Genomes and Genes
Gene Symbol: VPS16
Description: tethering complex subunit VPS16
Alias: CVT15, SVL6, VAM9, VPT16, tethering complex subunit VPS16
Species: Saccharomyces cerevisiae S288c
- Krämer L, Ungermann C. HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites. Mol Biol Cell. 2011;22:2601-11 pubmed publisher..We show that homotypic fusion and protein sorting (HOPS) binds Vam7 via its subunits Vps16 and Vps18...
- 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. ..
- 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..As HOPS Vps39 is also found at endosomes, our data thus suggest that these tethering complexes follow defined but distinct assembly pathways, and may undergo transition by simple subunit interchange. ..
- Angers C, Merz A. HOPS interacts with Apl5 at the vacuole membrane and is required for consumption of AP-3 transport vesicles. Mol Biol Cell. 2009;20:4563-74 pubmed publisher..We propose that AP-3 remains associated with budded vesicles, interacts with Vps41 and HOPS upon vesicle docking at the vacuole, and finally dissociates during docking or 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. ..
- Kulkarni A, Alpadi K, Namjoshi S, Peters C. A tethering complex dimer catalyzes trans-SNARE complex formation in intracellular membrane fusion. Bioarchitecture. 2012;2:59-69 pubmed..Here we report a novel finding that a HOPS tethering complex dimer catalyzes Rab GTPase-dependent formation of a topologically preferred QbQcR-Qa trans-SNARE 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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..the binding sites for vacuolar SNAREs and the Habc domain are located in the large head of the HOPS complex, where Vps16 and Vps33 have been identified before...
- Jasnos L, Korona R. Epistatic buffering of fitness loss in yeast double deletion strains. Nat Genet. 2007;39:550-4 pubmed..Based on our data and former theoretical work, we suggest that epistasis is likely to diminish the negative effects of mutations when the ability to produce biomass at high rates contributes significantly to fitness. ..
- 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. ..
- 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
- Miner G, Starr M, Hurst L, Sparks R, Padolina M, Fratti R. The Central Polybasic Region of the Soluble SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Vam7 Affects Binding to Phosphatidylinositol 3-Phosphate by the PX (Phox Homology) Domain. J Biol Chem. 2016;291:17651-63 pubmed publisher..PI3P binding was inhibited when the PX domain mutant Y42A was introduced into Vam7-6A to make Vam7-7A. Thus the Vam7 PBR affects PI3P binding by the PX domain and in turn affects binding to SNAREs and HOPS to support efficient fusion. ..
- 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..This is the first report demonstrating the involvement of a single syntaxin with two SM proteins at the same organelle. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..