VPS16/YPL045W Literature Guide Help

Other names published for VPS16: SVL6, VAM9, VPT16, YPL045W

VPS16 - Function/Process (29)

ReferenceOther Genes Addressed
Alpadi K, et al.  (2012) Sequential Analysis of Trans-SNARE Formation in Intracellular Membrane Fusion. PLoS Biol 10(1):e1001243
Zick M and Wickner W  (2012) Phosphorylation of the effector complex HOPS by the vacuolar kinase Yck3p confers Rab nucleotide specificity for vacuole docking and fusion. Mol Biol Cell 23(17):3429-37
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
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
Xu H, et al.  (2010) HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion. EMBO J 29(12):1948-60
Anand VC, et al.  (2009) Genome-wide analysis of AP-3-dependent protein transport in yeast. Mol Biol Cell 20(5):1592-604
Hickey CM, et al.  (2009) The Major Role of the Rab Ypt7p in Vacuole Fusion Is Supporting HOPS Membrane Association. J Biol Chem 284(24):16118-25
Mima J and Wickner W  (2009) Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion. Proc Natl Acad Sci U S A 106(38):16191-6
Schauer A, et al.  (2009) Vacuolar functions determine the mode of cell death. Biochim Biophys Acta 1793(3):540-5
Stroupe C, et al.  (2009) From the Cover: Feature Article: Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components. Proc Natl Acad Sci U S A 106(42):17626-33
Mima J, et al.  (2008) Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones. EMBO J 27(15):2031-42
Starai VJ, et al.  (2008) HOPS Proofreads the trans-SNARE Complex for Yeast Vacuole Fusion. Mol Biol Cell 19(6):2500-8
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
Starai VJ, et al.  (2007) Excess vacuolar SNAREs drive lysis and Rab bypass fusion. Proc Natl Acad Sci U S A 104(34):13551-8
Hancock LC, et al.  (2006) Genomic analysis of the Opi- phenotype. Genetics 173(2):621-34
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
Dimmer KS, et al.  (2002) Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae. Mol Biol Cell 13(3):847-53
Koning AJ, et al.  (2002) Mutations that affect vacuole biogenesis inhibit proliferation of the endoplasmic reticulum in Saccharomyces cerevisiae. Genetics 160(4):1335-52
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
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
Zhang S, et al.  (1999) Mutations in VPS16 and MRT1 stabilize mRNAs by activating an inhibitor of the decapping enzyme. Mol Cell Biol 19(11):7568-76
Zheng B, et al.  (1998) Isolation of yeast mutants defective for localization of vacuolar vital dyes. Proc Natl Acad Sci U S A 95(20):11721-6
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
Bode HP, et al.  (1995) Iron sequestration by the yeast vacuole. A study with vacuolar mutants of Saccharomyces cerevisiae. Eur J Biochem 228(2):337-42
Dulic V and Riezman H  (1990) Saccharomyces cerevisiae mutants lacking a functional vacuole are defective for aspects of the pheromone response. J Cell Sci 97 ( Pt 3):517-25
Robinson JS, et al.  (1988) Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol Cell Biol 8(11):4936-48