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Structure paper

TitleGlutamate gating of AMPA-subtype iGluRs at physiological temperatures.
Journal, issue, pagesNature, Vol. 641, Issue 8063, Page 788-796, Year 2025
Publish dateMar 26, 2025
AuthorsAnish Kumar Mondal / Elisa Carrillo / Vasanthi Jayaraman / Edward C Twomey /
PubMed AbstractIonotropic glutamate receptors (iGluRs) are tetrameric ligand-gated ion channels that mediate most excitatory neurotransmission. iGluRs are gated by glutamate, where on glutamate binding, they open ...Ionotropic glutamate receptors (iGluRs) are tetrameric ligand-gated ion channels that mediate most excitatory neurotransmission. iGluRs are gated by glutamate, where on glutamate binding, they open their ion channels to enable cation influx into postsynaptic neurons, initiating signal transduction. The structural mechanics of how glutamate gating occurs in full-length iGluRs is not well understood. Here, using the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid subtype iGluR (AMPAR), we identify the glutamate-gating mechanism. AMPAR activation by glutamate is augmented at physiological temperatures. By preparing AMPARs for cryogenic-electron microscopy at these temperatures, we captured the glutamate-gating mechanism. Activation by glutamate initiates ion channel opening that involves all ion channel helices hinging away from the pore axis in a motif that is conserved across all iGluRs. Desensitization occurs when the local dimer pairs decouple and enables closure of the ion channel below through restoring the channel hinges and refolding the channel gate. Our findings define how glutamate gates iGluRs, provide foundations for therapeutic design and demonstrate how physiological temperatures can alter iGluR function.
External linksNature / PubMed:40140570 / PubMed Central
MethodsEM (single particle)
Resolution3.46 - 4.78 Å
Structure data

46872

9dhp

EMDB-46872, PDB-9dhp:
Resting state 1 of the GluA2-gamma2 complex
Method: EM (single particle) / Resolution: 4.18 Å

46873

9dhq

EMDB-46873, PDB-9dhq:
Resting state 2 of the GluA2-gamma2 complex
Method: EM (single particle) / Resolution: 4.78 Å

46874

9dhr

EMDB-46874, PDB-9dhr:
Glutamate activated state of the GluA2-gamma2 complex
Method: EM (single particle) / Resolution: 3.54 Å

46875

9dhs

EMDB-46875, PDB-9dhs:
Desensitized state 1 of the GluA2-gamma2 complex
Method: EM (single particle) / Resolution: 4.48 Å

46876

9dht

EMDB-46876, PDB-9dht:
Desensitized state 2 of the GluA2-gamma2 complex
Method: EM (single particle) / Resolution: 4.31 Å

48557

9mrk

EMDB-48557, PDB-9mrk:
Glutamate activated state of the GluA2-gamma2 complex prepared at 37 degrees C
Method: EM (single particle) / Resolution: 3.62 Å

48558

9mrl

EMDB-48558, PDB-9mrl:
Desensitized state 1 of the GluA2-gamma2 complex prepared at 37 degrees C
Method: EM (single particle) / Resolution: 4.17 Å

48559

9mrm

EMDB-48559, PDB-9mrm:
Desensitized state 2 of the GluA2-gamma2 complex prepared at 37 degrees C
Method: EM (single particle) / Resolution: 4.52 Å

48560

9mrn

EMDB-48560, PDB-9mrn:
Consensus glutamate activated state of the GluA2-gamma2 complex
Method: EM (single particle) / Resolution: 3.46 Å

Chemicals

ChemComp-GLU:
GLUTAMIC ACID

Source
  • rattus norvegicus (Norway rat)
  • mus musculus (house mouse)
KeywordsTRANSPORT PROTEIN / ligand-gated ion channel / ionotropic glutamate receptor / ampa receptor / ion channel / ligand gated ion channel

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