KCNE1 binds to the KCNQ1 pore to regulate potassium channel activity

Yonathan F. Melman, Sung Yon Um, Andrew Krumerman, Anna Kagan, Thomas V. McDonald

Research output: Contribution to journalArticlepeer-review

126 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)927-937
Number of pages11
Issue number6
StatePublished - Jun 24 2004

ASJC Scopus subject areas

  • Neuroscience(all)


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