Differential modulation of SK channel subtypes by phosphorylation.

ABSTRACT: Small-conductance Ca²⁺-activated K⁺ (SK) channels are voltage-independent and are activated by Ca²⁺ binding to the calmodulin constitutively associated with the channels. Both the pore-forming subunits and the associated calmodulin are subject to phosphorylation. Here, we investigated the modulation of different SK channel subtypes by phosphorylation, using the cultured endothelial cells as a tool. We report that casein kinase 2 (CK2) negatively modulates the apparent Ca²⁺ sensitivity of SK1 and IK channel subtypes by more than 5-fold, whereas the apparent Ca²⁺ sensitivity of the SK3 and SK2 subtypes is only reduced by ∼2-fold, when heterologously expressed on the plasma membrane of cultured endothelial cells. The SK2 channel subtype e

SUBMITTER: Nam YW 

PROVIDER: S-EPMC8415101 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature