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

Richard W. Baker, Philip D. Jeffrey, Michael Zick, Ben P. Phillips, William T. Wickner, Frederick M. Hughson

Research output: Contribution to journalArticle

127 Scopus citations

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 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.

Original languageEnglish (US)
Pages (from-to)1111-1114
Number of pages4
JournalScience
Volume349
Issue number6252
DOIs
StatePublished - Sep 4 2015

All Science Journal Classification (ASJC) codes

  • General

Fingerprint Dive into the research topics of 'A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly'. Together they form a unique fingerprint.

  • Cite this

    Baker, R. W., Jeffrey, P. D., Zick, M., Phillips, B. P., Wickner, W. T., & Hughson, F. M. (2015). A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly. Science, 349(6252), 1111-1114. https://doi.org/10.1126/science.aac7906