Protein kinase C regulates the expression and function of various ion channels via phosphorylation, often by allosterically modulating the dependence of these channels on PIP2 for gating.
Ion channels are integral membrane proteins whose gating has been increasingly shown to depend on the presence of the low-abundance membrane phospholipid, phosphatidylinositol (4,5) bisphosphate. The expression and function of ion channels is tightly regulated via protein phosphorylation by specific kinases, including various PKC isoforms. Several channels have further been shown to be regulated by PKC through altered surface expression, probability of channel opening, shifts in voltage dependence of their activation, or changes in inactivation or desensitization. In this review, we survey the impact of phosphorylation of various ion channels by PKC isoforms and examine the dependence of phosphorylated ion channels on phosphatidylinositol (4,5) bisphosphate as a mechanistic endpoint to control channel gating.
Gada et al. (Mon,) reported a review. Protein kinase C regulates the expression and function of various ion channels via phosphorylation, often by allosterically modulating the dependence of these channels on PIP2 for gating.