High impact information on VAC7

• In both the absence and presence of Vac7p, the Vac14p-Fig4p complex controls the hyperosmotic shock-induced increase in PI3,5P2 levels [1].
• The Vac14p-Fig4p complex acts independently of Vac7p and couples PI3,5P2 synthesis and turnover [1].
• Interestingly, deletion of VAC7 also results in an enlarged vacuole morphology and has no detectable PtdIns(3,5)P2, suggesting that Vac7p functions as an upstream regulator, perhaps in a complex with Fab1p [2].
• VAC7 encodes a novel 128-kDa protein that is localized at the vacuole membrane [3].
• VAC7 encodes a 128-kDa transmembrane protein that localizes to vacuolar membranes [4].

Biological context of VAC7

• Surprisingly, despite the apparent lack of quantitative vacuolar inheritance, all daughter cells of vac6 and vac7 had obtained a vacuole before cell division [5].

Anatomical context of VAC7

• Both vac7 and fab1 null mutants have dramatically enlarged vacuoles and cannot grow at elevated temperatures [4].

Associations of VAC7 with chemical compounds

• In the BY4742 genetic background, loss of Vac14 causes much more penetrant effects on phosphoinositide metabolism and vacuolar trafficking than does loss of Vac7, another regulator of Fab1 [6].

Regulatory relationships of VAC7

• Genetic studies have indicated that Fab1 kinase is positively regulated by Vac7 and Vac14; deletion of either gene results in ablation of PtdIns(3,5)P2 synthesis and the formation of a grossly enlarged vacuole [7].

Other interactions of VAC7

• Additionally, vac7Delta mutants have nearly undetectable levels of PtdIns(3,5)P(2), suggesting that Vac7 functions to regulate Fab1 kinase activity [4].

References