VAM7/YGL212W Literature Guide Help

Other names published for VAM7: VPS43, VPL24, YGL212W

VAM7 - Protein-protein Interactions (25)

ReferenceOther Genes Addressed
Alpadi K, et al.  (2012) Sequential Analysis of Trans-SNARE Formation in Intracellular Membrane Fusion. PLoS Biol 10(1):e1001243
Izawa R, et al.  (2012) Distinct contributions of vacuolar Qabc- and R-SNARE proteins to membrane fusion specificity. J Biol Chem 287(5):3445-53
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
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
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
Chidambaram S, et al.  (2008) ENTH domain proteins are cargo adaptors for multiple SNARE proteins at the TGN endosome. J Cell Sci 121(Pt 3):329-38
Schluter C, et al.  (2008) Global Analysis of Yeast Endosomal Transport Identifies the Vps55/68 Sorting Complex. Mol Biol Cell 19(4):1282-1294
Fratti RA, et al.  (2007) Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification. J Biol Chem 282(20):14861-7
Jun Y, et al.  (2006) Reversible, cooperative reactions of yeast vacuole docking. EMBO J 25(22):5260-9
Roy R, et al.  (2006) Role of the Vam3p transmembrane segment in homodimerization and SNARE complex formation. Biochemistry 45(24):7654-60
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
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
Vollert CS and Uetz P  (2004) The phox homology (PX) domain protein interaction network in yeast. Mol Cell Proteomics 3(11):1053-64
Dilcher M, et al.  (2001) Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6. J Biol Chem 276(37):34537-44
Tsui MM, et al.  (2001) Selective formation of Sed5p-containing SNARE complexes is mediated by combinatorial binding interactions. Mol Biol Cell 12(3):521-38
Wang Y, et al.  (2001) Functional analysis of conserved structural elements in yeast syntaxin Vam3p. J Biol Chem 276(30):28598-605
Fukuda R, et al.  (2000) Functional architecture of an intracellular membrane t-SNARE. Nature 407(6801):198-202
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
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
Ungermann C and Wickner W  (1998) Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion. EMBO J 17(12):3269-76