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Pah1p negatively regulates the expression of V-ATPase genes as well as vacuolar acidification

Sherr, Goldie Libby, LaMassa, Nicole, Li, Erxin, Phillips, Greg, Shen, Chang-Hui
Biochemical and biophysical research communications 2017 v.491 pp. 693-700
H-transporting ATP synthase, acidification, biosynthesis, enzyme activity, genes, homeostasis, inositols, phospholipids, quantitative polymerase chain reaction, vacuoles, yeasts
In yeast, PAH1 plays an important role in cell homeostasis and lipid biosynthesis. PAH1 encodes for the PA phosphatase, Pah1p, which is responsible for de novo TAG and phospholipid synthesis. It has been suggested that the lack of Pah1p causes irregular vacuolar morphology and dysfunctional V-ATPase pump activity. However, the molecular connection between Pah1p and V-ATPase activity has remained unclear. Through real-time PCR, we have shown that PAH1 is maximally induced at the stationary stage in the presence of inositol. We also found that vacuoles were less fragmented when PAH1 is maximally expressed. Subsequently, we observed that vacuoles from pah1Δ cells were more acidic than those in WT cells. Furthermore, V-ATPase genes were upregulated in the absence of Pah1p. These results suggest that Pah1p plays an important role in vacuolar activity by negatively regulating the expression of V-ATPase genes. As such, we provide evidence to show the role of Pah1p in vacuolar acidification and fragmentation.