Abstract
BK channels are high conductance potassium channels synergistically activated by voltage and Ca2+. Their molecular architecture consists of homotetramers of α-subunits containing a membrane-spanning domain and a cytosolic structure including tandems of RCK-like domains (RCK1 and RCK2). These RCKs contain distinct high affinity Ca2+-binding sites mediating channel activation (Horrigan and Aldrich, 2002; Sweet and Cox, 2008). Full-length Cryo-EM structures of the channel revealed intersubunit interactions between these RCKs (Tao et al., 2017; Tao et al., 2019).
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