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Phosphatidylinositol 4,5-bisphosphate (PIP 2 ) is a membrane phospholipid that regulates the function of multiple ion channels, including some members of the voltage-gated potassium (Kv) channel superfamily. The PIP 2  sensitivity of Kv channels is well established for all five members of the Kv7 family and for Kv1.2 channels; however, regulation of other Kv channels by PIP 2  remains unclear. Here, we investigate the effects of PIP 2  on Kv2.1 channels by applying exogenous PIP 2  to the cytoplasmic face of excised membrane patches, activating muscarinic receptors (M1R), or depleting endogenous PIP 2  using a rapamycin-translocated 5-phosphatase (FKBP-Inp54p). Exogenous PIP 2  rescued Kv2.1 channels from rundown and partially prevented the shift in the voltage-dependence of inactivation observed in inside-out patch recordings. Native PIP 2  depletion by the recruitment of FKBP-Insp54P or M1R activation in whole-cell experiments, induced a shift in the voltage-dependence of inactivation, an acceleration of the closed-state inactivation, and a delayed recovery of channels from inactivation. No significant effects were observed on the activation mechanism by any of these treatments. Our data can be modeled by a 13-state allosteric model that takes into account that PIP 2  depletion facilitates inactivation of Kv2.1. We propose that PIP 2  regulates Kv2.1 channels by interfering with the inactivation mechanism.

Regulation of Kv2.1 channel inactivation by phosphatidylinositol 4,5-bisphosphate