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J. Biol. Chem., Vol. 261, Issue 26, 12134-12140, Sep, 1986
KP Huang, KF Chan, TJ Singh, H Nakabayashi and FL Huang
Ca2+-activated and phospholipid-dependent protein kinase (protein kinase C)
isolated from rat brain cytosol undergoes autophosphorylation in the
presence of Mg2+, ATP, Ca2+, phosphatidylserine, and diolein. Approximately
2-2.5 mol of phosphate were incorporated per mol of the kinase. After
sodium dodecyl sulfate-polyacrylamide gel electrophoresis and
autoradiography, the phosphorylated kinase showed a single protein band of
Mr = 82,000 compared to the Mr = 80,000 of the nonphosphorylated enzyme.
Analysis of the 32P-labeled tryptic peptides derived from the
autophosphorylated kinase by peptide mapping revealed that multiple sites
were phosphorylated. Both serine and threonine residues were found to be
labeled with 32P. Limited proteolysis of the autophosphorylated kinase with
trypsin resulted in the conversion of the kinase into a phospholipid- and
Ca2+-independent form. Two major 32P-labeled fragments, Mr = 48,000 and
38,000, were formed as a result of proteolysis, suggesting that the
catalytic domain and possibly the Ca2+- and phospholipid-binding region
were both phosphorylated. Protein kinase C autophosphorylation has a Km for
ATP (1.5 microM) about 10- fold lower than that for phosphorylation of
exogenous substrates. The kinetically preferred autophosphorylation appears
to be an intramolecular reaction. The autophosphorylated protein kinase C,
unlike the protease-degraded enzyme, still depends on Ca2+ and phospholipid
for maximal activity. However, the autophosphorylated form of the kinase
has a lower Ka for Ca2+ and a higher affinity for the binding of
[3H]phorbol-12, 13-dibutyrate. These findings suggest that
autophosphorylation of protein kinase C may be important in the regulation
of the enzymic activity subsequent to signal transduction.
Autophosphorylation of rat brain Ca2+-activated and phospholipid- dependent protein kinase
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