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Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry.

Authors: Peng, Junmin  Kim, Myung Jong  Cheng, Dongmei  Duong, Duc M  Gygi, Steven P  Sheng, Morgan 
Citation: Peng J, etal., J Biol Chem. 2004 May 14;279(20):21003-11. doi: 10.1074/jbc.M400103200. Epub 2004 Mar 12.
Pubmed: (View Article at PubMed) PMID:15020595
DOI: Full-text: DOI:10.1074/jbc.M400103200

The postsynaptic density (PSD) of central excitatory synapses plays a key role in postsynaptic signal transduction and contains a high concentration of glutamate receptors and associated scaffold and signaling proteins. We report here a comprehensive analysis of purified PSD fractions by liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS). We identified 374 different proteins that copurified with the PSD structure and discovered thirteen phosphorylated sites from eight proteins. These proteins were classified into numerous functional groups, implying that the signaling pathways in the PSD are complex and diverse. Furthermore, using quantitative mass spectrometry, we measured the molar concentration and relative stoichiometries of a number of glutamate receptor subunits and scaffold proteins in the postsynaptic density. Thus this proteomic study reveals crucial information about molecular abundance as well as molecular diversity in the PSD, and provides a basis for further studies on the molecular mechanisms of synaptic function and plasticity.

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RGD ID: 13702264
Created: 2018-07-18
Species: All species
Last Modified: 2018-07-18
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.