Phosphorylation of a constitutive serine inhibits BK channel variants containing the alternate exon "SRKR".

ABSTRACT: BK Ca(2+)-activated K(+) currents exhibit diverse properties across tissues. The functional variation in voltage- and Ca(2+)-dependent gating underlying this diversity arises from multiple mechanisms, including alternate splicing of Kcnma1, the gene encoding the pore-forming (α) subunit of the BK channel, phosphorylation of α subunits, and inclusion of β subunits in channel complexes. To address the interplay of these mechanisms in the regulation of BK currents, two native splice variants, BK0 and BKSRKR, were cloned from a tissue that exhibits dynamic daily expression of BK channel, the central circadian pacemaker in the suprachiasmatic nucleus (SCN) of mouse hypothalamus. The BK0 and BKSRKR variants differed by the inclusion of a four-amino acid alternate exon at splice site 1 (SRKR), wh

SUBMITTER: Shelley C 

PROVIDER: S-EPMC3840924 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature