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Probing the interaction between KCNE2 and KCNQ1 in their transmembrane regions.
Liu XS
,
Zhang M
,
Jiang M
,
Wu DM
,
Tseng GN
.
???displayArticle.abstract??? KCNE1-KCNE5 are single membrane-spanning proteins that associate with voltage-gated potassium channels to diversify their function. Other than the KCNQ1/KCNE1 complex, little is known about how KCNE proteins work. We focus on KCNE2, which associates with KCNQ1 to form K channels critical for gastric acid secretion in parietal cells. We use cysteine (Cys)-scanning mutagenesis to probe the functional role of residues along the KCNE2 transmembrane domain (TMD) in modulating KCNQ1 function. There is an alpha-helical periodicity in how Cys substitutions along the KCNE2TMD perturb KCNQ1 pore conductance/ion selectivity. However, positions where Cys substitutions perturb KCNQ1 gating kinetics cluster to the extracellular end and cytoplasmic half of the KCNE2TMD. This is the first systematic perturbation analysis of a KCNE TMD. We propose that the KCNE2TMD adopts an alpha-helical secondary structure with one face making intimate contact with the KCNQ1 pore domain, while the contacts with the KCNQ1 voltage-sensing domain appear more dynamic.
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