Abstract

We previously demonstrated that the expression of voltage-gated potassium channel Kv1.5 is regulated by Protein Kinase C (PKC)-activation mediated endocytic degradation involving Thr15 in the N terminus of the channel. In the present study, using mutagenesis, patch clamp, Western blot and immunocytochemical techniques, we further examined the molecular mechanisms of PKC activation-mediated degradation of Kv1.5 channels. As Kv1.4 expression is unaffected by PKC-activation, we swapped the N-termini between Kv1.5 and Kv1.4.

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