Chapter 12: Molecular and cellular studies on brain calcium/calmodulin-dependent protein kinase II

T. R. Soderling, K. Fukunaga, D. A. Brickey, Y. L. Fong, D. P. Rich, K. Smith, R. J. Colbran

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

This chapter discusses brain CaM-kinase II with a particular focus on its unique regulatory properties, its regulation in cultured brain cells, and its physiological functions. CaM-kinase II has widespread tissue distribution as oligomeric isozyme forms and is particularly abundant in the brain. In certain regions of the brain, such as hippocampus, it constitutes up to 2% of total protein, which probably makes it the most abundant enzyme in these tissues. CaM-kinase II is localized presynaptically where it is involved in Ca2+-dependent regulation of neurotransmitter biosynthesis and exocytosis. At excitatory synapses in forebrain, there is a thickening of the postsynaptic membrane called the postsynaptic density (PSD), and CaM-kinase II constitutes about 30–50% of the protein in the PSD. These excitatory synapses are subject to a usage-dependent enhancement of synaptic transmission called long-term potentiation (LTP)—a popular model for learning and memory.

Original languageEnglish
Pages (from-to)169-183
Number of pages15
JournalProgress in Brain Research
Volume89
Issue numberC
DOIs
Publication statusPublished - 1991 Jan 1
Externally publishedYes

ASJC Scopus subject areas

  • Neuroscience(all)

Fingerprint

Dive into the research topics of 'Chapter 12: Molecular and cellular studies on brain calcium/calmodulin-dependent protein kinase II'. Together they form a unique fingerprint.

Cite this