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J. Biol. Chem., Vol. 264, Issue 9, 4800-4804, 03, 1989
RJ Colbran, MK Smith, CM Schworer, YL Fong and TR Soderling
Regulatory mechanisms of rat brain Ca2+/calmodulin-dependent protein kinase
II (CaM-kinase II) were probed using a synthetic peptide (CaMK- (281-309]
corresponding to residues 281-309 (alpha-subunit) which contained the
calmodulin (CaM)-binding and inhibitory domains and also the initial
autophosphorylation site (Thr286). Kinetic analyses indicated that
inhibition of a completely Ca2+/CaM-independent form of CaM-kinase II by
CaMK-(281-309) was noncompetitive with respect to peptide substrate
(syntide-2) but was competitive with respect to ATP. Interaction of
CaMK-(281-309) with the ATP-binding site was independently confirmed since
inactivation of proteolyzed CaM-kinase II by phenylglyoxal (t1/2 = 7 min)
was blocked by ATP analog plus Mg2+ or by CaMK-(281-309). In the presence
of Ca2+/CaM, CaMK-(281-309) no longer protected against phenylglyoxal
inactivation, consistent with our previous observations (Colbran, R.J.,
Fong, Y.-L., Schworer, C.M., and Soderling, T.R. (1988) J. Biol. Chem. 263,
18145-18151) that binding of Ca2+/CaM to CaMK-(281-309) 1) blocks its
inhibitory property, and 2) enhances its phosphorylation at Thr 286. The
present study also showed that phosphorylation of CaMK-(281-309) decreased
its inhibitory potency at least 10-fold without affecting its Ca2+/CaM-
binding ability. Thus, CaM-kinase II is inactive in the absence of Ca2+/CaM
because an inhibitory domain within residues 281-309 interacts with the
catalytic domain and blocks ATP binding. Autophosphorylation of Thr286
results in a Ca2+/CaM-independent form of the kinase by disrupting the
inhibitory interaction with the catalytic domain.
Regulatory domain of calcium/calmodulin-dependent protein kinase II. Mechanism of inhibition and regulation by phosphorylation
Howard Hughes Medical Institute, Nashville, Tennessee 37232.
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