Evidence map›Paper›PMID 25023288›Full record

ArticleThe Journal of biological chemistry2014

Endocytic adaptor epidermal growth factor receptor substrate 15 (Eps15) is involved in the trafficking of ubiquitinated α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors.

Amy Lin, Heng-Ye Man

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. 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
1.2field-weighted citation impact, top 25% 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

19 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Selective endocytosis of CaScience advances · 2022
    Article
  3. Article
  4. The WD40-Repeat Protein WDR-20 and the Deubiquitinating Enzyme USP-46 Promote Cell Surface Levels of Glutamate Receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Mechanisms of AMPA Receptor Endosomal Sorting.Frontiers in molecular neuroscience · 2018
    Review
  11. Article
  12. Review
  13. Review
  14. Parkin Deficiency Reduces Hippocampal Glutamatergic Neurotransmission by Impairing AMPA Receptor Endocytosis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
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

2 authors at 1 institution in 1 country.

Amy LinFrom the Department of Biology, Boston University, Boston, Massachusetts 02215.
Heng-Ye ManFrom the Department of Biology, Boston University, Boston, Massachusetts 02215 hman@bu.edu.
Boston University · US

Funding

Molecular Mechanisms of Homeostatic Synaptic PlasticityR01MH079407 · NIMH · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MAN, HENGYE · 2008 to 2018
$3.9M
NIMH NIH HHS MH 079407NIMH NIH HHS R01 MH079407
6 · The paper itself

Abstract

AMPA-type glutamate receptors (AMPARs) play a critical role in mediating fast excitatory synaptic transmission in the brain. Alterations in receptor expression, distribution, and trafficking have been shown to underlie synaptic plasticity and higher brain functions, including learning and memory, as well as brain dysfunctions such as drug addiction and psychological disorders. Therefore, it is essential to elucidate the molecular mechanisms that regulate AMPAR dynamics. We have shown previously that mammalian AMPARs are subject to posttranslational modification by ubiquitin, with AMPAR ubiquitination enhancing receptor internalization and reducing AMPAR cell surface expression. Here we report a crucial role for epidermal growth factor receptor substrate 15 (Eps15), an endocytic adaptor, in ubiquitination-dependent AMPAR internalization. We find that suppression or overexpression of Eps15 results in changes in AMPAR surface expression. Eps15 interacts with AMPARs, which requires Nedd4-mediated GluA1 ubiquitination and the ubiquitin-interacting motif of Eps15. Importantly, we find that Eps15 plays an important role in AMPAR internalization. Knockdown of Eps15 suppresses the internalization of GluA1 but not the mutant GluA1 that lacks ubiquitination sites, indicating a role of Eps15 for the internalization of ubiquitinated AMPARs. These results reveal a novel molecular mechanism employed specifically for the trafficking of the ubiquitin-modified AMPARs.

Indexed as

EndocytosisAnimalsCalcium-Binding ProteinsCells, CulturedGene Knockdown TechniquesIntracellular Signaling Peptides and ProteinsProtein TransportRatsReceptors, AMPASynapsesUbiquitinationCalcium-Binding ProteinsEps15 protein, ratIntracellular Signaling Peptides and ProteinsReceptors, AMPAAdaptor ProteinEPS15Nedd4Receptor InternalizationTraffickingUbiquitylation (Ubiquitination)α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid Receptor (AMPA receptor, AMPAR)

Identifiers

PMID25023288
PMCPMC4148888
OpenAlexW2078650862

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.