Literature DB >> 30359599

The AMPA Receptor Code of Synaptic Plasticity.

Graham H Diering1, Richard L Huganir2.   

Abstract

Changes in the properties and postsynaptic abundance of AMPA-type glutamate receptors (AMPARs) are major mechanisms underlying various forms of synaptic plasticity, including long-term potentiation (LTP), long-term depression (LTD), and homeostatic scaling. The function and the trafficking of AMPARs to and from synapses is modulated by specific AMPAR GluA1-GluA4 subunits, subunit-specific protein interactors, auxiliary subunits, and posttranslational modifications. Layers of regulation are added to AMPAR tetramers through these different interactions and modifications, increasing the computational power of synapses. Here we review the reliance of synaptic plasticity on AMPAR variants and propose "the AMPAR code" as a conceptual framework. The AMPAR code suggests that AMPAR variants will be predictive of the types and extent of synaptic plasticity that can occur and that a hierarchy exists such that certain AMPARs will be disproportionally recruited to synapses during LTP/homeostatic scaling up, or removed during LTD/homeostatic scaling down.
Copyright © 2018 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  NMDA receptors; glutamate receptors; homeostatic plasticity; homeostatic scaling; learning; long-term depression; long-term potentiation; memory; synaptic plasticity

Mesh:

Substances:

Year:  2018        PMID: 30359599      PMCID: PMC6214363          DOI: 10.1016/j.neuron.2018.10.018

Source DB:  PubMed          Journal:  Neuron        ISSN: 0896-6273            Impact factor:   17.173


  155 in total

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6.  The Noonan syndrome-associated D61G variant of the protein tyrosine phosphatase SHP2 prevents synaptic down-scaling.

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7.  Preferential generation of Ca2+-permeable AMPA receptors by AKAP79-anchored protein kinase C proceeds via GluA1 subunit phosphorylation at Ser-831.

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8.  The auxiliary glutamate receptor subunit dSol-1 promotes presynaptic neurotransmitter release and homeostatic potentiation.

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9.  The amino-terminal domain of GluA1 mediates LTP maintenance via interaction with neuroplastin-65.

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