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Structural and Functional Architecture of AMPA-Type Glutamate Receptors and Their Auxiliary Proteins

Greger, IH; Watson, JF; Cull-Candy, SG; (2017) Structural and Functional Architecture of AMPA-Type Glutamate Receptors and Their Auxiliary Proteins. Neuron , 94 (4) pp. 713-730. 10.1016/j.neuron.2017.04.009. Green open access

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Abstract

AMPA receptors (AMPARs) are tetrameric ion channels that together with other ionotropic glutamate receptors (iGluRs), the NMDA and kainate receptors, mediate a majority of excitatory neurotransmission in the central nervous system. Whereas NMDA receptors gate channels with slow kinetics, responsible primarily for generating long-term synaptic potentiation and depression, AMPARs are the main fast transduction elements at synapses and are critical for the expression of plasticity. The kinetic and conductance properties of AMPARs are laid down during their biogenesis and are regulated by post-transcriptional RNA editing, splice variation, post-translational modification, and subunit composition. Furthermore, AMPAR assembly, trafficking, and functional heterogeneity depends on a large repertoire of auxiliary subunits-a feature that is particularly striking for this type of iGluR. Here, we discuss how the subunit structure, stoichiometry, and auxiliary subunits generate a heterogeneous plethora of receptors, each tailored to fulfill a vital role in fast synaptic signaling and plasticity.

Type: Article
Title: Structural and Functional Architecture of AMPA-Type Glutamate Receptors and Their Auxiliary Proteins
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1016/j.neuron.2017.04.009
Publisher version: http://dx.doi.org/10.1016/j.neuron.2017.04.009
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
Keywords: AMPA receptor, AMPAR assembly, AMPAR gating, Cryo-EM, LTP, TARP, auxiliary subunit, excitatory synaptic transmission, glutamate receptor, plasticity
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Neuro, Physiology and Pharmacology
URI: http://discovery.ucl.ac.uk/id/eprint/1556906
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