Calcium channel regulation by calcineurin, a Ca2+-activated phosphatase in mammalian brain.
The enzymatic addition or removal of phosphate esters on serine and threonine hydroxyls alters the activity of many proteins that contribute to the characteristic structure and function of nerve cells. Recently, calcineurin, a major calmodulin-binding protein in mammalian brain, has been purified and identified as a Ca2+-activated protein phosphatase. Preliminary experiments suggest that calcineurin may limit Ca2+ influx through dihydropyridine-sensitive Ca2+ channels in the plasma membrane by dephosphorylating the channel, or a closely associated protein, and inactivating it.
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D000818:Animals; D001921:Brain / Q000187:drug effects / Q000201:enzymology / Q000502:physiology*; D019703:Calcineurin; D015220:Calcium Channels / Q000187:drug effects* / Q000502:physiology; D002148:Calmodulin-Binding Proteins / Q000494:pharmacology*; D008564:Membrane Potentials; D010749:Phosphoprotein Phosphatases / Q000494:pharmacology*; D010744:Phosphoric Monoester Hydrolases / Q000494:pharmacology*
D015220:Calcium Channels; D002148:Calmodulin-Binding Proteins; D019703:Calcineurin; D010749:Phosphoprotein Phosphatases; D010744:Phosphoric Monoester Hydrolases