Evidence map›Paper›PMID 41379938›Full record

ArticleScience (New York, N.Y.)2026

Structure and organization of AMPA receptor-TARP complexes in the mammalian cerebellum.

Alexander M Scrutton, Nayanika Sengupta, Josip Ivica, Imogen Stockwell, Sew Peak-Chew, Bishal Singh, Kunimichi Suzuki, Veronica T Chang, Stephen H McLaughlin, James M Krieger and 2 more

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Functional CaScientific reports · 2026
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Alexander M Scrutton *Neurobiology Division, Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0001-6974-2609
Nayanika Sengupta *Neurobiology Division, Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0003-3120-1393
Josip Ivica *Neurobiology Division, Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0001-7943-604X
Imogen StockwellNeurobiology Division, Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-9712-1700
Sew Peak-ChewCell Biology Division, Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-7602-6384
Bishal SinghDepartment of Genomic Medicine; University of Texas MD Anderson Cancer Center Houston, TX, USA.ORCID 0000-0001-5760-6765
Kunimichi SuzukiDepartment of Physiology, Keio University School of Medicine, Tokyo 160-8582, Japan.ORCID 0000-0001-7699-2163
Veronica T ChangNeurobiology Division, Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0001-7047-9019
Stephen H McLaughlinPNAC Division, Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0001-9135-6253
James M KriegerNeurobiology Division, Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0001-6194-6244
A Radu AricescuNeurobiology Division, Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0003-3783-1388
Ingo H GregerNeurobiology Division, Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-7291-2581

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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 posttranscriptional modifications. Using mass spectrometry, cryo-electron microscopy, and electrophysiology, we characterize major cerebellar AMPARs in pigs: calcium-impermeable GluA2/A4 heteromers with four transmembrane AMPAR regulatory protein (TARP) subunits, mainly neuronal in origin, and BG-specific, calcium-permeable GluA1/A4 heteromers containing two type II TARPs. We also showed that GluA4 receptors frequently 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.

Indexed as

Calcium ChannelsCerebellumReceptors, AMPAAnimalsCryoelectron MicroscopyHEK293 CellsHumansNeuronsProtein DomainsProtein SubunitsSwineSynapsesSynaptic TransmissionCalcium Channelsglutamate receptor ionotropic, AMPA 2glutamate receptor ionotropic, AMPA 4Protein SubunitsReceptors, AMPA

Identifiers

PMID41379938
PMCPMC7619101

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.