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Calcium/Calmodulin-Dependent Protein Kinase II

Current topics in cellular regulationPublished 1 January 1990
Roger Colbran, Thomas R. Soderling
Citations184

TL;DR

Investigation of the physiological role of the kinase in brain and other tissues will be a particularly exciting area for future work, and the current knowledge of the in vitro properties and the availability of cDNA clones will hopefully expedite this research.

Abstract

There is a great deal known about the in vitro properties of CaM kinase II, both in terms of its substrate specificity and its regulation by calmodulin and autophosphorylation. Much of this characterization is based on experiments performed with the rat brain isozyme of CaM kinase II, although in the aspects examined to date isozymes of the kinase from other tissues appear to behave in a broadly similar manner in vitro. However, relatively little is known about the functions of the kinase in vivo. The proteins phosphorylated by the kinase (with the probable exception of synapsin I and tyrosine hydroxylase) and the role of kinase autophosphorylation in vivo remain largely unknown. Investigation of the physiological role of the kinase in brain and other tissues will be a particularly exciting area for future work. The current knowledge of the in vitro properties and the availability of cDNA clones will hopefully expedite this research.

Keywords

Materials ScienceBiochemistry, Genetics and Molecular Biology