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

Author(s): Baker, Richard W.; Jeffrey, Philip D.; Zick, Michael; Phillips, Ben P.; Wickner, William T.; et al

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Abstract: 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 vacuolar 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.
Publication Date: 4-Sep-2015
Electronic Publication Date: 3-Sep-2015
Citation: Baker, RW, Jeffrey, PD, Zick, M, Phillips, BP, Wickner, WT, Hughson, FM. (2015). A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly. Science, 349 (6252), 1111 - 1114. doi:10.1126/science.aac7906
DOI: doi:10.1126/science.aac7906
ISSN: 0036-8075
EISSN: 1095-9203
Pages: 1111 - 1114
Type of Material: Journal Article
Journal/Proceeding Title: Science
Version: Author's manuscript

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