Molecular constituents and phosphorylation-dependent regulation of the post-synaptic density

Mass Spectrom Rev. Jul-Aug 2002;21(4):266-86. doi: 10.1002/mas.10033.

Abstract

The post-synaptic density (PSD) contains receptors with associated signaling- and scaffolding-proteins that organize signal-transduction pathways near the post-synaptic membrane. The PSD plays an important role in synaptic plasticity, and protein phosphorylation is critical to the regulation of PSD function, including learning and memory. Recently, studies have investigated the protein constituents of the PSD and substrate proteins for various protein kinases by proteomic analysis. The present review focuses on the molecular properties of PSD proteins, and substrates of protein kinases and their regulation by phosphorylation in order to understand the role of PSD in synaptic plasticity.

Publication types

  • Review

MeSH terms

  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism
  • Humans
  • Long-Term Potentiation
  • MAP Kinase Signaling System / physiology*
  • Nerve Tissue Proteins / classification
  • Nerve Tissue Proteins / metabolism*
  • Phosphorylation
  • Proteomics
  • Synapses / metabolism*

Substances

  • Nerve Tissue Proteins
  • postsynaptic density proteins
  • Calcium-Calmodulin-Dependent Protein Kinases