Regulation of PI4P levels by PI4KIIIα during G-protein-coupled PLC signaling in <i>Drosophila</i> photoreceptors.

ABSTRACT: The activation of phospholipase C (PLC) is a conserved mechanism of receptor-activated cell signaling at the plasma membrane. PLC hydrolyzes the minor membrane lipid phosphatidylinositol 4,5-bisphosphate [PI(4,5)P₂], and continued signaling requires the resynthesis and availability of PI(4,5)P₂ at the plasma membrane. PI(4,5)P₂ is synthesized by the phosphorylation of phosphatidylinositol 4-phosphate (PI4P). Thus, a continuous supply of PI4P is essential to support ongoing PLC signaling. While the enzyme PI4KA has been identified as performing this function in cultured mammalian cells, its function in the context of an in vivo physiological model has not been established. In this study, we show that, in Drosophila photoreceptors, PI4KIIIα acti

SUBMITTER: Balakrishnan SS 

PROVIDER: S-EPMC6104824 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature