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pubmed-article:9890937pubmed:abstractTextThe phosphorylation state of three identified neural-specific protein kinase C substrates (RC3, GAP-43/B-50, and MARCKS) was monitored in hippocampal slices of mice lacking the gamma-subtype of protein kinase C and wild-type controls by quantitative immunoprecipitation following 32Pi labeling. Depolarization with potassium, activation of glutamate receptors with glutamate, or direct stimulation of protein kinase C with a phorbol ester increased RC3 phosphorylation in wild-type animals but failed to affect RC3 phosphorylation in mice lacking the gamma-subtype of protein kinase C. Our results suggests the following biochemical pathway: activation of a postsynaptic (metabotropic) glutamate receptor stimulates the gamma-subtype of protein kinase C, which in turn phosphorylates RC3. The inability to increase RC3 phosphorylation in mice lacking the gamma-subtype of protein kinase C by membrane depolarization or glutamate receptor activation may contribute to the spatial learning deficits and impaired hippocampal LTP observed in these mice.lld:pubmed
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pubmed-article:9890937pubmed:articleTitleSubstrate phosphorylation in the protein kinase Cgamma knockout mouse.lld:pubmed
pubmed-article:9890937pubmed:affiliationRudolf Magnus Institute for Neurosciences, Department of Medical Pharmacology, Unversiteitsweg 100, 3584 CG Utrecht, The Netherlands. geert.ramakers@basalmed.uio.nolld:pubmed
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