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2020 - Allosteric mechanism for KCNE1 modulation of KCNQ1 potassium channel activation

icon sp96  Syncropatch 768 PE publication in eLife (2020)

Authors:

Kuenze G., Vanoye C.G., Desai R.R., Adusumili S., Brewer K.R., Woods H., McDonald E.F., Sanders C.R., George Jr. A.L.

Journal:
eLife (2020) doi: 10.7554/eLife.57680


Abstract:

The function of the voltage-gated KCNQ1 potassium channel is regulated by co-assembly with KCNE auxiliary subunits. KCNQ1-KCNE1 channels generate the slow delayed rectifier current, IKs, which contributes to the repolarization phase of the cardiac action potential. A three amino acid motif (F57-T58-L59, FTL) in KCNE1 is essential for slow activation of KCNQ1-KCNE1 channels. However, how this motif interacts with KCNQ1 to control its function is unknown. Combining computational modeling with electrophysiological studies, we developed structural models of the KCNQ1-KCNE1 complex that suggest how KCNE1 controls KCNQ1 activation. The FTL motif binds at a cleft between the voltage-sensing and pore domains and appears to affect the channel gate by an allosteric mechanism. Comparison with the KCNQ1-KCNE3 channel structure suggests a common transmembrane-binding mode for different KCNEs and illuminates how specific differences in the interaction of their triplet motifs determine the profound differences in KCNQ1 functional modulation by KCNE1 versus KCNE3.


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