Evidence map›Paper›PMID 26465157›Full record

ArticlePloS one2015

Inhibition of Receptor Dimerization as a Novel Negative Feedback Mechanism of EGFR Signaling.

Malgorzata Kluba, Yves Engelborghs, Johan Hofkens, Hideaki Mizuno

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 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Assessment of cAMP-PKA Signaling in Candida glabrata by FRET-Based Biosensors.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  5. Article
  6. Article
  7. The complexities of PKCα signaling in cancer.Advances in biological regulation · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Feedback Regulation of Syk by Protein Kinase C in Human Platelets.International journal of molecular sciences · 2019
    Article
  13. Review
  14. CyclicOncotarget · 2018
    Article
  15. 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 1 institution in 1 country.

Malgorzata KlubaLaboratory of Biomolecular Network Dynamics, Biochemistry, Molecular and Structural Biology Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200G box 2403, 3001, Heverlee, Belgium.
Yves EngelborghsLaboratory of Biomolecular Network Dynamics, Biochemistry, Molecular and Structural Biology Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200G box 2403, 3001, Heverlee, Belgium.
Johan HofkensMolecular Imaging and Photonics, Department of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001, Heverlee, Belgium.
Hideaki MizunoLaboratory of Biomolecular Network Dynamics, Biochemistry, Molecular and Structural Biology Section, Department of Chemistry, KU Leuven, Celestijnenlaan 200G box 2403, 3001, Heverlee, Belgium.
KU Leuven · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dimerization of the epidermal growth factor receptor (EGFR) is crucial for initiating signal transduction. We employed raster image correlation spectroscopy to continuously monitor the EGFR monomer-dimer equilibrium in living cells. EGFR dimer formation upon addition of EGF showed oscillatory behavior with a periodicity of about 2.5 min, suggesting the presence of a negative feedback loop to monomerize the receptor. We demonstrated that monomerization of EGFR relies on phospholipase Cγ, protein kinase C, and protein kinase D (PKD), while being independent of Ca2+ signaling and endocytosis. Phosphorylation of the juxtamembrane threonine residues of EGFR (T654/T669) by PKD was identified as the factor that shifts the monomer-dimer equilibrium of ligand bound EGFR towards the monomeric state. The dimerization state of the receptor correlated with the activity of an extracellular signal-regulated kinase, downstream of the EGFR. Based on these observations, we propose a novel, negative feedback mechanism that regulates EGFR signaling via receptor monomerization.

Indexed as

AnimalsCalcium SignalingCell MembraneCHO CellsCricetulusDimerizationEndocytosisEpidermal Growth FactorErbB ReceptorsExtracellular Signal-Regulated MAP KinasesLigandsPhosphorylationSignal TransductionEpidermal Growth FactorErbB ReceptorsExtracellular Signal-Regulated MAP KinasesLigands

Identifiers

PMID26465157
PMCPMC4605717
OpenAlexW2339981958

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.