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Keywords:

  • Ca2+/calmodulin-dependent protein kinase II (CaM KII);
  • post-synaptic density;
  • phosphorylation;
  • synaptic plasticity;
  • long-term potentiation;
  • glutamate receptor;
  • proteomics analysis

Abstract

Table 1. 
I.Introduction267
II.Isolation of the PSD267
III.Molecular Properties of PSD Constituents269
 A. Glutamate Receptors269
 B. CaM Kinase II and Protein Kinases269
 C. Scaffold and Receptor-Clustering Molecules272
 D. Association Proteins and Adaptor Proteins272
 E. Cytoskeletal Proteins273
 F. Enzymes273
 G. Proteins of Other Classes273
 H. Proteins of Other Fractions274
IV.Identification of PSD Proteins Based on Mass Spectrometry274
V.Substrates of Protein Kinases274
 A. CaM Kinase II Substrates274
 B. PKA and PKC Substrates275
 C. Substrates of MAP Kinase Cascade Kinases275
 D. Src Family Kinase Substrates276
VI.Regulation of PSD Proteins by Phosphorylation-Dephosphorylation276
 A. NMDA Receptor277
 B. AMPA and Kainate Receptors278
 C. Metabotropic Glutamate Receptors (mGluRs)279
 D. CaM Kinase II279
 E. K+-Channel Proteins280
 F. Scaffold- and Adaptor-Proteins280
 G. nNOS280
 H. Dynamin281
 I. Membrane Proteins281
VII.Perspectives281
VIII.Conclusions282
Abbreviations282
References282

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. © 2003 Wiley Periodicals, Inc., Mass Spec Rev 21:266–286, 2002; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/mas.10033