Reversible generation of a Ca2+-independent form of Ca2+(calmodulin)-dependent protein kinase II by an autophosphorylation mechanism

C. M. Schworer, R. J. Colbran, T. R. Soderling

    Research output: Contribution to journalArticlepeer-review

    187 Scopus citations


    The Ca2+(calmodulin (CaM))-dependent protein kinase II, purified from either rabbit liver or rat brain, was preincubated under conditions that are known to promote its autophosphorylation. When kinase activity was assayed after this preincubation, it was observed that excess EGTA could block no more than 40-60% of the total Ca2+- and CaM-dependent activity compared to 95% inhibition by EGTA prior to preincubation. In the EGTA assay, free Ca2+ was calculated to be <1 nM; therefore, this activity was designated Ca2+-independent activity. Formation of this Ca2+-independent form of the kinase was shown to be associated with autophosphorylation based on the following observations: (a) it required the presence of Ca2+, CaM, and ATP; (b) the ATP analogs adenylyl imidodiphosphate and adenylyl methylenediphosphate could not substitute for ATP; (c) generation of the independent form was associated with incorporation of phosphate into the kinase; and (d) addition of protein phosphatase partially dephosphorylated the kinase and restored its Ca2+ dependence. This phenomenon may be of physiological importance because it would prolong the effects of extracellular signals that only transiently increase the intracellular Ca2+ level.

    Original languageEnglish (US)
    Pages (from-to)8581-8584
    Number of pages4
    JournalJournal of Biological Chemistry
    Issue number19
    StatePublished - 1986

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology


    Dive into the research topics of 'Reversible generation of a Ca<sup>2+</sup>-independent form of Ca<sup>2+</sup>(calmodulin)-dependent protein kinase II by an autophosphorylation mechanism'. Together they form a unique fingerprint.

    Cite this