Protein kinase C in synaptic plasticity: changes in the in situ phosphorylation state of identified pre- and postsynaptic substrates

Prog Neuropsychopharmacol Biol Psychiatry. 1997 Apr;21(3):455-86. doi: 10.1016/s0278-5846(97)00013-4.

Abstract

1. Long-term potentiation and its counterpart long-term depression are two forms of activity dependent synaptic plasticity, in which protein kinases and protein phosphatases are essential. 2. B-50/GAP-43 and RC3/neurogranin are two defined neuronal PKC substrates with different synaptic localization. B-50/GAP-43 is a presynaptic protein and RC3/neurogranin is only found at the postsynaptic site. Measuring their phosphorylation state in hippocampal slices, allows us to simultaneously monitor changes in pre- and postsynaptic PKC mediated phosphorylation. 3. Induction of LTP in the CA1 field of the hippocampus is accompanied with an increase in the in situ phosphorylation of both B-50/GAP-43 and RC3/neurogranin, during narrow, partially overlapping, time windows. 4. Pharmacological data show that mGluR stimulation results in an increase in the in situ phosphorylation of B-50/GAP-43 and RC3/neurogranin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Hippocampus / physiology*
  • Long-Term Potentiation / physiology
  • Nerve Tissue Proteins / metabolism
  • Neuronal Plasticity / physiology*
  • Phosphoprotein Phosphatases / metabolism
  • Phosphorylation
  • Protein Kinase C / metabolism*
  • Protein Kinases / metabolism
  • Substrate Specificity
  • Synapses / physiology*

Substances

  • Nerve Tissue Proteins
  • Protein Kinases
  • Protein Kinase C
  • Phosphoprotein Phosphatases