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Structure paper

TitleProton-triggered rearrangement of the AMPA receptor N-terminal domains impacts receptor kinetics and synaptic localization.
Journal, issue, pagesNat Struct Mol Biol, Vol. 31, Issue 10, Page 1601-1613, Year 2024
Publish dateAug 13, 2024
AuthorsJosip Ivica / Nejc Kejzar / Hinze Ho / Imogen Stockwell / Viktor Kuchtiak / Alexander M Scrutton / Terunaga Nakagawa / Ingo H Greger /
PubMed AbstractAMPA glutamate receptors (AMPARs) are ion channel tetramers that mediate the majority of fast excitatory synaptic transmission. They are composed of four subunits (GluA1-GluA4); the GluA2 subunit ...AMPA glutamate receptors (AMPARs) are ion channel tetramers that mediate the majority of fast excitatory synaptic transmission. They are composed of four subunits (GluA1-GluA4); the GluA2 subunit dominates AMPAR function throughout the forebrain. Its extracellular N-terminal domain (NTD) determines receptor localization at the synapse, ensuring reliable synaptic transmission and plasticity. This synaptic anchoring function requires a compact NTD tier, stabilized by a GluA2-specific NTD interface. Here we show that low pH conditions, which accompany synaptic activity, rupture this interface. All-atom molecular dynamics simulations reveal that protonation of an interfacial histidine residue (H208) centrally contributes to NTD rearrangement. Moreover, in stark contrast to their canonical compact arrangement at neutral pH, GluA2 cryo-electron microscopy structures exhibit a wide spectrum of NTD conformations under acidic conditions. We show that the consequences of this pH-dependent conformational control are twofold: rupture of the NTD tier slows recovery from desensitized states and increases receptor mobility at mouse hippocampal synapses. Therefore, a proton-triggered NTD switch will shape both AMPAR location and kinetics, thereby impacting synaptic signal transmission.
External linksNat Struct Mol Biol / PubMed:39138332 / PubMed Central
MethodsEM (single particle)
Resolution2.57 - 3.69 Å
Structure data

44232

9b5z

EMDB-44232, PDB-9b5z:
GluA2 flip Q in complex with TARPgamma2 at pH8, consensus structure of LBD-TMD-TARPgamma2
Method: EM (single particle) / Resolution: 2.71 Å

44233

9b60

EMDB-44233, PDB-9b60:
GluA2 flip Q in complex with TARPgamma2 at pH8, consensus structure of TMD-TARPgamma2
Method: EM (single particle) / Resolution: 2.57 Å

44234

9b61

EMDB-44234, PDB-9b61:
GluA2 flip Q in complex with TARPgamma2 at pH5, consensus structure of LBD-TMD-TARPgamma2
Method: EM (single particle) / Resolution: 2.81 Å

44244

9b63

EMDB-44244, PDB-9b63:
GluA2 flip Q in complex with TARPgamma2 at pH5, consensus structure of TMD-TARPgamma2
Method: EM (single particle) / Resolution: 2.76 Å

44245

9b64

EMDB-44245, PDB-9b64:
GluA2 flip Q in complex with TARPgamma2 at pH5, class23, structure of LBD-TMD-TARPgamma2
Method: EM (single particle) / Resolution: 3.56 Å

44248

9b67

EMDB-44248, PDB-9b67:
GluA2 flip Q in complex with TARPgamma2 at pH8, class1, structure of LBD-TMD-TARPgamma2
Method: EM (single particle) / Resolution: 3.39 Å

44249

9b68

EMDB-44249, PDB-9b68:
GluA2 flip Q in complex with TARPgamma2 at pH8, class1, structure of NTD
Method: EM (single particle) / Resolution: 3.6 Å

44250

9b69

EMDB-44250, PDB-9b69:
GluA2 flip Q in complex with TARPgamma2 at pH8, class12, structure of NTD
Method: EM (single particle) / Resolution: 3.69 Å

44251

9b6a

EMDB-44251, PDB-9b6a:
GluA2 flip Q in complex with TARPgamma2 at pH8, class12, structure of LBD-TMD-TARPgamma2
Method: EM (single particle) / Resolution: 3.35 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • mus musculus (house mouse)
  • rattus norvegicus (Norway rat)
KeywordsTRANSPORT PROTEIN / AMPA receptor / ionotropic glutamate receptor / ion channel / auxiliary subunit

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