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Structure paper

TitleGluA4 AMPA receptor gating mechanisms and modulation by auxiliary proteins.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 12, Page 2416-2428, Year 2025
Publish dateSep 15, 2025
AuthorsCarlos Vega-Gutiérrez / Javier Picañol-Párraga / Irene Sánchez-Valls / Victoria Del Pilar Ribón-Fuster / David Soto / Beatriz Herguedas /
PubMed AbstractAMPA-type glutamate receptors, fundamental ion channels for fast excitatory neurotransmission and synaptic plasticity, contain a GluA tetrameric core surrounded by auxiliary proteins such as ...AMPA-type glutamate receptors, fundamental ion channels for fast excitatory neurotransmission and synaptic plasticity, contain a GluA tetrameric core surrounded by auxiliary proteins such as transmembrane AMPA receptor regulatory proteins (TARPs) or Cornichons. Their exact composition and stoichiometry govern functional properties, including kinetics, calcium permeability and trafficking. The GluA1-GluA3 subunits predominate in the adult forebrain and are well characterized. However, we lack structural information on full-length GluA4-containing AMPARs, a subtype that has specific roles in brain development and specific cell types in mammals. Here we present the cryo-electron microscopy structures of rat GluA4:TARP-γ2 trapped in active, resting and desensitized states, covering a full gating cycle. Additionally, we describe the structure of GluA4 alone, which displays a classical Y-shaped conformation. In resting conditions, GluA4:TARP-γ2 adopts two conformations, one resembling the desensitized states of other GluA subunits. Moreover, we identify a regulatory site for TARP-γ2 in the ligand-binding domain that modulates gating kinetics. Our findings uncover distinct features of GluA4, highlighting how subunit composition and auxiliary proteins shape receptor structure and dynamics, expanding glutamatergic signaling diversity.
External linksNat Struct Mol Biol / PubMed:40954371
MethodsEM (single particle)
Resolution2.61 - 3.8 Å
Structure data

52862

9igz

EMDB-52862, PDB-9igz:
GluA4 in complex with TARP-2, resting state, structure of N-terminal domain
Method: EM (single particle) / Resolution: 3.5 Å

53031

9qdn

EMDB-53031, PDB-9qdn:
GluA4 in complex with TARP-2, resting state I, structure of TMD/LBD
Method: EM (single particle) / Resolution: 2.71 Å

53285

9qpw

EMDB-53285, PDB-9qpw:
GluA4, resting state, structure of TMD/LBD
Method: EM (single particle) / Resolution: 3.8 Å

54065

9rms

EMDB-54065, PDB-9rms:
GluA4 in complex with TARP-2, Resting II state, structure of TMD/LBD domains
Method: EM (single particle) / Resolution: 3.8 Å

54069

9rmw

EMDB-54069, PDB-9rmw:
GluA4 in complex with TARP-2, open state, structure of TMD/LBD domains
Method: EM (single particle) / Resolution: 2.9 Å

54080

9rn4

EMDB-54080, PDB-9rn4:
GluA4 in complex with TARP-2, desensitized state, structure of TMD/LBD domains
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-54081: GluA4 in complex with TARP-2, open state, map of LBD domain
Method: EM (single particle) / Resolution: 3.2 Å

54083

9rn7

EMDB-54083, PDB-9rn7:
GluA4 in complex with TARP-2, Desensitized state, structure of TMD domain
Method: EM (single particle) / Resolution: 3.1 Å

54092

9rnh

EMDB-54092, PDB-9rnh:
GluA4 in complex with TARP-2, Resting II state, structure of TMD domain
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-54217: GluA4 in complex with TARP-2, open state, map of TMD domain
Method: EM (single particle) / Resolution: 2.79 Å

EMDB-54225: GluA4 in complex with TARP-2, Resting I state, map of TMD domain
Method: EM (single particle) / Resolution: 2.61 Å

EMDB-54237: GluA4 in complex with TARP-2, Resting I state, map of LBD domain
Method: EM (single particle) / Resolution: 2.95 Å

EMDB-54250: GluA4, Resting state, map of LBD domain
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-PLM:
PALMITIC ACID

ChemComp-OLC:
(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate

ChemComp-E2Q:
6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide

ChemComp-HOH:
WATER

ChemComp-CYZ:
CYCLOTHIAZIDE

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-CA:
Unknown entry

Source
  • Rattus novergicus (Norway rat)
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / Gria4 / Voltage-dependent calcium channel gamma-2 / AMPA Receptor / GluA4-TARP2 / Resting state / NTD / Calcium Voltage-Gated Channel Auxiliary Subunit Gamma 2 / GluA4_TARP-2 / NBQX / GluA4 / TMD/LBD / Resting state II / Desensitized state / TMD

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