Evidence map›Paper›PMID 28303090›Full record

ArticleFrontiers in molecular neuroscience2017

The Inhibitory Effect of α/β-Hydrolase Domain-Containing 6 (ABHD6) on the Surface Targeting of GluA2- and GluA3-Containing AMPA Receptors.

Mengping Wei, Moye Jia, Jian Zhang, Lulu Yu, Yunzhi Zhao, Yingqi Chen, Yimeng Ma, Wei Zhang, Yun S Shi, Chen Zhang

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular neuroscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 31% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Efficient and rapid isolation of native AMPA receptor complexes for cryo-EM.Protein science : a publication of the Protein Society · 2026
    Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. ABHD6: Its Place in Endocannabinoid Signaling and Beyond.Trends in pharmacological sciences · 2019
    Review
  11. Review
  12. Identification of Protein Tyrosine Phosphatase Receptor Type O (PTPRO) as a Synaptic Adhesion Molecule that Promotes Synapse Formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  13. 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 at 4 institutions in 1 country.

Mengping WeiState Key Laboratory of Membrane Biology, School of Life Sciences, Peking UniversityBeijing, China; PKU-IDG (International Digital Group)/McGovern Institute for Brain Research, Peking UniversityBeijing, China.
Moye JiaState Key Laboratory of Membrane Biology, School of Life Sciences, Peking UniversityBeijing, China; PKU-IDG (International Digital Group)/McGovern Institute for Brain Research, Peking UniversityBeijing, China.
Jian ZhangState Key Laboratory of Membrane Biology, School of Life Sciences, Peking UniversityBeijing, China; PKU-IDG (International Digital Group)/McGovern Institute for Brain Research, Peking UniversityBeijing, China.
Lulu YuState Key Laboratory of Membrane Biology, School of Life Sciences, Peking UniversityBeijing, China; PKU-IDG (International Digital Group)/McGovern Institute for Brain Research, Peking UniversityBeijing, China.
Yunzhi ZhaoState Key Laboratory of Membrane Biology, School of Life Sciences, Peking UniversityBeijing, China; PKU-IDG (International Digital Group)/McGovern Institute for Brain Research, Peking UniversityBeijing, China.
Yingqi ChenState Key Laboratory of Membrane Biology, School of Life Sciences, Peking UniversityBeijing, China; PKU-IDG (International Digital Group)/McGovern Institute for Brain Research, Peking UniversityBeijing, China.
Yimeng MaState Key Laboratory of Membrane Biology, School of Life Sciences, Peking UniversityBeijing, China; PKU-IDG (International Digital Group)/McGovern Institute for Brain Research, Peking UniversityBeijing, China.
Wei ZhangDepartment of Pharmacology, Institute of Chinese Integrative Medicine, Hebei Medical University Shijiazhuang, China.
Yun S ShiMinistry of Education (MOE) Key Laboratory of Model Animal for Disease Study, Model Animal Research Center of Nanjing University Nanjing, China.
Chen ZhangState Key Laboratory of Membrane Biology, School of Life Sciences, Peking UniversityBeijing, China; PKU-IDG (International Digital Group)/McGovern Institute for Brain Research, Peking UniversityBeijing, China.
Chinese Institute for Brain Research · CNPeking University · CNHebei Medical University · CNNanjing University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPARs) are major excitatory receptors that mediate fast neurotransmission in the mammalian brain. The surface expression of functional AMPARs is crucial for synaptic transmission and plasticity. AMPAR auxiliary subunits control the biosynthesis, membrane trafficking, and synaptic targeting of AMPARs. Our previous report showed that α/β-hydrolase domain-containing 6 (ABHD6), an auxiliary subunit for AMPARs, suppresses the membrane delivery and function of GluA1-containing receptors in both heterologous cells and neurons. However, it remained unclear whether ABHD6 affects the membrane trafficking of glutamate receptor subunits, GluA2 and GluA3. Here, we examine the effects of ABHD6 overexpression in HEK293T cells expressing GluA1, GluA2, GluA3, and stargazin, either alone or in combination. The results show that ABHD6 suppresses the glutamate-induced currents and the membrane expression of AMPARs when expressing GluA2 or GluA3 in the HEK293T cells. We generated a series of GluA2 and GluA3 C-terminal deletion constructs and confirm that the C-terminus of GluAs is required for ABHD6's inhibitory effects on glutamate-induced currents and surface expression of GluAs. Meanwhile, our pull-down experiments reveal that ABHD6 binds to GluA1-3, and deletion of the C-terminal domain of GluAs abolishes this binding. These findings demonstrate that ABHD6 inhibits the AMPAR-mediated currents and its surface expression, independent of the type of AMPAR subunits, and this inhibitor's effects are mediated through the binding with the GluAs C-terminal regions.

Indexed as

ABHD6AMPA receptorglutamatesprotein–protein interactionsreceptor trafficking

Identifiers

PMID28303090
PMCPMC5333494
OpenAlexW2599434887

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.