Genomes and Genes
Gene Symbol: VPS33
Description: tethering complex ATP-binding subunit VPS33
Alias: CLS14, MET27, PEP14, SLP1, VAM5, VPL25, VPT33, tethering complex ATP-binding subunit VPS33
Species: Saccharomyces cerevisiae S288c
- Wada Y, Kitamoto K, Kanbe T, Tanaka K, Anraku Y. The SLP1 gene of Saccharomyces cerevisiae is essential for vacuolar morphogenesis and function. Mol Cell Biol. 1990;10:2214-23 pubmed..Genetic and molecular biological analyses revealed that SLP1 is identical to VPS33, which is required for vacuolar protein sorting as reported by Robinson et al. (J. S. Robinson, D. J. Klionsky, L...
- Plemel R, Lobingier B, Brett C, Angers C, Nickerson D, Paulsel A, et al. Subunit organization and Rab interactions of Vps-C protein complexes that control endolysosomal membrane traffic. Mol Biol Cell. 2011;22:1353-63 pubmed publisher..Biochemical and genetic experiments demonstrate the importance of these regions, revealing the Vps11 CTD as a key integrator of Vps-C complex assembly, Rab signaling, and endosomal and lysosomal traffic. ..
- Dulubova I, Yamaguchi T, Wang Y, Sudhof T, Rizo J. Vam3p structure reveals conserved and divergent properties of syntaxins. Nat Struct Biol. 2001;8:258-64 pubmed
- Seals D, Eitzen G, Margolis N, Wickner W, Price A. A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion. Proc Natl Acad Sci U S A. 2000;97:9402-7 pubmed..HOPS initially associates with vacuole SNAREs in "cis" and, after release by priming, hops to Ypt7p, activating this Ypt/Rab switch to initiate docking. ..
- Karunakaran V, Wickner W. Fusion proteins and select lipids cooperate as membrane receptors for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vam7p. J Biol Chem. 2013;288:28557-66 pubmed publisher..Acidic lipids allow low concentrations of Vam7p to suffice for fusion; without acidic lipids, the block to fusion is partially bypassed by high concentrations of Vam7p. ..
- Pieren M, Schmidt A, Mayer A. The SM protein Vps33 and the t-SNARE H(abc) domain promote fusion pore opening. Nat Struct Mol Biol. 2010;17:710-7 pubmed publisher..We investigated the contributions of the SM protein Vps33 to hemifusion and pore opening between yeast vacuoles...
- Robinson J, Klionsky D, Banta L, Emr S. Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol Cell Biol. 1988;8:4936-48 pubmed..Representative alleles from each of the 33 vpt complementation groups (vpt1 through vpt33) were shown to exhibit defects in the sorting and processing of several native vacuolar proteins, including the ..
- Wang L, Seeley E, Wickner W, Merz A. Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle. Cell. 2002;108:357-69 pubmed..Their vertex enrichment requires cis-SNARE complex disassembly and is thus part of the normal fusion pathway. ..
- Wang C, Stromhaug P, Kauffman E, Weisman L, Klionsky D. Yeast homotypic vacuole fusion requires the Ccz1-Mon1 complex during the tethering/docking stage. J Cell Biol. 2003;163:973-85 pubmed..Accordingly, we propose that the Ccz1-Mon1 complex is critical for the Ypt7-dependent tethering/docking stage leading to the formation of a trans-SNARE complex and subsequent vacuole fusion. ..
- Laage R, Ungermann C. The N-terminal domain of the t-SNARE Vam3p coordinates priming and docking in yeast vacuole fusion. Mol Biol Cell. 2001;12:3375-85 pubmed..We conclude that the N-terminus of Vam3p is required for coordination of priming and docking during homotypic vacuole fusion. ..
- Lobingier B, Merz A. Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex. Mol Biol Cell. 2012;23:4611-22 pubmed publisher..b>Vps33 is an SM protein and subunit of the Vps-C complexes HOPS (homotypic fusion and protein sorting) and CORVET (class ..
- Rieder S, Emr S. A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuole. Mol Biol Cell. 1997;8:2307-27 pubmed..Thus we propose that the class C Vps proteins are components of a hetero-oligomeric protein complex that mediates the delivery of multiple transport intermediates to the vacuole. ..
- Peplowska K, Markgraf D, Ostrowicz C, Bange G, Ungermann C. The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis. Dev Cell. 2007;12:739-50 pubmed..Both complexes share the four class C Vps proteins: Vps11, Vps16, Vps18, and Vps33. The HOPS complex, in addition, contains Vps41/Vam2 and Vam6, whereas the CORVET complex has the Vps41 homolog ..
- Brett C, Plemel R, Lobingier B, Lobinger B, Vignali M, Fields S, et al. Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase. J Cell Biol. 2008;182:1141-51 pubmed publisher..We propose that signal propagation through the Ypt7 pathway is controlled by integrated feedback and feed-forward loops. In this model, Yck3 enforces a requirement for the activated Rab in docking and fusion. ..
- Collins K, Thorngren N, Fratti R, Wickner W. Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion. EMBO J. 2005;24:1775-86 pubmed..Sec17p may displace HOPS from SNAREs to permit subsequent rounds of fusion. ..
- Ostrowicz C, Bröcker C, Ahnert F, Nordmann M, Lachmann J, Peplowska K, et al. Defined subunit arrangement and rab interactions are required for functionality of the HOPS tethering complex. Traffic. 2010;11:1334-46 pubmed publisher..Both complexes contain two Rab-binding proteins at one end, and the Sec1/Munc18-like Vps33 at the opposite side, suggesting a model on membrane bridging via Rab-GTP and SNARE binding...
- Subramanian S, Woolford C, Jones E. The Sec1/Munc18 protein, Vps33p, functions at the endosome and the vacuole of Saccharomyces cerevisiae. Mol Biol Cell. 2004;15:2593-605 pubmed..Consistent with this, vps33 mutants secrete the Golgi precursor form of the vacuolar hydrolase CPY into the medium...
- Karunakaran S, Fratti R. The lipid composition and physical properties of the yeast vacuole affect the hemifusion-fusion transition. Traffic. 2013;14:650-62 pubmed publisher..Together, these data indicate that the physical properties and the lipid composition of the membrane affect the function of SNAREs in promoting the hemifusion-fusion transition. ..
- Lobingier B, Nickerson D, Lo S, Merz A. SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18. elife. 2014;3:e02272 pubmed publisher..We now report that, in addition to their established roles as fusion accelerators, SM proteins Sly1 and Vps33 directly shield SNARE complexes from Sec17- and Sec18-mediated disassembly...
- Ho R, Stroupe C. The HOPS/Class C Vps Complex Tethers High-Curvature Membranes via a Direct Protein-Membrane Interaction. Traffic. 2016;17:1078-90 pubmed publisher..We propose that HOPS localizes via the Vps41p ALPS motif to these high-curvature regions. There, HOPS binds via Vps39p to Ypt7p in an apposed vacuole membrane. ..
- Qiu Q, Fratti R. The Na+/H+ exchanger Nhx1p regulates the initiation of Saccharomyces cerevisiae vacuole fusion. J Cell Sci. 2010;123:3266-75 pubmed publisher..In addition, the weak base chloroquine restored nhx1? fusion to wild-type levels. Together, these data indicate that Nhx1p regulates the initiation of fusion by controlling vacuole lumen pH. ..
- Sasser T, Qiu Q, Karunakaran S, Padolina M, Reyes A, Flood B, et al. Yeast lipin 1 orthologue pah1p regulates vacuole homeostasis and membrane fusion. J Biol Chem. 2012;287:2221-36 pubmed publisher..These findings demonstrate that Pah1p and PA phosphatase activity are critical for vacuole homeostasis and fusion. ..
- Cabrera M, Ostrowicz C, Mari M, LaGrassa T, Reggiori F, Ungermann C. Vps41 phosphorylation and the Rab Ypt7 control the targeting of the HOPS complex to endosome-vacuole fusion sites. Mol Biol Cell. 2009;20:1937-48 pubmed publisher..Our data suggest that Vps41 phosphorylation fine-tunes the organization of vacuole fusion sites and provide evidence for a fusion "hot spot" on the vacuole limiting membrane. ..
- Zurita Martinez S, Puria R, Pan X, Boeke J, Cardenas M. Efficient Tor signaling requires a functional class C Vps protein complex in Saccharomyces cerevisiae. Genetics. 2007;176:2139-50 pubmed
- Lazar T, Scheglmann D, Gallwitz D. A novel phospholipid-binding protein from the yeast Saccharomyces cerevisiae with dual binding specificities for the transport GTPase Ypt7p and the Sec1-related Vps33p. Eur J Cell Biol. 2002;81:635-46 pubmed..IVY1 for: Interacting with Vps33p and Ypt7p) was found to interact with both the GTPase Ypt7p and the Sec1-related Vps33 protein...
- Xu H, Wickner W. Bem1p is a positive regulator of the homotypic fusion of yeast vacuoles. J Biol Chem. 2006;281:27158-66 pubmed..2005) Genes Dev. 19, 2606-2618), we did not find phosphorylation of Bem1p at Ser-72 to be required for Bem1p-stimulated fusion. Taken together, Bem1p is a positive regulator of lipid mixing during vacuole hemifusion and fusion. ..
- Behrmann H, LÃ¼rick A, Kuhlee A, Balderhaar H, BrÃ¶cker C, KÃ¼mmel D, et al. Structural identification of the Vps18 Î²-propeller reveals a critical role in the HOPS complex stability and function. J Biol Chem. 2014;289:33503-12 pubmed publisher..We thus conclude that the Î²-propeller of Vps18 is required for HOPS stability and function and that it can serve as a starting point for further structural analyses of the HOPS tethering complex. ..
- Orr A, Wickner W, Rusin S, Kettenbach A, Zick M. Yeast vacuolar HOPS, regulated by its kinase, exploits affinities for acidic lipids and Rab:GTP for membrane binding and to catalyze tethering and fusion. Mol Biol Cell. 2015;26:305-15 pubmed publisher..After phosphorylation by the vacuolar kinase Yck3p, phospho-HOPS needs both Ypt7p:GTP and acidic lipids to support fusion. ..
- Baker R, Jeffrey P, Zick M, Phillips B, Wickner W, Hughson F. A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly. Science. 2015;349:1111-4 pubmed publisher..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 ..
- Bugnicourt A, Froissard M, Sereti K, Ulrich H, Haguenauer Tsapis R, Galan J. Antagonistic roles of ESCRT and Vps class C/HOPS complexes in the recycling of yeast membrane proteins. Mol Biol Cell. 2004;15:4203-14 pubmed..Genetic analyses indicated that these phenotypes were due to the functioning of the Vps class C complex in trafficking both to and from the late endosomal compartment. ..
- Hoffman Sommer M, Kucharczyk R, Piekarska I, Kozlowska E, Rytka J. Mutations in the Saccharomyces cerevisiae vacuolar fusion proteins Ccz1, Mon1 and Ypt7 cause defects in cell cycle progression in a num1Delta background. Eur J Cell Biol. 2009;88:639-52 pubmed publisher..Together, these results indicate that deregulation of the cell cycle in these mutants results from two separate mechanisms, one of which is related to calcium homeostasis. ..
- Gerhardt B, Kordas T, Thompson C, Patel P, Vida T. The vesicle transport protein Vps33p is an ATP-binding protein that localizes to the cytosol in an energy-dependent manner. J Biol Chem. 1998;273:15818-29 pubmed..Overall, these data support a model where Vps33p cycles between soluble and particulate forms in an ATP-dependent manner, which may facilitate the specificity of transport vesicle docking or targeting to the yeast lysosome/vacuole. ..
- Conibear E, Stevens T. Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi. Mol Biol Cell. 2000;11:305-23 pubmed..The Vps52/53/54 complex joins a growing list of distinct multisubunit complexes that regulate membrane-trafficking events. ..
- Schwartz M, Nickerson D, Lobingier B, Plemel R, Duan M, Angers C, et al. Sec17 (?-SNAP) and an SM-tethering complex regulate the outcome of SNARE zippering in vitro and in vivo. elife. 2017;6: pubmed publisher..The formation of a metastable trans-complex, catalyzed by HOPS and its SM subunit Vps33, is followed by subsequent zippering transitions that increase the probability of fusion...
- LÃ¼rick A, Kuhlee A, BrÃ¶cker C, KÃ¼mmel D, Raunser S, Ungermann C. The Habc domain of the SNARE Vam3 interacts with the HOPS tethering complex to facilitate vacuole fusion. J Biol Chem. 2015;290:5405-13 pubmed publisher..It is assumed that the Sec1/Munc18-like Vps33 within the HOPS complex is largely responsible for SNARE chaperoning...
- Sasser T, Lawrence G, Karunakaran S, Brown C, Fratti R. The yeast ATP-binding cassette (ABC) transporter Ycf1p enhances the recruitment of the soluble SNARE Vam7p to vacuoles for efficient membrane fusion. J Biol Chem. 2013;288:18300-10 pubmed publisher..The attenuated fusion of ycf1? vacuoles was rescued by the addition of recombinant Vam7p to in vitro experiments. Thus, Ycf1p contributes in the recruitment of Vam7p to the vacuole for efficient membrane fusion. ..
- Alpadi K, Kulkarni A, Namjoshi S, Srinivasan S, Sippel K, Ayscough K, et al. Dynamin-SNARE interactions control trans-SNARE formation in intracellular membrane fusion. Nat Commun. 2013;4:1704 pubmed publisher..Our findings provide new insight into the role of dynamins in membrane fusion by directly acting on SNARE proteins. ..
- Balderhaar H, Lachmann J, Yavavli E, Bröcker C, Lürick A, Ungermann C. The CORVET complex promotes tethering and fusion of Rab5/Vps21-positive membranes. Proc Natl Acad Sci U S A. 2013;110:3823-8 pubmed publisher..We therefore conclude that CORVET is a tethering complex that promotes fusion of Rab5-positive membranes and thus facilitates receptor down-regulation and recycling at the late endosome. ..
- Darsow T, Rieder S, Emr S. A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole. J Cell Biol. 1997;138:517-29 pubmed..Genetic interactions between VAM3 and a SEC1 family member, VPS33, suggest the two proteins may act together to direct the docking and/or fusion of multiple transport intermediates ..
- Chou H, Dukovski D, Chambers M, Reinisch K, Walz T. CATCHR, HOPS and CORVET tethering complexes share a similar architecture. Nat Struct Mol Biol. 2016;23:761-3 pubmed publisher..We also show that HOPS, a tethering complex acting in the endolysosomal pathway, shares a similar architecture, thus suggesting that multisubunit tethering complexes use related structural frameworks. ..