VAM7/YGL212W Literature Guide Help

Other names published for VAM7: VPS43, VPL24, YGL212W

VAM7 - Cellular Location (17)

ReferenceOther Genes Addressed
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
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
Wiederhold E, et al.  (2009) The yeast vacuolar membrane proteome. Mol Cell Proteomics 8(2):380-92
Collins KM and Wickner WT  (2007) Trans-SNARE complex assembly and yeast vacuole membrane fusion. Proc Natl Acad Sci U S A 104(21):8755-60
Fratti RA and Wickner W  (2007) Distinct targeting and fusion functions of the PX and SNARE domains of yeast vacuolar Vam7p. J Biol Chem 282(17):13133-8
Decker BL and Wickner WT  (2006) Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast. J Biol Chem 281(20):14523-8
Lee SA, et al.  (2006) Molecular mechanism of membrane docking by the Vam7p PX domain. J Biol Chem 281(48):37091-101
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
Starai VJ, et al.  (2005) Ion regulation of homotypic vacuole fusion in Saccharomyces cerevisiae. J Biol Chem 280(17):16754-62
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
Wang L, et al.  (2003) Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion. J Cell Biol 160(3):365-74
Cheever ML, et al.  (2001) Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes. Nat Cell Biol 3(7):613-8
Fukuda R, et al.  (2000) Functional architecture of an intracellular membrane t-SNARE. Nature 407(6801):198-202
Ungermann C, et al.  (2000) A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking. Proc Natl Acad Sci U S A 97(16):8889-91
Ungermann C, et al.  (1999) Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion. J Cell Biol 145(7):1435-42
Sato TK, et al.  (1998) Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking. Mol Cell Biol 18(9):5308-19