| First Author | Ramakers GM | Year | 1999 |
| Journal | J Biol Chem | Volume | 274 |
| Issue | 4 | Pages | 1873-4 |
| PubMed ID | 9890937 | Mgi Jnum | J:52934 |
| Mgi Id | MGI:1330676 | Doi | 10.1074/jbc.274.4.1873 |
| Citation | Ramakers GM, et al. (1999) Substrate phosphorylation in the protein kinase Cgamma knockout mouse. J Biol Chem 274(4):1873-4 |
| abstractText | The 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. |
