Isoform diversity and modulation of sodium channels by protein kinases.
Although voltage-dependent sodium channels from the brain have been realized as targets for regulatory protein phosphorylation since the first isolation of sodium channels as proteins, the functional role of phosphoprotein formation has been obscured until recently. The review summarizes progress on the modulation of voltage-dependent sodium channels by serine/threonine protein kinases, i.e. PKA and PKC. Divergent modulation is discussed in context with divergent primary structure of the alpha-subunit.
Schreibmayer
W
W
Institute for Medical Physics and Biophysics, Graz, Austria. Wolfgang.Schreibmayer@kfunigraz.ac.at
D000818:Animals; D001921:Brain / Q000502:physiology; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D006321:Heart / Q000502:physiology*; D006801:Humans; D009474:Neurons / Q000502:physiology; D020033:Protein Isoforms / Q000235:genetics / Q000502:physiology; D011493:Protein Kinase C / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D015222:Sodium Channels / Q000235:genetics / Q000502:physiology*
D020033:Protein Isoforms; D015222:Sodium Channels; D011494:Protein Kinases; D017346:Protein Serine-Threonine Kinases; D017868:Cyclic AMP-Dependent Protein Kinases; D011493:Protein Kinase C