SK channels and calmodulin.
Calcium ions are Nature's most widely used signaling mechanism, mediating communication between pathways at virtually every physiological level. Ion channels are no exception, as the activities of a wide range of ion channels are intricately shaped by fluctuations in intracellular Ca(2+) levels. Mirroring the importance and the breadth of Ca(2+) signaling, free Ca(2+) levels are tightly controlled, and a myriad of Ca(2+) binding proteins transduce Ca(2+) signals, each with its own nuance, comprising a constantly changing symphony of metabolic activity. The founding member of Ca(2+) binding proteins is calmodulin (CaM), a small, acidic, modular protein endowed with gymnastic-like flexibility and E-F hand motifs that chelate Ca(2+) ions. In this review, I will trace the history that led to the realization that CaM serves as the Ca(2+)-gating cue for SK channels, the experiments that revealed that CaM is an intrinsic subunit of SK channels, and itself a target of regulation.
a Vollum Institute ; Oregon Health & Science University ; Portland , OR USA.
John P
JP
Adelman
D000818:Animals; D001030:Apamin / Q000378:metabolism; D002118:Calcium / Q000378:metabolism; D002147:Calmodulin / Q000378:metabolism*; D006801:Humans; D011188:Potassium / Q000378:metabolism; D051640:Small-Conductance Calcium-Activated Potassium Channels / Q000378:metabolism*
D002147:Calmodulin; D051640:Small-Conductance Calcium-Activated Potassium Channels; D001030:Apamin; D011188:Potassium; D002118:Calcium
Ca2+-gating; E-F hands; Paramecium; SK channel; calmodulin; curing; intrinsic subunit