Volume 53, Issue s1 pp. 45-52
NORMAL AND ABERRANT STRUCTURE OF NEURONS AND GLIA

Neuronal excitability and calcium/calmodulin-dependent protein kinase type II: Location, location, location

Xiao-Bo Liu

Xiao-Bo Liu

Center for Neuroscience, University of California, Davis, Davis, California, U.S.A.

Departments of Cell Biology and Human Anatomy

Search for more papers by this author
Karl D. Murray

Karl D. Murray

Center for Neuroscience, University of California, Davis, Davis, California, U.S.A.

Psychiatry and Behavioral Science, University of California, Davis, Davis, California, U.S.A.

Search for more papers by this author
First published: 21 May 2012
Citations: 104
Address correspondence to Karl D. Murray, Center for Neuroscience, UC Davis, Davis, CA 95618, U.S.A. E-mail: [email protected]

Summary

Calcium/calmodulin-dependent protein kinase type II (CaMKII) is a highly abundant serine/threonine kinase comprising a significant fraction of total protein in mammalian forebrain and forming a major component of the postsynaptic density. CaMKII is essential for certain forms of synaptic plasticity and memory consolidation and this is mediated through substrate binding and intramolecular phosphorylation of holoenzyme subunits. CaMKII is multifunctional; it targets a variety of cellular substrates, and this diversity depends on holoenzyme subunit composition. CaMKII comprises homooligomeric and heterooligomeric complexes generated from four subunits (α, β, δ, and γ) encoded by separate genes that are further expanded by extensive alternative splicing to more than 30 different isoforms. Much attention has been paid to understanding the regulation of CaMKII function through its structural diversity and/or substrate specificity. However, given the importance of subunit composition to holoenzyme activity, it is likely that specificity of cellular expression of CaMKII isoforms also plays a major role in regulation of enzyme function. Herein we review the cellular colocalization of CaMKII isoforms with special regard to the cell-type specificity of isoform expression in brain. In addition, we highlight the remarkable specificity of subcellular localization by the CaMKIIα isoform. In addition, we discuss the role that this cellular specificity of expression might play in propagating the type of recurrent neuronal activity associated with disorders such as temporal lobe epilepsy.

The full text of this article hosted at iucr.org is unavailable due to technical difficulties.

click me