VPS33/YLR396C Literature Guide Help

Other names published for VPS33: CLS14, MET27, PEP14, SLP1, VAM5, VPL25, VPT33, YLR396C

VPS33 - Protein-protein Interactions (29)

ReferenceOther Genes Addressed
Alpadi K, et al.  (2012) Sequential Analysis of Trans-SNARE Formation in Intracellular Membrane Fusion. PLoS Biol 10(1):e1001243
Karunakaran S, et al.  (2012) SNAREs, HOPS and regulatory lipids control the dynamics of vacuolar actin during homotypic fusion in S. cerevisiae. J Cell Sci 125(Pt 7):1683-92
Kulkarni A, et al.  (2012) A tethering complex dimer catalyzes trans-SNARE complex formation in intracellular membrane fusion. Bioarchitecture 2(2):59-69
Lobingier BT and Merz AJ  (2012) Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex. Mol Biol Cell 23(23):4611-22
Kramer L and Ungermann C  (2011) HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites. Mol Biol Cell 22(14):2601-11
Plemel RL, et al.  (2011) Subunit organization and Rab interactions of Vps-C protein complexes that control endolysosomal membrane traffic. Mol Biol Cell 22(8):1353-63
Xu H, et al.  (2011) A lipid-anchored SNARE supports membrane fusion. Proc Natl Acad Sci U S A 108(42):17325-30
Hickey CM and Wickner W  (2010) HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly. Mol Biol Cell 21(13):2297-305
Ostrowicz CW, et al.  (2010) Defined subunit arrangement and rab interactions are required for functionality of the HOPS tethering complex. Traffic 11(10):1334-46
Pieren M, et al.  (2010) The SM protein Vps33 and the t-SNARE H(abc) domain promote fusion pore opening. Nat Struct Mol Biol 17(6):710-7
Angers CG and Merz AJ  (2009) HOPS interacts with Apl5 at the vacuole membrane and is required for consumption of AP-3 transport vesicles. Mol Biol Cell 20(21):4563-74
Cabrera M, et al.  (2009) Vps41 phosphorylation and the Rab Ypt7 control the targeting of the HOPS complex to endosome-vacuole fusion sites. Mol Biol Cell 20(7):1937-48
Hu SH, et al.  (2007) Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide binding mode of Sec1/Munc18 proteins. Proc Natl Acad Sci U S A 104(21):8773-8
Peplowska K, et al.  (2007) The CORVET Tethering Complex Interacts with the Yeast Rab5 Homolog Vps21 and Is Involved in Endo-Lysosomal Biogenesis. Dev Cell 12(5):739-50
Jun Y, et al.  (2006) Reversible, cooperative reactions of yeast vacuole docking. EMBO J 25(22):5260-9
Stroupe C, et al.  (2006) Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p. EMBO J 25(8):1579-89
Collins KM, et al.  (2005) Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion. EMBO J 24(10):1775-86
Subramanian S, et al.  (2004) The Sec1/Munc18 protein, Vps33p, functions at the endosome and the vacuole of Saccharomyces cerevisiae. Mol Biol Cell 15(6):2593-605
Thorngren N, et al.  (2004) A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion. EMBO J 23(14):2765-76
Wang CW, et al.  (2003) Yeast homotypic vacuole fusion requires the Ccz1-Mon1 complex during the tethering/docking stage. J Cell Biol 163(5):973-85
Aloy P and Russell RB  (2002) Interrogating protein interaction networks through structural biology. Proc Natl Acad Sci U S A 99(9):5896-901
Lazar T, et al.  (2002) 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 81(12):635-46
Dulubova I, et al.  (2001) Vam3p structure reveals conserved and divergent properties of syntaxins. Nat Struct Biol 8(3):258-64
Peterson MR and Emr SD  (2001) The class C Vps complex functions at multiple stages of the vacuolar transport pathway. Traffic 2(7):476-86
Sato TK, et al.  (2000) Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion. Mol Cell 6(3):661-71
Seals DF, et al.  (2000) A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion. Proc Natl Acad Sci U S A 97(17):9402-7
Wurmser AE, et al.  (2000) New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion. J Cell Biol 151(3):551-62
Ungermann C, et al.  (1998) A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion. J Cell Biol 140(1):61-9
Rieder SE and Emr SD  (1997) A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuole. Mol Biol Cell 8(11):2307-27