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Kv15-Kvbeta13 and PKC

, : Kv15-Kvbeta13 and PKC.

Kv1.5 channels are the primary channels contributing to the ultrarapid outward potassium current (IKur). The regulatory Kv?1.3 subunit converts Kv1.5 channels from delayed rectifiers with a modest degree of slow inactivation to channels with both fast and slow inactivation components. Previous studies have shown that inhibition of PKC with calphostin C abolishes the fast inactivation induced by Kv?1.3. In this study, we investigated the mechanisms underlying this phenomenon using electrophysiological, biochemical, and confocal microscopy approaches. To achieve this, we used HEK293 cells (which lack Kv? subunits) transiently cotransfected with Kv1.5+Kv?1.3 and also rat ventricular and atrial tissue to study native ?-? subunit interactions. Immunocytochemistry assays demonstrated that these channel subunits colocalize in control conditions and after calphostin C treatment. Moreover, coimmunoprecipitation studies showed that Kv1.5 and Kv?1.3 remain associated after PKC inhibition. After knocking down all PKC isoforms by siRNA or inhibiting PKC with calphostin C, Kv?1.3-induced fast inactivation at +6 mV was abolished. However, depolarization to +1 mV revealed Kv?1.3-induced inactivation, indicating that PKC inhibition causes a dramatic positive shift of the inactivation curve. Our results demonstrate that calphostin C-mediated abolishment of fast inactivation is not due to the dissociation of Kv1.5 and Kv?1.3. Finally, immunoprecipitation and immunocytochemistry experiments revealed an association between Kv1.5, Kv?1.3, the receptor for activated C kinase (RACK1), PKC?I, PKC?II, and PKC? in HEK293 cells. A very similar Kv1.5 channelosome was found in rat ventricular tissue but not in atrial tissue.


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