MEMBRANE FUSION A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly

被引：227

作者：

Baker, Richard W. ^{[1
]}

Jeffrey, Philip D. ^{[1
]}

Zick, Michael ^{[2
]}

Phillips, Ben P. ^{[1
]}

Wickner, William T. ^{[2
]}

Hughson, Frederick M. ^{[1
]}

机构：

[1] Princeton Univ, Dept Mol Biol, Princeton, NJ 08544 USA

[2] Geisel Sch Med Dartmouth, Dept Biochem, Hanover, NH 03755 USA

来源：

SCIENCE | 2015年 / 349卷 / 6252期

关键词：

STRUCTURAL BASIS; HOPS COMPLEX; DOMAIN; 3A; MUNC18-1; BINDS; YEAST; RECRUITMENT; CHAPERONES; REVEALS; VAM7;

D O I：

10.1126/science.aac7906

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Fusion of intracellular transport vesicles requires soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) and Sec1/Munc18-family (SM) proteins. Membrane-bridging SNARE complexes are critical for fusion, but their spontaneous assembly is inefficient and may require SM proteins in vivo. We report x-ray structures of Vps33, the SM subunit of the yeast homotypic fusion and vacuole protein-sorting (HOPS) complex, bound to two individual SNAREs. The two SNAREs, one from each membrane, are held in the correct orientation and register for subsequent complex assembly. Vps33 and potentially other SM proteins could thus act as templates for generating partially zipped SNARE assembly intermediates. HOPS was essential to mediate SNARE complex assembly at physiological SNARE concentrations. Thus, Vps33 appears to catalyze SNARE complex assembly through specific SNARE motif recognition.

引用

页码：1111 / 1114

页数：4

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