KCNE1 binds to the KCNQ1 pore to regulate potassium channel activity

被引:127
作者
Melman, YF
Um, SY
Krumerman, A
Kagan, A
McDonald, TV
机构
[1] Albert Einstein Coll Med, Dept Med, Bronx, NY 10461 USA
[2] Albert Einstein Coll Med, Dept Mol Pharmacol, Bronx, NY 10461 USA
关键词
D O I
10.1016/j.neuron.2004.06.001
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Potassium channels control the resting membrane potential and excitability of biological tissues. Many voltage-gated potassium channels are controlled through interactions with accessory subunits of the KCNE family through mechanisms still not known. Gating of mammalian channel KCNQ1 is dramatically regulated by KCNE subunits. We have found that multiple segments of the channel pore structure bind to the accessory protein KCNE1. The sites that confer KCNE1 binding are necessary for the functional interaction, and all sites must be present in the channel together for proper regulation by the accessory subunit. Specific gating control is localized to a single site of interaction between the ion channel and accessory subunit. Thus, direct physical interaction with the ion channel pore is the basis of KCNE1 regulation of K+ channels.
引用
收藏
页码:927 / 937
页数:11
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