Evidence map›Paper›PMID 33627404›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

The amino-terminal domain of GluA1 mediates LTP maintenance via interaction with neuroplastin-65.

Chao-Hua Jiang, Mengping Wei, Chen Zhang, Yun Stone Shi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 57 citations in OpenAlex.

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  6. Neuroplastin-55 is a receptor of Manf and protects against diet-induced obesity by promoting adipose browning.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Dynamic extracellular interactions with AMPA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
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  11. Article
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  17. 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
  18. Tuning synaptic strength by regulation of AMPA glutamate receptor localization.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Review
  19. Progressive reduction of nuclear receptor Nr4a1 mediates age-dependent cognitive decline.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024
    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 3 institutions in 1 country.

Chao-Hua JiangState Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Affiliated Drum Tower Hospital of Nanjing University Medical School, Nanjing University, 210032 Nanjing, China.ORCID 0000-0001-5675-8441
Mengping WeiSchool of Basic Medical Sciences, Beijing Key Laboratory of Neural Regeneration and Repair, Advanced Innovation Center for Human Brain Protection, Capital Medical University, Beijing 100069, China.ORCID 0000-0003-1169-5824
Chen ZhangSchool of Basic Medical Sciences, Beijing Key Laboratory of Neural Regeneration and Repair, Advanced Innovation Center for Human Brain Protection, Capital Medical University, Beijing 100069, China; yunshi@nju.edu.cn czhang@ccmu.edu.cn.ORCID 0000-0002-7940-8054
Yun Stone ShiState Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Affiliated Drum Tower Hospital of Nanjing University Medical School, Nanjing University, 210032 Nanjing, China; yunshi@nju.edu.cn czhang@ccmu.edu.cn.ORCID 0000-0002-8842-9818
Capital Medical University · CNNanjing Brain Hospital · CNNanjing Drum Tower Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Long-term potentiation (LTP) has long been considered as an important cellular mechanism for learning and memory. LTP expression involves NMDA receptor-dependent synaptic insertion of AMPA receptors (AMPARs). However, how AMPARs are recruited and anchored at the postsynaptic membrane during LTP remains largely unknown. In this study, using CRISPR/Cas9 to delete the endogenous AMPARs and replace them with the mutant forms in single neurons, we have found that the amino-terminal domain (ATD) of GluA1 is required for LTP maintenance. Moreover, we show that GluA1 ATD directly interacts with the cell adhesion molecule neuroplastin-65 (Np65). Neurons lacking Np65 exhibit severely impaired LTP maintenance, and Np65 deletion prevents GluA1 from rescuing LTP in AMPARs-deleted neurons. Thus, our study reveals an essential role for GluA1/Np65 binding in anchoring AMPARs at the postsynaptic membrane during LTP.

Indexed as

AnimalsEmbryo, MammalianExcitatory Postsynaptic PotentialsFemaleGene Expression RegulationGenes, ReporterGreen Fluorescent ProteinsHEK293 CellsHippocampusHumansLong-Term PotentiationLuminescent ProteinsMaleMembrane GlycoproteinsMicePrimary Cell CultureGreen Fluorescent ProteinsLuminescent ProteinsMembrane Glycoproteinsneuroplastin protein, mouseReceptors, AMPARed Fluorescent Proteinamino-terminal domainAMPA receptorsGluA1LTPneuroplastin

Identifiers

PMID33627404
PMCPMC7936340
OpenAlexW3130616985

What OpenQuestion holds

Textmetadata
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.