab GTP酶激活与SNARE复合体组装之间的偶联机制目前仍知之甚少。同型融合与液泡蛋白分选(HOPS)复合体将这两个过程联系起来:它是液泡Rab GTP酶Ypt7p的效应器,也是液泡SNARE复合体组装所必需的。我们现在报告,纯的活性HOPS复合体可结合磷酸肌醇以及液泡SNARE蛋白Vam7p 的PX结构域。这些结合相互作用支持HOPS复合体与液泡的结合,并解释了它与磷酸肌醇、Ypt7p、Vam7p以及其他SNARE蛋白在对接液泡上的相同微结构域中的富集现象。HOPS复合体在这些微结构域中的聚集可能是将Rab GTP酶激活与SNARE复合体组装偶联起来的关键因素。

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