Key result
KCNQ1-MinK complexes undergo clathrin- and dynamin 2-dependent internalization, decreasing cell-surface channels relative to homomeric KCNQ1 and redefining MinK as an endocytic chaperone.
MinK acts as an endocytic chaperone for KCNQ1, providing a dynamic mechanism for controlling net surface Kv channel subunit composition, current density, and gating kinetics.
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May influence IKs density and repolarization; extends trafficking models but leaves open in vivo arrhythmia relevance.
Xu et al. (2009) studied Cardiac ventricular repolarization. MinK co-expression vs. Homomeric KCNQ1 channels was evaluated on Channel internalization and gating kinetics. KCNQ1-MinK complexes undergo clathrin- and dynamin 2-dependent internalization, decreasing cell-surface channels relative to homomeric KCNQ1 and redefining MinK as an endocytic chaperone.
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