Evidence map›Paper›PMID 35705039›Full record

ArticleCell reports2022

Time-resolved proximity labeling of protein networks associated with ligand-activated EGFR.

Mireia Perez Verdaguer, Tian Zhang, Sachin Surve, Joao A Paulo, Callen Wallace, Simon C Watkins, Steven P Gygi, Alexander Sorkin

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Subcellular Cartography of the Phosphoinositide Multiverse.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2026
    Review
  6. Article
  7. Beyond the membrane: rethinking EGFR signaling in physiology and cancer.Cellular and molecular life sciences : CMLS · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

8 authors at 2 institutions in 1 country.

Mireia Perez VerdaguerDepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Tian ZhangDepartment of Cell Biology, Harvard University Medical School, Boston, MA, USA.
Sachin SurveDepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Joao A PauloDepartment of Cell Biology, Harvard University Medical School, Boston, MA, USA.
Callen WallaceDepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Simon C WatkinsDepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Steven P GygiDepartment of Cell Biology, Harvard University Medical School, Boston, MA, USA. Electronic address: steven_gygi@hms.harvard.edu.
Alexander SorkinDepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA. Electronic address: sorkin@pitt.edu.
University of Pittsburgh · USHarvard University · US

Funding

PATHOGENESIS OF CANCER--ROLE OF EGF RECEPTOR ENDOCYTOSISR01CA089151 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SORKIN, ALEXANDER D · 2001 to 2023
$6.9M
Signaling by the EGF Receptor from EndosomesR01GM124186 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SORKIN, ALEXANDER D · 2017 to 2021
$1.6M
NCI NIH HHS R01 CA089151NIGMS NIH HHS R01 GM124186
6 · The paper itself

Abstract

Ligand binding to the EGF receptor (EGFR) triggers multiple signal-transduction processes and promotes endocytosis of the receptor. The mechanisms of EGFR endocytosis and its cross-talk with signaling are poorly understood. Here, we combine peroxidase-catalyzed proximity labeling, isobaric peptide tagging, and quantitative mass spectrometry to define the dynamics of the proximity proteome of ligand-activated EGFR. Using this approach, we identify a network of signaling proteins, which remain associated with the receptor during its internalization and trafficking through the endosomal system. We show that Trk-fused gene (TFG), a protein known to function at the endoplasmic reticulum exit sites, is enriched in the proximity proteome of EGFR in early/sorting endosomes and localized in these endosomes and demonstrate that TFG regulates endosomal sorting of EGFR. This study provides a comprehensive resource of time-dependent nanoscale environment of EGFR, thus opening avenues to discovering new regulatory mechanisms of signaling and intracellular trafficking of receptor tyrosine kinases.

Indexed as

ErbB ReceptorsProteomeEndocytosisEndosomesEpidermal Growth FactorLigandsProtein TransportEpidermal Growth FactorErbB ReceptorsLigandsProteomeCP: Molecular biologyEGF receptorendocytosisproximity labelingsignaling

Identifiers

PMID35705039
PMCPMC9248364
OpenAlexW4282940173

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.