Sherr Goldie Libby, LaMassa Nicole, Li Erxin, Phillips Greg, Shen Chang-Hui
Department of Biology, College of Staten Island, City University of New York, 2800 Victory Blvd, Staten Island, NY 10314, United States; PhD Program in Biology, The Graduate Center, City University of New York, 365 Fifth Avenue, New York 10016, United States.
Department of Biology, College of Staten Island, City University of New York, 2800 Victory Blvd, Staten Island, NY 10314, United States.
Biochem Biophys Res Commun. 2017 Sep 23;491(3):693-700. doi: 10.1016/j.bbrc.2017.07.127. Epub 2017 Jul 26.
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.
在酵母中,PAH1在细胞内稳态和脂质生物合成中发挥重要作用。PAH1编码PA磷酸酶Pah1p,它负责从头合成三酰甘油(TAG)和磷脂。有人提出,缺乏Pah1p会导致液泡形态不规则和V-ATP酶泵活性功能失调。然而,Pah1p与V-ATP酶活性之间的分子联系仍不清楚。通过实时定量PCR,我们发现,在肌醇存在的情况下,PAH1在稳定期被最大程度地诱导表达。我们还发现,当PAH1最大程度表达时,液泡的碎片化程度较低。随后,我们观察到,pah1Δ细胞的液泡比野生型(WT)细胞的液泡酸性更强。此外,在缺乏Pah1p的情况下,V-ATP酶基因上调。这些结果表明,Pah1p通过负向调节V-ATP酶基因的表达,在液泡活性中发挥重要作用。因此,我们提供了证据,证明Pah1p在液泡酸化和碎片化中的作用。