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dc.contributor.authorZhong, Xiaotian
dc.contributor.authorMalhotra, Rajeev
dc.contributor.authorGuidotti, Guido
dc.date.accessioned2019-10-03T17:42:23Z
dc.date.issued2000
dc.identifier.citationZhong, Xiaotian, Rajeev Malhotra, and Guido Guidotti. 2000. “Regulation of Yeast Ectoapyrase Ynd1p Activity by Activator Subunit Vma13p of Vacuolar H+-ATPase.” Journal of Biological Chemistry 275 (45): 35592–99. https://doi.org/10.1074/jbc.m006932200.
dc.identifier.issn0021-9258
dc.identifier.issn1083-351X
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41467497*
dc.description.abstractCD39-like ectoapyrases are involved in protein and lipid glycosylation in the Golgi lumen of Saccharomyces cerevisiae, By using a two-hybrid screen, we found that air activator subunit (Vma13p) of yeast vacuolar HC ATPase:CV-ATPase) binds to the cytoplasmic domain of Ynd1p, a yeast ectoapyrase. Interaction of Ynd1p with Vma13p was demonstrated by direct binding and coimmunoprecipitation, Surprisingly, the membrane-bound ADPase activity of Ynd1p in a vma13 Delta mutant was drastically increased compared with that of Ynd1p in VMA13 cells. A similar increase in the apyrase activity of Ynd1p was found in a vma1 Delta mutant, in which the catalytic subunit A of V-ATPase is missing, and the membrane peripheral subunits including Vma13p are dissociated from the membranes. However, the E286Q mutant of VMA1, which assembles inactive V-ATPase complex including Vma13p in the membrane, retained wild type levels' of Ynd1p activity, demonstrating that the presence of Vmal13p rather than the function of V-ATPase in the membrane represses Ynd1p activity. These results suggest that association of Vma13p with the cytoplasmic domain of Ynd1p regulates its apyrase activity in the Golgi lumen.
dc.language.isoen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology
dash.licenseLAA
dc.titleRegulation of Yeast Ectoapyrase Ynd1p Activity by Activator Subunit Vma13p of Vacuolar H + -ATPase
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalThe Journal of Biological Chemistry
dash.depositing.authorGuidotti, Guido::abe40fd7ddb25ca3706ce593535bc2f0::600
dc.date.available2019-10-03T17:42:23Z
dash.workflow.comments1Science Serial ID 105814
dc.identifier.doi10.1074/jbc.M006932200
dash.source.volume275;45
dash.source.page35592-35599


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