Key result
The KCNE3 transmembrane domain is sufficient for assembly with and modulation of KCNQ1 channels, suggesting a bipartite model for KCNQ1 modulation by KCNE1 and KCNE3 subunits.
Population
In vitro model expressing KCNQ1 channels and KCNE3/KCNE1 mutants
Design
Preclinical
Authors
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Swapping the KCNE transmembrane triplet alters KCNQ1 modulation; extends prior proposals but leaves open relevance in native channels.
The study proposes a bipartite model for KCNQ1 modulation where the KCNE3 transmembrane domain is sufficient for channel assembly and modulation, overriding the COOH terminus contribution.
Gage et al. (2004) studied this question. KCNE3 truncation mutants was evaluated on KCNQ1 channel complex basal activation and modulation. The KCNE3 transmembrane domain is sufficient for assembly with and modulation of KCNQ1 channels, suggesting a bipartite model for KCNQ1 modulation by KCNE1 and KCNE3 subunits.
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