Phosphorylation of calcineurin: effect on calmodulin binding |
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Authors: | M B Calalb R L Kincaid T R Soderling |
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Affiliation: | Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232. |
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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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