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

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    10 Scopus citations

    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 (US)
    Pages (from-to)169-183
    Number of pages15
    JournalProgress in Brain Research
    Volume89
    Issue numberC
    DOIs
    StatePublished - Jan 1 1991

    ASJC Scopus subject areas

    • Neuroscience(all)

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    Soderling, T. R., Fukunaga, K., Brickey, D. A., Fong, Y. L., Rich, D. P., Smith, K., & Colbran, R. J. (1991). Chapter 12: Molecular and cellular studies on brain calcium/calmodulin-dependent protein kinase II. Progress in Brain Research, 89(C), 169-183. https://doi.org/10.1016/S0079-6123(08)61722-7