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Journal ArticleDOI

Biology of AMPA receptor interacting proteins - From biogenesis to synaptic plasticity.

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TLDR
An overview of the catalogue of AMPAR interacting proteins and how they contribute to the complex biology of this central glutamate receptor can be found in this article, where an array of transmembrane proteins operate as auxiliary subunits that in addition to receptor trafficking and stabilization also substantially impact AMPAR gating and pharmacology.
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This article is published in Neuropharmacology.The article was published on 2021-07-13. It has received 11 citations till now. The article focuses on the topics: Ionotropic glutamate receptor & AMPA receptor.

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Journal ArticleDOI

Mechanisms underlying TARP modulation of the GluA1/2-γ8 AMPA receptor

TL;DR: In this paper , electron cryo-microscopy structures of the GluA1/2 TARP-γ8 complex, in both open and desensitized states (at 3.5 Å), reveal state-selective engagement of the LBDs by the large TARPγ8 loop ('β1'), elucidating how this TARP stabilizes specific gating states.
Journal ArticleDOI

Mechanisms underlying TARP modulation of the GluA1/2-γ8 AMPA receptor

TL;DR: In this paper , electron cryo-microscopy structures of the GluA1/2 TARP-γ8 complex, in both open and desensitized states (at 3.5 Å), reveal state-selective engagement of the LBDs by the large TARPγ8 loop ('β1'), elucidating how this TARP stabilizes specific gating states.
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Influence of the TARP γ8-Selective Negative Allosteric Modulator JNJ-55511118 on AMPA Receptor Gating and Channel Conductance

TL;DR: In this paper , a patch-clamp electrophysiological recording from heterologously expressed AMPARs was used to characterize the actions of the γ8-selective AMPAR inhibitor JNJ-55511118 on GluA2(Q) receptors expressed in HEK cells.
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Diversity of AMPA Receptor Ligands: Chemotypes, Binding Modes, Mechanisms of Action, and Therapeutic Effects

TL;DR: A review of AMPA receptor ligands can be found in this paper , where the structural diversity of new chemotypes of agonists, competitive AMPA receptors, positive and negative allosteric modulators, transmembrane AMPA regulatory protein (TARP) dependent allosterics, ion channel blockers as well as their binding sites are discussed.
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The many faces of the AMPA-type ionotropic glutamate receptor

Derek Bowie
- 01 Jan 2022 - 
TL;DR: For instance, the authors provides a series of issues dedicated to each member of the Glutamate receptor superfamily that includes both ionotropic and metabotropic classes, including NMDA, AMPA-and kainate-selective iGluRs.
References
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Journal ArticleDOI

Subunit‐selective N‐terminal domain associations organize the formation of AMPA receptor heteromers

TL;DR: It is shown that the extracellular, membrane‐distal AMPAR N‐terminal domains (NTDs) orchestrate selective routes of heteromeric assembly via a surprisingly wide spectrum of subunit‐specific association affinities, which explains why heteromers predominate and how GluA2‐lacking, Ca2+‐permeable homomers could form.
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Cornichons Modify Channel Properties of Recombinant and Glial AMPA Receptors

TL;DR: Together, these experiments support the view that CNIHs are capable of altering key properties of AMPARs and suggest that they may do so in glia and help clarify the role of glial cells in this regulation of transmembrane proteins.
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Phase Separation-Mediated TARP/MAGUK Complex Condensation and AMPA Receptor Synaptic Transmission

TL;DR: Charge neutralization mutations in TARP_CT Arg-rich motif weakened TARP's condensation with PSD-95 and impaired TARP-mediated AMPAR synaptic transmission in mice hippocampal neurons, which may have implications for understanding clustering of other synaptic transmembrane proteins.
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Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum

TL;DR: It is shown that a single alternatively spliced residue within the ligand‐binding domain alters AMPAR secretion from the ER, and implication that gating transitions in the ER determine iGluR secretory traffic.
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Structural Bases of Desensitization in AMPA Receptor-Auxiliary Subunit Complexes

TL;DR: Cryo-EM structures of an AMPAR in complex with the auxiliary subunit GSG1L in the closed and desensitized states are reported and suggest that AMPAR auxiliary subunits share a modular architecture and use a common transmembrane scaffold for differentially regulate AMPAR gating.
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