Structural highlights
Publication Abstract from PubMed
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.
A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly.,Baker RW, Jeffrey PD, Zick M, Phillips BP, Wickner WT, Hughson FM Science. 2015 Sep 4;349(6252):1111-4. doi: 10.1126/science.aac7906. PMID:26339030[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Baker RW, Jeffrey PD, Zick M, Phillips BP, Wickner WT, Hughson FM. A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly. Science. 2015 Sep 4;349(6252):1111-4. doi: 10.1126/science.aac7906. PMID:26339030 doi:http://dx.doi.org/10.1126/science.aac7906
