Key result
Mutation of basic residues (Lys-354, Lys-358, Arg-360, Lys-362) in the KCNQ1 proximal C terminus abolishes phosphoinositide binding and shifts channel activation toward depolarized potentials.
Population
KCNQ1/KCNE1 potassium channel complex
Comparison
Mutation of basic residues to alanine and… vs Wild-type KCNQ1 channel
Design
Preclinical
Authors
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Disrupts KCNQ1 gating in vitro; leaves open relevance to native cardiac IKs or arrhythmia mechanisms.
Identifies a specific cluster of basic residues in the KCNQ1 proximal C terminus that are essential for PIP2 binding and subsequent channel regulation.
Thomas et al. (2010) studied this question. Mutation of basic residues (Lys-354, Lys-358, Arg-360, Lys-362) in KCNQ1 vs. Wild-type KCNQ1 was evaluated on Binding to phosphoinositides and voltage dependence of channel activation. Mutation of basic residues (Lys-354, Lys-358, Arg-360, Lys-362) in the KCNQ1 proximal C terminus abolishes phosphoinositide binding and shifts channel activation toward depolarized potentials.
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