VAM3/YOR106W Literature Guide Help

Other names published for VAM3: PTH1, YOR106W

VAM3 - Cellular Location (22)

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
Logan MR, et al.  (2011) Functional analysis of RhoGDI inhibitory activity on vacuole membrane fusion. Biochem J 434(3):445-57
Wiederhold E, et al.  (2009) The yeast vacuolar membrane proteome. Mol Cell Proteomics 8(2):380-92
Brett CL and Merz AJ  (2008) Osmotic regulation of rab-mediated organelle docking. Curr Biol 18(14):1072-7
Isgandarova S, et al.  (2007) Stimulation of Actin Polymerization by Vacuoles via Cdc42p-dependent Signaling. J Biol Chem 282(42):30466-75
Roy R, et al.  (2006) Role of the Vam3p transmembrane segment in homodimerization and SNARE complex formation. Biochemistry 45(24):7654-60
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
Dietrich LE, et al.  (2005) ATP-independent control of Vac8 palmitoylation by a SNARE subcomplex on yeast vacuoles. J Biol Chem 280(15):15348-55
Brown CR, et al.  (2003) The Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery. J Biol Chem 278(28):25688-99
Rohde J, et al.  (2003) The transmembrane domain of Vam3 affects the composition of cis- and trans-SNARE complexes to promote homotypic vacuole fusion. J Biol Chem 278(3):1656-62
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
Wang L, et al.  (2002) Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle. Cell 108(3):357-69
Fukuda R, et al.  (2000) Functional architecture of an intracellular membrane t-SNARE. Nature 407(6801):198-202
Reggiori F, et al.  (2000) Polar transmembrane domains target proteins to the interior of the yeast vacuole. Mol Biol Cell 11(11):3737-49
Rehling P, et al.  (1999) Formation of AP-3 transport intermediates requires Vps41 function. Nat Cell Biol 1(6):346-53
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
Darsow T, et al.  (1998) Acidic di-leucine motif essential for AP-3-dependent sorting and restriction of the functional specificity of the Vam3p vacuolar t-SNARE. J Cell Biol 142(4):913-22
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
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
Darsow T, et al.  (1997) A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole. J Cell Biol 138(3):517-29
Wada Y, et al.  (1997) Vam3p, a new member of syntaxin related protein, is required for vacuolar assembly in the yeast Saccharomyces cerevisiae. J Cell Sci 110 ( Pt 11):1299-306