Evidence map›Paper›PMID 29523688›Full record

ArticleThe Journal of biological chemistry2018

Proteomics reveals novel protein associations with early endosomes in an epidermal growth factor-dependent manner.

Julie A Gosney, Daniel W Wilkey, Michael L Merchant, Brian P Ceresa

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Proteome-Wide Covalent Targeting of Acidic Residues with TunableJournal of the American Chemical Society · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Influenza A virus exploits transferrin receptor recycling to enter host cells.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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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 1 institution in 1 country.

Julie A GosneyFrom the Departments of Pharmacology and Toxicology and.
Daniel W WilkeyMedicine, University of Louisville, Louisville, Kentucky 40202.
Michael L MerchantMedicine, University of Louisville, Louisville, Kentucky 40202.
Brian P CeresaFrom the Departments of Pharmacology and Toxicology and brian.ceresa@louisville.edu.
University of Louisville · US

Funding

Role of oxidized linoleic acid metabolites in the pathogenesis of alcoholic liver diseaseP20GM113226 · NIGMS · UNIVERSITY OF LOUISVILLE · PI GHARE, SMITA S · 2016 to 2025
$24.1M
The Role of Nutrition in the Development/Progression of Alcohol-Induced Organ InjuryP50AA024337 · NIAAA · UNIVERSITY OF LOUISVILLE · PI SHIRISH S BARVE · 2016 to 2026
$17.9M
Identifying novel c-Cbl antagonists to promote corneal epithelial regenerationR21EY027032 · NEI · UNIVERSITY OF LOUISVILLE · PI CERESA, BRIAN P. · 2016 to 2017
$424k
NEI NIH HHS R21 EY027032NIAAA NIH HHS P50 AA024337NIGMS NIH HHS P20 GM113226
6 · The paper itself

Abstract

The epidermal growth factor receptor (EGFR) is a receptor tyrosine kinase that is an integral component of proliferative signaling. EGFRs on the cell surface become activated upon EGF binding and have an increased rate of endocytosis. Once in the cytoplasm, the EGF·EGFR complex is trafficked to the lysosome for degradation, and signaling is terminated. During trafficking, the EGFR kinase domain remains active, and the internalized EGFR can continue signaling to downstream effectors. Although effector activity varies based on the EGFR's endocytic location, it is not clear how this occurs. In an effort to identify proteins that uniquely associate with the internalized, liganded EGFR in the early endosome, we developed an early endosome isolation strategy to analyze their protein composition. Post-nuclear supernatant from HeLa cells stimulated with and without EGF were separated on an isotonic 17% Percoll gradient. The gradient was fractionated, and early endosomal fractions were pooled and immunoisolated with an EEA1 mAb. The isolated endosomes were validated by immunoblot using antibodies against organelle-specific marker proteins and transmission EM. These early endosomes were also subjected to LC-MS/MS for proteomic analysis. Five proteins were detected in endosomes in a ligand-dependent manner: EGFR, RUFY1, STOML2, PTPN23, and CCDC51. Knockdown of RUFY1 or PTPN23 by RNAi indicated that both proteins play a role in EGFR trafficking. These experiments indicate that endocytic trafficking of activated EGFR changes the protein composition, membrane trafficking, and signaling potential of the early endosome.

Indexed as

EndocytosisEndosomesEpidermal Growth FactorErbB ReceptorsHeLa CellsHumansProtein TransportProteomicsSignal TransductionEpidermal Growth FactorErbB Receptorsendosomeepidermal growth factor receptor (EGFR)membrane traffickingproteomicsreceptor endocytosis

Identifiers

PMID29523688
PMCPMC5912451
OpenAlexW2791521637

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.