Key result
Mutagenesis of negatively charged residues close to the selectivity filter of Kir3.1/Kir3.4 reduced slow activation and Ba2+ block, indicating polyamine unbinding is the primary mechanism.
Population
Cardiac muscarinic K+ channel, Kir3.1/Kir3.4
Comparison
Site-directed mutagenesis of negatively charged… vs Wild-type channels
Design
Preclinical
Authors
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Hypothesis-generating for IKACh regulation; leaves open translation to human arrhythmias or therapies.
Slow activation of the cardiac muscarinic K+ channel is primarily driven by the unbinding of polyamines from negatively charged residues near the selectivity filter, rather than an intrinsic gating mechanism.
Lancaster et al. (2000) studied Cardiac muscarinic K+ channel function. Site-directed mutagenesis was evaluated on Slow activation and Ba2+ block. Mutagenesis of negatively charged residues close to the selectivity filter of Kir3.1/Kir3.4 reduced slow activation and Ba2+ block, indicating polyamine unbinding is the primary mechanism.
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