Abstract
G protein-gated inward rectifier potassium (KG) channel underlies the deceleration of the heartbeat upon vagal nerve stimulation and the formation of slow inhibitory postsynaptic membrane potential in neurons. The KG channels are tetramers and either heteromeric or homomeric assembly of Kir3.1-Kir3.4 subunits and their splicing variants. Like the other inward rectifiers, the KG channel possesses two distinct domains, a transmembrane domain and a cytoplasmic domain. The cytoplasmic domain of KG channel containing either Kir3.2 or Kir3.4 is thought to interact with channel activators such as G protein βγ subunit, intracellular Na+ and PIP2, and control the channel gating at the transmembrane domain.
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