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G-protein-gated inward rectifier potassium (GIRK) channels are regulated by G proteins and PIP 2 . Here, using cryo-EM single particle analysis we describe the equilibrium ensemble of structures of neuronal GIRK2 as a function of the C8-PIP 2  concentration. We find that PIP 2  shifts the equilibrium between two distinguishable structures of neuronal GIRK (GIRK2), extended and docked, towards the docked form. In the docked form the cytoplasmic domain, to which G βγ  binds, becomes accessible to the cytoplasmic membrane surface where G βγ  resides. Furthermore, PIP 2  binding reshapes the G βγ  binding surface on the cytoplasmic domain, preparing it to receive G βγ . We find that cardiac GIRK (GIRK1/4) can also exist in both extended and docked conformations. These findings lead us to conclude that PIP 2  influences GIRK channels in a structurally similar manner to Kir2.2 channels. In Kir2.2 channels, the PIP 2 -induced conformational changes open the pore. In GIRK channels, they prepare the channel for activation by G βγ .

Cryo-EM analysis of PIP 2 regulation in mammalian GIRK channels