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Phosphorylation of calcineurin: effect on calmodulin binding
Authors:M B Calalb  R L Kincaid  T R Soderling
Affiliation:Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232.
Abstract:The effect of phosphorylation of calcineurin on calmodulin (CaM) binding was examined using a synthetic peptide which contains the CaM-binding domain and the serine phosphorylation site. The peptide, corresponding to residues 391-414 of brain calcineurin A subunit, was rapidly phosphorylated by protein kinase C and Ca2+/CaM-dependent protein kinase II but not by cAMP-dependent protein kinase. Phosphorylation of peptide 391-414 did not significantly alter the binding of CaM when compared to the non-phosphorylated peptide.
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