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TitleGating and noelin clustering of native Ca-permeable AMPA receptors.
Journal, issue, pagesNature, Vol. 645, Issue 8080, Page 526-534, Year 2025
Publish dateJun 23, 2025
AuthorsChengli Fang / Cathy J Spangler / Jumi Park / Natalie Sheldon / Laurence O Trussell / Eric Gouaux /
PubMed AbstractAMPA-type ionotropic glutamate receptors (AMPARs) are integral to fast excitatory synaptic transmission and have vital roles in synaptic plasticity, motor coordination, learning and memory. Whereas ...AMPA-type ionotropic glutamate receptors (AMPARs) are integral to fast excitatory synaptic transmission and have vital roles in synaptic plasticity, motor coordination, learning and memory. Whereas extensive structural studies have been conducted on recombinant AMPARs and native calcium-impermeable (CI)-AMPARs alongside their auxiliary proteins, the molecular architecture of native calcium-permeable (CP)-AMPARs has remained undefined. Here, to determine the subunit composition, physiological architecture and gating mechanisms of CP-AMPARs, we visualize these receptors, immunoaffinity purified from rat cerebella, and resolve their structures using cryo-electron microscopy (cryo-EM). Our results indicate that the predominant assembly consists of GluA1 and GluA4 subunits, with the GluA4 subunit occupying the B and D positions, and auxiliary subunits, including transmembrane AMPAR regulatory proteins (TARPs) located at the B' and D' positions, and cornichon homologues (CNIHs) or TARPs located at the A' and C' positions. Furthermore, we resolved the structure of the noelin (NOE1)-GluA1-GluA4 complex, in which NOE1 specifically binds to the GluA4 subunit at the B and D positions. Notably, NOE1 stabilizes the amino-terminal domain layer without affecting gating properties of the receptor. NOE1 contributes to AMPAR function by forming dimeric AMPAR assemblies that are likely to engage in extracellular networks, clustering receptors in synaptic environments and modulating receptor responsiveness to synaptic inputs.
External linksNature / PubMed:40550474 / PubMed Central
MethodsEM (single particle)
Resolution3.26 - 9.34 Å
Structure data

EMDB-49711: Cryo-EM map of LBD-TMD combined from all cerebellar CP-AMPAR subtypes with 4 TARPs
Method: EM (single particle) / Resolution: 3.99 Å

EMDB-49712: Cryo-EM map of LBD-TMD combined from all cerebellar CP-AMPAR subtypes with 2 TARPs
Method: EM (single particle) / Resolution: 3.74 Å

EMDB-49713: Cryo-EM map of LBD-TMD combined from all cerebellar CP-AMPAR subtypes with 2 TARPs 2CNIHs
Method: EM (single particle) / Resolution: 4.03 Å

EMDB-49714: Cryo-EM map of Noelin 1 with cerebellar GluA1/A4
Method: EM (single particle) / Resolution: 3.33 Å

EMDB-49715: Cryo-EM map of cerebellar GluA1/A4 with ordered ATD
Method: EM (single particle) / Resolution: 4.29 Å

EMDB-49716: Cryo-EM map of cerebellar GluA1/A4 with disordered ATD
Method: EM (single particle) / Resolution: 4.76 Å

EMDB-49717: Cryo-EM map of LBD-TMD in the active state combined from all cerebellar CP-AMPAR subtypes with 4 auxiliary proteins
Method: EM (single particle) / Resolution: 3.96 Å

EMDB-49718: Cryo-EM map of cerebellar GluA1/A4 LBD-TMD in desensitized state
Method: EM (single particle) / Resolution: 9.02 Å

EMDB-49719: Cryo-EM map of cerebellar GluA1/A4 LBD-TMD in Noelin-AMPAR complex in desensitized state
Method: EM (single particle) / Resolution: 9.34 Å

EMDB-49720: Cryo-EM map of recombinant GluA4 with ordered ATD
Method: EM (single particle) / Resolution: 8.02 Å

EMDB-49721: Cryo-EM map of recombinant GluA4 with disordered ATD
Method: EM (single particle) / Resolution: 4.61 Å

EMDB-49722: Cryo-EM map of recombinant GluA4 with Noelin 1
Method: EM (single particle) / Resolution: 7.44 Å

49723

9nr6

EMDB-49723: The structure of Noelin 1 with GluA1/A4-ATD
PDB-9nr6: The structure of Noelin 1 with cerebellar GluA1/A4-ATD
Method: EM (single particle) / Resolution: 3.26 Å

49724

9nr7

EMDB-49724, PDB-9nr7:
The structure of GluA1/A4 LBD-TMD in Noelin-AMPAR complex
Method: EM (single particle) / Resolution: 4.18 Å

49725

9nr8

EMDB-49725, PDB-9nr8:
The structure of cerebellar GluA1/A4 ATD
Method: EM (single particle) / Resolution: 3.53 Å

49726

9nr9

EMDB-49726, PDB-9nr9:
The structure of GluA1/A4 LBD-TMD with 2 TARPs
Method: EM (single particle) / Resolution: 4.22 Å

49727

9nra

EMDB-49727, PDB-9nra:
The structure of GluA1/A4 LBD-TMD with 4 auxiliary subunits
Method: EM (single particle) / Resolution: 4.18 Å

Chemicals

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

ChemComp-CA:
Unknown entry

ChemComp-ZK1:
{[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid / antagonist, medication*YM

Source
  • rattus norvegicus (Norway rat)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / iGluR / CP-AMPA receptors / Noelin 1

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