Evidence map›Paper›PMID 26575183›Full record

ArticlePloS one2015

Single Particle Tracking Reveals that EGFR Signaling Activity Is Amplified in Clathrin-Coated Pits.

Jenny Ibach, Yvonne Radon, Márton Gelléri, Michael H Sonntag, Luc Brunsveld, Philippe I H Bastiaens, Peter J Verveer

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.1field-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

35 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Biased activation of the receptor tyrosine kinase HER2.Cellular and molecular life sciences : CMLS · 2023
    Article
  8. Article
  9. Article
  10. Choosing the Probe for Single-Molecule Fluorescence Microscopy.International journal of molecular sciences · 2022
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Tyrosine Kinase Receptors in Oncology.International journal of molecular sciences · 2020
    Review
  17. Article
  18. PTEN: Bridging Endocytosis and Signaling.Cold Spring Harbor perspectives in medicine · 2020
    Review
  19. Article
  20. Components of the GTraffic (Copenhagen, Denmark) · 2020
    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

7 authors at 2 institutions in 2 countries.

Jenny IbachDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Yvonne RadonDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Márton GellériDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Michael H SonntagLaboratory of Chemical Biology, Department of Biomedical Engineering, and Institute of Complex Molecular Systems, Eindhoven University of Technology, Eindhoven, The Netherlands.
Luc BrunsveldLaboratory of Chemical Biology, Department of Biomedical Engineering, and Institute of Complex Molecular Systems, Eindhoven University of Technology, Eindhoven, The Netherlands.
Philippe I H BastiaensDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Peter J VerveerDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Max Planck Institute of Molecular Physiology · DEEindhoven University of Technology · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signaling from the epidermal growth factor receptor (EGFR) via phosphorylation on its C-terminal tyrosine residues requires self-association, which depends on the diffusional properties of the receptor and its density in the plasma membrane. Dimerization is a key event for EGFR activation, but the role of higher order clustering is unknown. We employed single particle tracking to relate the mobility and aggregation of EGFR to its signaling activity. EGFR mobility alternates between short-lived free, confined and immobile states. In the immobile state, EGFR tends to aggregate in clathrin-coated pits, which is further enhanced in a phosphorylation-dependent manner and does not require ligand binding. EGFR phosphorylation is further amplified by cross-phosphorylation in clathrin-coated pits. Because phosphorylated receptors can escape from the pits, local gradients of signaling active EGFR are formed. These results show that amplification of EGFR phosphorylation by receptor clustering in clathrin-coated pits supports signal activation at the plasma membrane.

Indexed as

ClathrinCluster AnalysisCoated Pits, Cell-MembraneErbB ReceptorsHumansLigandsMCF-7 CellsMicroscopy, ConfocalPhosphorylationSignal TransductionClathrinErbB ReceptorsLigands

Identifiers

PMID26575183
PMCPMC4648588
OpenAlexW2250126128

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.