VPS33 Antibody

1. Thus, Vps33/HOPS promotes productive SNARE assembly in the presence of otherwise inhibitory Sec17. PMID: 28925353
2. Homotypic fusion and protein-sorting/class C vacuole protein-sorting (HOPS/class C Vps) complex can tether low-curvature membranes, that is, liposomes with a diameter of 100 nm, only when the yeast vacuolar Ypt7p is present in both tethered membranes. PMID: 25995379
3. Sec17 directly promotes selective loading of Sly1 and Vps33 onto cognate SNARE complexes PMID: 24837546
4. Vps33 appears to catalyze SNARE complex assembly through specific SNARE motif recognition. PMID: 26339030
5. Data show that the binding sites for vacuolar SNAREs and the SNARE Vam3 Habc domain are located in the large head of the HOPS complex, where vesicular transport proteins Vps16 and Vps33 have been identified. PMID: 25564619
6. we identify missense mutations of Vps33 that produce a novel set of defects, including cargo missorting and the loss of Vps33-HOPS association PMID: 23051737
7. contribution of Vps33 to hemifusion and pore opening between vacuoles. Mutations in Vps33 that weaken its interactions with the SNARE complex allowed normal trans-SNARE pairing and lipid mixing but retarded content mixing. PMID: 20453860
8. Vps33p functions at multiple trafficking steps and is not limited to action at the vacuolar membrane PMID: 15047864

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KEGG: sce:YLR396C

STRING: 4932.YLR396C