| Activity-dependent protein dynamics define interconnected cores of co-regulated postsynaptic proteins. | |
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MedLine Citation:
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PMID: 23035237 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. While 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 observe widespread changes in relative synaptic abundances encompassing essentially all proteins, supporting the view that molecular composition of the PSD is tightly regulated. In most cases, we observe 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 amount impacts on synaptic strength and size. Our data show that the unbiased investigation of activity-dependent signaling of the PSD proteome can offer valuable new information on synaptic plasticity. |
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Authors:
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Jonathan C Trinidad; Agnes Thalhammer; Alma L Burlingame; Ralf Schoepfer |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-10-3 |
Journal Detail:
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Title: Molecular & cellular proteomics : MCP Volume: - ISSN: 1535-9484 ISO Abbreviation: Mol. Cell Proteomics Publication Date: 2012 Oct |
Date Detail:
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Created Date: 2012-10-4 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101125647 Medline TA: Mol Cell Proteomics Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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University of California, United States; |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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