Document Detail

Activity-dependent protein dynamics define interconnected cores of co-regulated postsynaptic proteins.
MedLine Citation:
PMID:  23035237     Owner:  NLM     Status:  MEDLINE    
Synapses are highly dynamic structures that mediate cell-cell communication in the central nervous system. Their molecular composition is altered in an activity-dependent fashion, which modulates the efficacy of subsequent synaptic transmission events. Whereas activity-dependent trafficking of individual key synaptic proteins into and out of the synapse has been characterized previously, global activity-dependent changes in the synaptic proteome have not been studied. To test the feasibility of carrying out an unbiased large-scale approach, we investigated alterations in the molecular composition of synaptic spines following mass stimulation of the central nervous system induced by pilocarpine. We observed widespread changes in relative synaptic abundances encompassing essentially all proteins, supporting the view that the molecular composition of the postsynaptic density is tightly regulated. In most cases, we observed that members of gene families displayed coordinate regulation even when they were not known to physically interact. Analysis of correlated synaptic localization revealed a tightly co-regulated cluster of proteins, consisting of mainly glutamate receptors and their adaptors. This cluster constitutes a functional core of the postsynaptic machinery, and changes in its size affect synaptic strength and synaptic size. Our data show that the unbiased investigation of activity-dependent signaling of the postsynaptic density proteome can offer valuable new information on synaptic plasticity.
Jonathan C Trinidad; Agnes Thalhammer; Alma L Burlingame; Ralf Schoepfer
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-10-03
Journal Detail:
Title:  Molecular & cellular proteomics : MCP     Volume:  12     ISSN:  1535-9484     ISO Abbreviation:  Mol. Cell Proteomics     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2012-12-31     Completed Date:  2013-06-24     Revised Date:  2014-03-31    
Medline Journal Info:
Nlm Unique ID:  101125647     Medline TA:  Mol Cell Proteomics     Country:  United States    
Other Details:
Languages:  eng     Pagination:  29-41     Citation Subset:  IM    
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MeSH Terms
Cell Communication
Cell Membrane / metabolism
Central Nervous System / metabolism*
Guanylate Kinase / metabolism
Membrane Proteins / metabolism
Mice, Inbred C57BL
Neuronal Plasticity / physiology
Neurons / metabolism*
Pilocarpine / pharmacology
Post-Synaptic Density / metabolism*
Protein Transport
Receptors, Glutamate / metabolism
Signal Transduction
Synapses / physiology*
Synaptic Transmission*
Grant Support
8P41GM103481/GM/NIGMS NIH HHS; P41 GM103481/GM/NIGMS NIH HHS; P50 GM081879/GM/NIGMS NIH HHS; //Biotechnology and Biological Sciences Research Council; //Wellcome Trust
Reg. No./Substance:
0/Membrane Proteins; 0/Receptors, Glutamate; 01MI4Q9DI3/Pilocarpine; EC protein, mouse; EC Kinase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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