Genomes and Genes
Gene Symbol: VTA1
Species: Saccharomyces cerevisiae S288c
- Rue S, Mattei S, Saksena S, Emr S. Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting. Mol Biol Cell. 2008;19:475-84 pubmed..Moreover, this approach revealed that Ist1-Did2 and Vta1-Vps60 compose two functional units...
- Dimaano C, Jones C, Hanono A, Curtiss M, Babst M. Ist1 regulates Vps4 localization and assembly. Mol Biol Cell. 2008;19:465-74 pubmed..The activity of the MVB pathway might be in part determined by outcome of these two competing activities. ..
- Nickerson D, West M, Odorizzi G. Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes. J Cell Biol. 2006;175:715-20 pubmed
- Azmi I, Davies B, Dimaano C, Payne J, Eckert D, Babst M, et al. Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1. J Cell Biol. 2006;172:705-17 pubmed..However, regulation of Vps4 function is not understood. We characterize Vta1 as a positive regulator of Vps4 both in vivo and in vitro...
- Scott A, Chung H, Gonciarz Swiatek M, Hill G, Whitby F, Gaspar J, et al. Structural and mechanistic studies of VPS4 proteins. EMBO J. 2005;24:3658-69 pubmed..weight complexes and active, membrane-associated double-ring structures that bind ATP and coassemble with LIP5/Vta1. Finally, HIV-1 budding was inhibited by mutations in a loop that projects into the center of the modeled hVPS4B ..
- Yang D, Hurley J. Structural role of the Vps4-Vta1 interface in ESCRT-III recycling. Structure. 2010;18:976-84 pubmed publisher..Vps4 assembles on its membrane-bound ESCRT-III substrate with its cofactor, Vta1. The crystal structure of the dimeric VSL domain of yeast Vta1 with the small ATPase and the betadomains of Vps4 ..
- Vajjhala P, Catchpoole E, Nguyen C, Kistler C, Munn A. Vps4 regulates a subset of protein interactions at the multivesicular endosome. FEBS J. 2007;274:1894-907 pubmed..Our studies indicate that the MIT domain has a dual role in substrate binding and recruitment to endosomes and indicate that Vps4 disassembles the MVB sorting machinery by direct effects on multiple proteins. ..
- Nickerson D, West M, Henry R, Odorizzi G. Regulators of Vps4 ATPase activity at endosomes differentially influence the size and rate of formation of intralumenal vesicles. Mol Biol Cell. 2010;21:1023-32 pubmed publisher..These morphological effects probably result from Vps4-mediated manipulations of ESCRT-III, because we show dissociation of ESCRT-0, -I, and -II from endosomes is not directly dependent on Vps4 activity. ..
- Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, et al. Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. J Biol Chem. 2012;287:43899-908 pubmed publisher..Vps4 activity is stimulated by the interaction between Vta1 and Vps60, but the structural basis for this interaction is unclear...
- Norgan A, Davies B, Azmi I, Schroeder A, Payne J, Lynch G, et al. Relief of autoinhibition enhances Vta1 activation of Vps4 via the Vps4 stimulatory element. J Biol Chem. 2013;288:26147-56 pubmed publisher..The AAA-ATPase Vps4 is required for ESCRT function, and its full activity is dependent upon the co-factor Vta1. The Vta1 carboxyl-terminal Vta1 SBP1 Lip5 (VSL) domain stimulates Vps4 function by facilitating oligomerization of ..
- Shestakova A, Hanono A, Drosner S, Curtiss M, Davies B, Katzmann D, et al. Assembly of the AAA ATPase Vps4 on ESCRT-III. Mol Biol Cell. 2010;21:1059-71 pubmed publisher..steps are mediated by a complex network of at least 12 distinct interactions between Vps4, ESCRT-III, Ist1, Vta1, and Did2. The order of events leading to active, ESCRT-III-associated Vps4 is poorly understood...
- Vajjhala P, Wong J, To H, Munn A. The beta domain is required for Vps4p oligomerization into a functionally active ATPase. FEBS J. 2006;273:2357-73 pubmed..In addition, it is required for interaction with Vta1p, which works in concert with Vps4p in vivo...
- Sciskala B, Kölling R. Interaction maps of the Saccharomyces cerevisiae ESCRT-III protein Snf7. Eukaryot Cell. 2013;12:1538-46 pubmed publisher..In summary, our study argues against the view that the ESCRT cycle is governed by single one-to-one interactions between individual components and emphasizes the network character of the ESCRT interactions. ..
- Monroe N, Han H, Gonciarz M, Eckert D, Karren M, Whitby F, et al. The oligomeric state of the active Vps4 AAA ATPase. J Mol Biol. 2014;426:510-25 pubmed publisher..The Vta1p activator binds hexameric yeast Vps4p without changing the oligomeric state of Vps4p, implying that the active ..
- Davies B, Norgan A, Payne J, Schulz M, Nichols M, TAN J, et al. Vps4 stimulatory element of the cofactor Vta1 contacts the ATPase Vps4 Î±7 and Î±9 to stimulate ATP hydrolysis. J Biol Chem. 2014;289:28707-18 pubmed publisher..Vps4 ATPase activity modulates ESCRT function and is itself modulated by its cofactor Vta1 and its substrate ESCRT-III...
- Tan J, Davies B, Payne J, Benson L, Katzmann D. Conformational Changes in the Endosomal Sorting Complex Required for the Transport III Subunit Ist1 Lead to Distinct Modes of ATPase Vps4 Regulation. J Biol Chem. 2015;290:30053-65 pubmed publisher..Together, these data support a model in which Ist1-Did2 interactions during ESCRT-III polymerization coordinate Vps4 activity with the timing of ESCRT-III disassembly. ..
- Monroe N, Han H, Shen P, Sundquist W, Hill C. Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase. elife. 2017;6: pubmed publisher..We report a 4.3 Å resolution cryo-EM structure of the active Vps4 hexamer with its cofactor Vta1, ADP·BeFx, and an ESCRT-III substrate peptide...
- Shiflett S, Vaughn M, Huynh D, Kaplan J, Ward D. Bph1p, the Saccharomyces cerevisiae homologue of CHS1/beige, functions in cell wall formation and protein sorting. Traffic. 2004;5:700-10 pubmed..Together, these data suggest that Bph1p associates with a membrane and is involved in protein sorting and cell wall formation. ..