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Multiple PIP 2  dependent molecular processes including receptor activated phospholipase C activity occur at the neuronal plasma membranes, yet levels of this lipid at the plasma membrane are remarkably stable. Although the existence of unique pools of PIP 2  supporting these events has been proposed, the mechanism by which they are generated is unclear. In  Drosophila  photoreceptors, the hydrolysis of PIP 2  by G-protein coupled phospholipase C activity is essential for sensory transduction of photons. We identify dPIP5K as an enzyme essential for PIP 2  re-synthesis in photoreceptors. Loss of  dPIP5K  causes profound defects in the electrical response to light and light-induced PIP 2  dynamics at the photoreceptor membrane. Overexpression of dPIP5K was able to accelerate the rate of PIP 2  synthesis following light induced PIP 2  depletion. Other PIP 2  dependent processes such as endocytosis and cytoskeletal function were unaffected in photoreceptors lacking  dPIP5K  function. These results provide evidence for the existence of a unique dPIP5K dependent pool of PIP 2  required for normal  Drosophila  phototransduction. Our results define the existence of multiple pools of PIP 2  in photoreceptors generated by distinct lipid kinases and supporting specific molecular processes at neuronal membranes.

plos genetics

A dPIP5K Dependent Pool of Phosphatidylinositol 4,5 Bisphosphate (PIP2) Is Required for G-Protein Coupled Signal Transduction in Drosophila Photoreceptors