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Structure paper

TitleStructure and organization of AMPA receptor-TARP complexes in the mammalian cerebellum.
Journal, issue, pagesScience, Page eaeb3577, Year 2025
Publish dateDec 11, 2025
AuthorsAlexander M Scrutton / Nayanika Sengupta / Josip Ivica / Imogen Stockwell / Sew Peak-Chew / Bishal Singh / Kunimichi Suzuki / Veronica T Chang / Stephen H McLaughlin / James M Krieger / A Radu Aricescu / Ingo H Greger /
PubMed AbstractAMPA receptors (AMPARs) are multimodal transducers of glutamatergic signals throughout the brain. Their diversity is exemplified in the cerebellum; at afferent synapses, AMPARs mediate high-frequency ...AMPA receptors (AMPARs) are multimodal transducers of glutamatergic signals throughout the brain. Their diversity is exemplified in the cerebellum; at afferent synapses, AMPARs mediate high-frequency excitation, whereas in Bergmann glia (BG) they support calcium transients that modulate synaptic transmission. This spectrum arises from different combinations of core subunits (GluA1-4), auxiliary proteins, and post-transcriptional modifications. Here, using mass-spectrometry, cryo-EM, and electrophysiology, we characterize major cerebellar AMPARs in pig: calcium-impermeable GluA2/A4 heteromers with four TARP subunits, mainly neuronal in origin, and BG-specific calcium-permeable GluA1/A4 heteromers containing two Type-2 TARPs. We also showed that GluA4 receptors consistently exhibit compact N-terminal domains that promote their synaptic delivery. Our study defines the organizational principles of mammalian cerebellar AMPAR complexes and reveals how different receptor subtypes support cell-type specific functions.
External linksScience / PubMed:41379938
MethodsEM (single particle)
Resolution3.26 - 4.5 Å
Structure data

54543

9s3o

EMDB-54543, PDB-9s3o:
Cerebellar GluA2/4 NTD heterophilic tetramer interface (focused refinement)
Method: EM (single particle) / Resolution: 3.9 Å

54547

9s3q

EMDB-54547, PDB-9s3q:
Cerebellar GluA1/4 NTD tetramer (focused refinement)
Method: EM (single particle) / Resolution: 3.26 Å

54556

9s3z

EMDB-54556, PDB-9s3z:
Cerebellar GluA1/4 LBD tetramer (focused refinement)
Method: EM (single particle) / Resolution: 3.55 Å

54558

9s41

EMDB-54558, PDB-9s41:
Cerebellar GluA1/4 TMD with TARP gamma 7 (focused refinement)
Method: EM (single particle) / Resolution: 3.66 Å

EMDB-54559: Cerebellar GluAx/A4 TMD with four TARPs (focused refinement)
Method: EM (single particle) / Resolution: 3.57 Å

EMDB-55413: GluA4 N-terminal domain bound to nanobody NB74 (focused refinement)
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-55414: GluA4 LBD-TMD with TARP gamma 2 (focused refinement)
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-55418: GluA4 with TARP gamma2 (consensus refinement)
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-55419: Full-length GluA4 with TARP gamma 2 (composite map)
Method: EM (single particle) / Resolution: 4.5 Å

Chemicals

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

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

Source
  • sus scrofa (pig)
  • Rattus norvegicus (Norway rat)
KeywordsSIGNALING PROTEIN / AMPA ionotropic glutamate receptor

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