June 1, 2001Journal of Biological ChemistryOpen Access

Coupling of Voltage-dependent Potassium Channel Inactivation and Oxidoreductase Active Site of Kvβ Subunits

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Structured PICO

Population

Xenopus oocytes expressing voltage-dependent potassium (Kv) channels and Kvbeta subunits

Intervention

Structure-based mutations in the oxidoreductase active site, substrate binding domain, or cofactor binding domain of Kvbeta subunits (Kvbeta1.1 and Kvbeta3.1)

Comparator

Wild-type Kvbeta subunits

Outcome

Kv channel inactivating activity (gating mode)surrogate

Kvbeta oxidoreductase activity couples voltage-dependent potassium channel inactivation to cellular redox regulation.

Discussion

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Implication

May link Kvbeta oxidoreductase activity to channel inactivation in animal models; leaves open therapeutic translation to human arrhythmias.

Cite This Study

Bähring et al. (2001) studied this question.

synapsesocial.com/papers/6a8d20960bd5a3045f314d20 https://doi.org/10.1074/jbc.m100483200

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Implication

May link Kvbeta oxidoreductase activity to channel inactivation in animal models; leaves open therapeutic translation to human arrhythmias.

Coupling of Voltage-dependent Potassium Channel Inactivation and Oxidoreductase Active Site of Kvβ Subunits

Structured PICO

Discussion

Implication

Cite This Study

Coupling of Voltage-dependent Potassium Channel Inactivation and Oxidoreductase Active Site of Kvβ Subunits

Structured PICO

Discussion

Implication

Cite This Study

Also Consider

Also Consider