Evidence map›Paper›PMID 34426577›Full record

ArticleNature communications2021

AMPA receptor anchoring at CA1 synapses is determined by N-terminal domain and TARP γ8 interactions.

Jake F Watson, Alexandra Pinggera, Hinze Ho, Ingo H Greger

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.9field-weighted citation impact, top 8% of its field
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

23 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Dynamic extracellular interactions with AMPA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. MINFLUX fluorescence nanoscopy in biological tissue.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. bioRxiv : the preprint server for biology · 2024
    Article
  8. Article
  9. Review
  10. Activity-dependent diffusion trapping of AMPA receptors as a key step for expression of early LTP.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  11. Tuning synaptic strength by regulation of AMPA glutamate receptor localization.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Review
  12. Synaptic memory and CaMKII.Physiological reviews · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Unraveling the mysteries of dendritic spine dynamics: Five key principles shaping memory and cognition.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 2 institutions in 2 countries.

Jake F Watson *Neurobiology Division, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom.ORCID 0000-0002-8698-3823
Alexandra Pinggera *Neurobiology Division, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom.ORCID 0000-0001-7120-6194
Hinze HoNeurobiology Division, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom.ORCID 0000-0003-1082-9851
Ingo H GregerNeurobiology Division, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom. ig@mrc-lmb.cam.ac.uk.ORCID 0000-0002-7291-2581
MRC Laboratory of Molecular Biology · GBInstitute of Science and Technology Austria · AT

Funding

Biotechnology and Biological Sciences Research Council BB/N002113/1Medical Research Council MC_U105174197
6 · The paper itself

Abstract

AMPA receptor (AMPAR) abundance and positioning at excitatory synapses regulates the strength of transmission. Changes in AMPAR localisation can enact synaptic plasticity, allowing long-term information storage, and is therefore tightly controlled. Multiple mechanisms regulating AMPAR synaptic anchoring have been described, but with limited coherence or comparison between reports, our understanding of this process is unclear. Here, combining synaptic recordings from mouse hippocampal slices and super-resolution imaging in dissociated cultures, we compare the contributions of three AMPAR interaction domains controlling transmission at hippocampal CA1 synapses. We show that the AMPAR C-termini play only a modulatory role, whereas the extracellular N-terminal domain (NTD) and PDZ interactions of the auxiliary subunit TARP γ8 are both crucial, and each is sufficient to maintain transmission. Our data support a model in which γ8 accumulates AMPARs at the postsynaptic density, where the NTD further tunes their positioning. This interplay between cytosolic (TARP γ8) and synaptic cleft (NTD) interactions provides versatility to regulate synaptic transmission and plasticity.

Indexed as

Amino Acid SequenceAnimalsCA1 Region, HippocampalFluorescent DyesImaging, Three-DimensionalMiceMice, Inbred C57BLModels, NeurologicalMutationNeuronal PlasticityNeuronsNuclear ProteinsProtein BindingProtein DomainsProtein MultimerizationReceptors, AMPAFluorescent DyesNuclear ProteinsReceptors, AMPATARP

Identifiers

PMID34426577
PMCPMC8382838
OpenAlexW3195715762

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.