Y. L. Fong

TL;DR: The chapter summarizes the present knowledge of CaM kinase II with the particular emphasis on the molecular mechanisms involved in the regulation of kinase activity, and reviews the literature concerning the putative physiological functions of the kinase.

TL;DR: Two peptide analogs of Ca2+/calmodulin-dependent protein kinase II were synthesized and used to probe interactions of the various regulatory domains of the kinase, showing nonlinear Michaelis-Menton kinetics, with maximal phosphorylation at 20 microM and decreased phosphorylated at higher concentrations.

TL;DR: The baculovirus system expressed large quantities ofMCaMKII-alpha with characteristics similar to the rat brain CaMKII, thus providing an expression system for the detailed biochemical analysis of MCaMK II-alpha.

TL;DR: The results indicate that Arg283 is a very important determinant for the regulatory autophosphorylation of Thr286 that generates the Ca2(+)-independent activity but is not essential for the other multiple autoph phosphorylations within Ca2+/calmodulin-dependent protein kinase II, and that Arg 283 is only one of several important residues for the inhibitory potency of the autoinhibitory domain.

TL;DR: These unique biochemical regulatory properties, coupled with an unusual high concentration in the postsynaptic density of excitatory synapses, makes CaM-kinase II an attractive candidate for involvement in synaptic plasticity.