PMID: 19912759Oct 1, 1990Paper

Proteolytic activation of calcium/calmodulin-dependent protein kinase II: Putative function in synaptic plasticity

Molecular and Cellular Neurosciences
D P RichT R Soderling

Abstract

Rat forebrain Ca(2+)/calmodulin-dependent protein kinase II (CaM-kinase II) in isolated postsynaptic densities (PSD) was subjected to limited proteolysis with chymotrypsin or mu-calpain, a Ca(2+)-dependent protease. Incubation of the kinase with either protease resulted in a three- to fivefold enhancement of total kinase activity and solubilization of Ca(2+)/calmodulin (CaM)-independent activity from the PSD. Maximal enhancement of CaM-kinase II activity was observed when autophosphorylated or Ca(2+)/CaM-bound forms of the enzyme were proteolyzed. Analysis of the proteolytic products by Western blotting with a polyclonal antibody raised against soluble CaM-kinase II indicated that both proteases generated several immunoreactive fragments between 21 and 32 kDa. However, unlike chymotrypsin, mu-calpain degraded only a small fraction of the intact kinase subunits. (125)I-labeled CaM overlays indicated a major CaM-binding fragment of approximately 23 kDa in mu-calpain digests of purified cytosolic CaM-kinase II. This fragment was also shown to contain the regulatory autophosphorylation site (Thr-286(alpha)/287(beta)) of the kinase. Immunoblotting with antibody to the catalytic domain of the kinase indicated that there was a single ...Continue Reading

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Citations

Nov 1, 1993·Molecular and Cellular Biochemistry·T R Soderling
Jun 1, 1994·The International Journal of Biochemistry·T Suzuki
Dec 1, 1992·Neurochemistry International·R J Colbran
Apr 1, 1996·Neurochemistry International·K FukunagaE Miyamoto
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