RGD Reference Report - Proteomics analysis of rat brain postsynaptic density. Implications of the diverse protein functional groups for the integration of synaptic physiology. - Rat Genome Database

Send us a Message



Submit Data |  Help |  Video Tutorials |  News |  Publications |  Download |  REST API |  Citing RGD |  Contact   

Proteomics analysis of rat brain postsynaptic density. Implications of the diverse protein functional groups for the integration of synaptic physiology.

Authors: Li, Ka Wan  Hornshaw, Martin P  Van Der Schors, Roel C  Watson, Rod  Tate, Stephen  Casetta, Bruno  Jimenez, Connie R  Gouwenberg, Yvonne  Gundelfinger, Eckart D  Smalla, Karl-Heinz  Smit, August B 
Citation: Li KW, etal., J Biol Chem. 2004 Jan 9;279(2):987-1002. doi: 10.1074/jbc.M303116200. Epub 2003 Oct 7.
RGD ID: 13702402
Pubmed: PMID:14532281   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M303116200   (Journal Full-text)

The postsynaptic density contains multiple protein complexes that together relay the presynaptic neurotransmitter input to the activation of the postsynaptic neuron. In the present study we took two independent proteome approaches for the characterization of the protein complement of the postsynaptic density, namely 1) two-dimensional gel electrophoresis separation of proteins in conjunction with mass spectrometry to identify the tryptic peptides of the protein spots and 2) isolation of the trypsin-digested sample that was labeled with isotope-coded affinity tag, followed by liquid chromatography-tandem mass spectrometry for the partial separation and identification of the peptides, respectively. Functional grouping of the identified proteins indicates that the postsynaptic density is a structurally and functionally complex organelle that may be involved in a broad range of synaptic activities. These proteins include the receptors and ion channels for glutamate neurotransmission, proteins for maintenance and modulation of synaptic architecture, sorting and trafficking of membrane proteins, generation of anaerobic energy, scaffolding and signaling, local protein synthesis, and correct protein folding and breakdown of synaptic proteins. Together, these results imply that the postsynaptic density may have the ability to function (semi-) autonomously and may direct various cellular functions in order to integrate synaptic physiology.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Rplp0Rattranslation at postsynapse involved_inNAS PMID:14532281SynGO 
Rplp0Rattranslation at presynapse involved_inNAS PMID:14532281SynGO 

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Rplp0Ratpostsynapse is_active_inNAS PMID:14532281SynGO 
Hnrnph1Ratpostsynaptic density is_active_inEXP PMID:14532281SynGO 
Hnrnph1Ratpostsynaptic density is_active_inIDA PMID:14532281SynGO 
Hnrnph2Ratpostsynaptic density is_active_inEXP PMID:14532281SynGO 
Hnrnph2Ratpostsynaptic density is_active_inIDA PMID:14532281SynGO 
Pcbp1Ratpostsynaptic density is_active_inEXP PMID:14532281SynGO 
Pcbp1Ratpostsynaptic density is_active_inIDA PMID:14532281SynGO 
PuraRatpostsynaptic density is_active_inEXP PMID:14532281SynGO 
PuraRatpostsynaptic density is_active_inIDA PMID:14532281SynGO 
Rplp0Ratpresynapse is_active_inNAS PMID:14532281SynGO 
Rplp0Ratribosome is_active_inNAS PMID:14532281SynGO 
Eif5aRatsynapse is_active_inEXP PMID:14532281SynGO 
Eif5aRatsynapse is_active_inIDA PMID:14532281SynGO 
Rplp0Ratsynapse is_active_inEXP PMID:14532281SynGO 
Rplp0Ratsynapse is_active_inIDA PMID:14532281SynGO 
TufmRatsynapse is_active_inEXP PMID:14532281SynGO 
TufmRatsynapse is_active_inIDA PMID:14532281SynGO 

Objects Annotated

Genes (Rattus norvegicus)
Eif5a  (eukaryotic translation initiation factor 5A)
Hnrnph1  (heterogeneous nuclear ribonucleoprotein H1)
Hnrnph2  (heterogeneous nuclear ribonucleoprotein H2)
Pcbp1  (poly(rC) binding protein 1)
Pura  (purine rich element binding protein A)
Rplp0  (ribosomal protein lateral stalk subunit P0)
Tufm  (Tu translation elongation factor, mitochondrial)

Objects referenced in this article
Gene AC099137.1 null Rattus norvegicus

Additional Information