Calcium/calmodulin-dependent protein kinase II.
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.
Colbran
R J
RJ
Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232.
Soderling
T R
TR
D000595:Amino Acid Sequence; D000818:Animals; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D016384:Consensus Sequence; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism; D008969:Molecular Sequence Data; D009928:Organ Specificity; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity; D013569:Synapses / Q000201:enzymology
D007527:Isoenzymes; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases