Evidence map›Paper›PMID 31748519›Full record

ArticleNature communications2019

AMPA receptors in the synapse turnover by monomer diffusion.

Jyoji Morise, Kenichi G N Suzuki, Ayaka Kitagawa, Yoshihiko Wakazono, Kogo Takamiya, Taka A Tsunoyama, Yuri L Nemoto, Hiromu Takematsu, Akihiro Kusumi, Shogo Oka

Abstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

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  19. Phosphorylation-Dependent Regulation of CaFrontiers in synaptic neuroscience · 2020
    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

10 authors.

Jyoji MoriseDepartment of Biological Chemistry, Division of Human Health Sciences, Graduate School of Medicine, Kyoto University, Kyoto, 606-8507, Japan.
Kenichi G N SuzukiCenter for Highly Advanced Integration of Nano and Life Sciences (G-CHAIN), Gifu University, Gifu, 501-1193, Japan. kgsuzuki@gifu-u.ac.jp.
Ayaka KitagawaDepartment of Biological Chemistry, Division of Human Health Sciences, Graduate School of Medicine, Kyoto University, Kyoto, 606-8507, Japan.
Yoshihiko WakazonoDepartment of Integrative Physiology, Faculty of Medicine, University of Miyazaki, Miyazaki, 889-1692, Japan.
Kogo TakamiyaDepartment of Integrative Physiology, Faculty of Medicine, University of Miyazaki, Miyazaki, 889-1692, Japan.
Taka A TsunoyamaMembrane Cooperativity Unit, Okinawa Institute of Science and Technology Graduate University (OIST), Onna-son, Okinawa, 904-0495, Japan.ORCID http://orcid.org/0000-0003-1457-7612
Yuri L NemotoMembrane Cooperativity Unit, Okinawa Institute of Science and Technology Graduate University (OIST), Onna-son, Okinawa, 904-0495, Japan.
Hiromu TakematsuDepartment of Biological Chemistry, Division of Human Health Sciences, Graduate School of Medicine, Kyoto University, Kyoto, 606-8507, Japan.
Akihiro KusumiInstitute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Kyoto, 606-8507, Japan. akihiro.kusumi@oist.jp.
Shogo OkaDepartment of Biological Chemistry, Division of Human Health Sciences, Graduate School of Medicine, Kyoto University, Kyoto, 606-8507, Japan. shogo@hs.med.kyoto-u.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The number and subunit compositions of AMPA receptors (AMPARs), hetero- or homotetramers composed of four subunits GluA1-4, in the synapse is carefully tuned to sustain basic synaptic activity. This enables stimulation-induced synaptic plasticity, which is central to learning and memory. The AMPAR tetramers have been widely believed to be stable from their formation in the endoplasmic reticulum until their proteolytic decomposition. However, by observing GluA1 and GluA2 at the level of single molecules, we find that the homo- and heterotetramers are metastable, instantaneously falling apart into monomers, dimers, or trimers (in 100 and 200 ms, respectively), which readily form tetramers again. In the dendritic plasma membrane, GluA1 and GluA2 monomers and dimers are far more mobile than tetramers and enter and exit from the synaptic regions. We conclude that AMPAR turnover by lateral diffusion, essential for sustaining synaptic function, is largely done by monomers of AMPAR subunits, rather than preformed tetramers.

Indexed as

Neuronal PlasticityAnimalsCell MembraneCHO CellsCricetulusDendritesDiffusionHEK293 CellsHumansMiceMicroscopy, FluorescenceNeuronsPatch-Clamp TechniquesReceptors, AMPASingle Molecule ImagingSynapsesglutamate receptor ionotropic, AMPA 2Receptors, AMPA

Identifiers

PMID31748519
PMCPMC6868016

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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.