Key result
Mutation of Ser-95 to aspartic acid or treatment with calcineurin inhibitors blocked DREAM-mediated membrane expression of the Kv4.2 potassium channel without affecting channel tetramerization.
Population
In vitro models studying DREAM/KChIP3 and Kv4.2 potassium channels
Comparison
Mutation of Ser-95 to aspartic acid; treatment… vs Wild-type DREAM or untreated controls
Design
Preclinical
Authors
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Hypothesis-generating for DREAM-calcineurin regulation of Kv4.2 in animal models; leaves open any clinical relevance for arrhythmias or channelopathies.
Phosphorylation of DREAM by GRK2 at Ser-95 and its dephosphorylation by calcineurin are critical regulatory steps for the membrane trafficking of Kv4.2 potassium channels.
Ruiz‐Gómez et al. (2006) studied this question. Mutation of Ser-95 to aspartic acid / calcineurin inhibitors was evaluated on Membrane expression of Kv4.2 potassium channel. Mutation of Ser-95 to aspartic acid or treatment with calcineurin inhibitors blocked DREAM-mediated membrane expression of the Kv4.2 potassium channel without affecting channel tetramerization.
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