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Papers In Press, published online ahead of print January 19, 2001
J. Biol. Chem, 10.1074/jbc.C000741200
Submitted on October 19, 2000
Revised on December 22, 2000
Accepted on January 19, 2001
Biomedical Science, University of Edinburgh, Edinburgh EH8 9AG
Corresponding Author: mike.shipston{at}ed.ac.uk
Alternative exon splicing and reversible protein phosphorylation of large conductance calcium-activated potassium (BK) channels represent fundamental control mechanisms for the regulation of cellular excitability. BK channels are encoded by a single gene that undergoes extensive, hormonally regulated exon splicing. In native tissues BK channels display considerable diversity and plasticity in their regulation by cAMP-dependent protein kinase (PKA). Differential regulation of alternatively spliced BK channels by PKA may provide a molecular basis for the diversity and plasticity of BK channel sensitivities to PKA. Here we demonstrate that PKA activates BK channels lacking splice inserts (ZERO) but inhibits channels expressing a 59 amino acid exon at splice site 2 (STREX-1). Channel activation is dependent upon a conserved C-terminal PKA consensus motif (S869) whereas, inhibition is mediated via a STREX-1 exon specific PKA consensus site. Thus, alternative splicing acts as a molecular switch to determine the sensitivity of potassium channels to protein phosphorylation.
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