Septins tune lipid kinase activity and PI(4,5)P₂ turnover during G-protein-coupled PLC signalling in vivo.

ABSTRACT: Phosphatidylinositol 4,5-bisphosphate [PI(4,5)P₂] hydrolysis by phospholipase C (PLC) is a conserved mechanism of signalling. Given the low abundance of PI(4,5)P₂, its hydrolysis needs to be coupled to resynthesis to ensure continued PLC activity; however, the mechanism by which depletion is coupled to resynthesis remains unknown. PI(4,5)P₂ synthesis is catalyzed by the phosphorylation of phosphatidylinositol 4 phosphate (PI4P) by phosphatidylinositol 4 phosphate 5 kinase (PIP5K). In Drosophila photoreceptors, photon absorption is transduced into PLC activity and during this process, PI(4,5)P₂ is resynthesized by a PIP5K. However, the mechanism by which PIP5K activity is coupled to PI(4,5)P₂ hydrolysis is unknown. In this study,

SUBMITTER: Kumari A 

PROVIDER: S-EPMC8921834 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature