Long-term potentiation and synaptic protein phosphorylation

Behav Brain Res. 1995 Jan 23;66(1-2):53-9. doi: 10.1016/0166-4328(94)00124-x.

Abstract

Long-term potentiation (LTP) is a well known experimental model for studying the activity-dependent enhancement of synaptic plasticity, and because of its long duration and its associative properties, it has been proposed as a system to investigate the molecular mechanisms of memory formation. At present, there are several lines of evidence that indicate that pre- and postsynaptic kinases and their specific substrates are involved in molecular mechanisms underlying LTP. Many studies focus on the involvement of protein kinase C (PKC). One way to investigate the role of PKC in long-term potentiation is to determine the degree of phosphorylation of its substrates after in situ phosphorylation in hippocampal slices. Two possible targets are the presynaptic membrane-associated protein B-50 (a.k.a. GAP 43, neuromodulin and F1), which has been implicated in different forms of synaptical plasticity in the brain such as neurite outgrowth, hippocampal LTP and neurotransmitter release, and the postsynaptic protein neurogranin (a.k.a. RC3, BICKS and p17) which function remains to be determined. This review will focus on the protein kinase C activity in pre- and postsynaptic compartment during the early phase of LTP and the possible involvement of its substrates B-50 and neurogranin.

Publication types

  • Review

MeSH terms

  • Animals
  • Calcium Channels / physiology
  • Calmodulin-Binding Proteins / metabolism
  • Culture Techniques
  • GAP-43 Protein
  • Hippocampus / physiology*
  • Long-Term Potentiation / physiology*
  • Membrane Glycoproteins / metabolism
  • Memory / physiology*
  • Nerve Tissue Proteins / metabolism*
  • Neurogranin
  • Phosphoproteins / metabolism*
  • Protein Kinase C / physiology*
  • Synapses / physiology*

Substances

  • Calcium Channels
  • Calmodulin-Binding Proteins
  • GAP-43 Protein
  • Membrane Glycoproteins
  • Nerve Tissue Proteins
  • Phosphoproteins
  • Neurogranin
  • Protein Kinase C