Phosphorylation of calcineurin: Effect on calmodulin binding

Mihail B. Calalb, Randall L. Kincaid, Thomas R. Soderling

    Research output: Contribution to journalArticle

    10 Scopus citations

    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.

    Original languageEnglish (US)
    Pages (from-to)551-556
    Number of pages6
    JournalBiochemical and Biophysical Research Communications
    Volume172
    Issue number2
    DOIs
    StatePublished - Oct 30 1990

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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