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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2006-10-18
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pubmed:abstractText |
Trafficking of AMPA receptors (AMPA-Rs) to and from synapses controls the strength of excitatory synaptic transmission. However, proteins that cluster AMPA-Rs at synapses remain poorly understood. Here we show that PSD-95-like membrane-associated guanylate kinases (PSD-MAGUKs) mediate this synaptic targeting, and we uncover a remarkable functional redundancy within this protein family. By manipulating endogenous neuronal PSD-MAGUK levels, we find that both PSD-95 and PSD-93 independently mediate AMPA-R targeting at mature synapses. We also reveal unanticipated synapse heterogeneity as loss of either PSD-95 or PSD-93 silences largely nonoverlapping populations of excitatory synapses. In adult PSD-95 and PSD-93 double knockout animals, SAP-102 is upregulated and compensates for the loss of synaptic AMPA-Rs. At immature synapses, PSD-95 and PSD-93 play little role in synaptic AMPA-R clustering; instead, SAP-102 dominates. These studies establish a PSD-MAGUK-specific regulation of AMPA-R synaptic expression that establishes and maintains glutamatergic synaptic transmission in the mammalian central nervous system.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Dlgh3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Dlgh4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mpp2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, AMPA
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0896-6273
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
52
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
307-20
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:17046693-Animals,
pubmed-meshheading:17046693-COS Cells,
pubmed-meshheading:17046693-Cell Differentiation,
pubmed-meshheading:17046693-Cells, Cultured,
pubmed-meshheading:17046693-Cercopithecus aethiops,
pubmed-meshheading:17046693-Dendritic Spines,
pubmed-meshheading:17046693-Down-Regulation,
pubmed-meshheading:17046693-Glutamic Acid,
pubmed-meshheading:17046693-Guanylate Kinase,
pubmed-meshheading:17046693-Hippocampus,
pubmed-meshheading:17046693-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:17046693-Membrane Proteins,
pubmed-meshheading:17046693-Mice,
pubmed-meshheading:17046693-Mice, Knockout,
pubmed-meshheading:17046693-Neuropeptides,
pubmed-meshheading:17046693-Organ Culture Techniques,
pubmed-meshheading:17046693-Protein Transport,
pubmed-meshheading:17046693-Rats,
pubmed-meshheading:17046693-Receptor Aggregation,
pubmed-meshheading:17046693-Receptors, AMPA,
pubmed-meshheading:17046693-Synapses,
pubmed-meshheading:17046693-Synaptic Membranes,
pubmed-meshheading:17046693-Synaptic Transmission
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pubmed:year |
2006
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pubmed:articleTitle |
Synapse-specific and developmentally regulated targeting of AMPA receptors by a family of MAGUK scaffolding proteins.
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pubmed:affiliation |
Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, California 94143, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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