Key result
KCNE1 proteins slow KCNQ1 activation kinetics ~100-fold through variable stoichiometry.
This review provides insights into the molecular mechanisms by which KCNE1 proteins modulate the gating of KCNQ1 cardiac potassium channels.
Advances molecular models of cardiac IKs; leaves open validation of variable stoichiometry in native myocytes.
KCNQ1 channel is a cardiac voltage-gated potassium channel. KCNQ1 forms an ion channel complex with auxiliary subunit KCNE proteins. KCNE proteins dramatically change KCNQ1 gating, for example, KCNE1 slows the activation kinetics of KCNQ1 channels 100-times slower. The mechanisms how KCNE1 proteins modify KCNQ1 channel gating have been central questions yet to be answered. Here we review recent findings regarding the structure-function relationships of KCNQ1/KCNE1 complex, including the stoichiometry and the functional interactions between the subunits, and discuss how KCNE1 proteins modify the gating of KCNQ1 channels.
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Nakajo et al. (2013) conducted a review in Cardiac voltage-gated ion channels (KCNQ1/KCNE1). KCNE1 modulation of KCNQ1 was evaluated. KCNE1 proteins dramatically change KCNQ1 gating by slowing the activation kinetics 100-times, with recent single-molecule imaging revealing a variable stoichiometry up to 4:4.
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