title: Alternative splicing of potassium channels: a dynamic switch of cellular excitability.
abstract: Alternative splicing of pre-messenger RNA and reversible protein phosphorylation are fundamental mechanisms for regulating protein structure and function. Recent studies of one class of potassium channel (BK(Ca)) reveal dynamic reciprocal interactions between pre-mRNA splicing and protein phosphorylation. Splicing is regulated by phosphorylation, and exon selection determines the sensitivity of the channel protein to regulation by protein phosphorylation. These studies reveal a powerful dynamic molecular switch to determine cellular excitability.
authors.affiliation: Membrane Biology Group, Section of Biomedical Science, University of Edinburgh Medical School, Hugh Robson Building, EH8 9XD, Edinburgh, UK. mike.shipston@ed.ac.uk
authors.forename: M J
authors.initials: MJ
authors.lastname: Shipston
mesh_terms: D017398:Alternative Splicing / Q000235:genetics*; D000818:Animals; D054734:Calcium-Calmodulin-Dependent Protein Kinase Type 4; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism; D002460:Cell Line; D005091:Exons / Q000235:genetics* / Q000502:physiology; D006801:Humans; D008958:Models, Molecular; D010766:Phosphorylation; D015221:Potassium Channels / Q000235:genetics* / Q000378:metabolism
chemical_list: D015221:Potassium Channels; C517683:CAMK4 protein, human; D054734:Calcium-Calmodulin-Dependent Protein Kinase Type 4; D017871:Calcium-Calmodulin-Dependent Protein Kinases