VAM3/YOR106W Literature Guide Help

Other names published for VAM3: PTH1, YOR106W

VAM3 - Protein Sequence Features (17)

ReferenceOther Genes Addressed
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
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
Schwartz ML and Merz AJ  (2009) Capture and release of partially zipped trans-SNARE complexes on intact organelles. J Cell Biol 185(3):535-49
Starai VJ, et al.  (2008) HOPS Proofreads the trans-SNARE Complex for Yeast Vacuole Fusion. Mol Biol Cell 19(6):2500-8
Schindler C and Spang A  (2007) Interaction of SNAREs with ArfGAPs Precedes Recruitment of Sec18p/NSF. Mol Biol Cell 18(8):2852-63
Roy R, et al.  (2006) Role of the Vam3p transmembrane segment in homodimerization and SNARE complex formation. Biochemistry 45(24):7654-60
Dulubova I, et al.  (2001) Vam3p structure reveals conserved and divergent properties of syntaxins. Nat Struct Biol 8(3):258-64
Laage R and Ungermann C  (2001) The N-terminal domain of the t-SNARE Vam3p coordinates priming and docking in yeast vacuole fusion. Mol Biol Cell 12(11):3375-85
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
Rehling P, et al.  (1999) Formation of AP-3 transport intermediates requires Vps41 function. Nat Cell Biol 1(6):346-53
Abeliovich H, et al.  (1998) Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures. J Biol Chem 273(19):11719-27
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
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