Affiliation:
1. National Centre for Biological Sciences-TIFR, GKVK Campus, Bellary Road, Bangalore 560065, India
2. TIFR Center for Interdisciplinary Science, Hyderabad, 500107, India
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 to perform 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 activity is required to support signaling during G-protein coupled PLC activation. Depletion of PI4KIIIα results in impaired electrical responses to light and reduced plasma membrane levels of PI4P and PI(4,5)P2. Depletion of conserved proteins Efr3 and TTC7 that assemble PI4KIIIα at the plasma membrane also results in an impaired light response and reduced plasma membrane PI4P and PI(4,5)P2 levels. Thus PI4KIIIα activity at the plasma membrane generates PI4P and supports PI(4,5)P2 levels during receptor activated PLC signaling.
Publisher
The Company of Biologists
Cited by
29 articles.
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