Evidence map›Paper›PMID 25650738›Full record

ArticleeLife2015

Regulation of EGFR signal transduction by analogue-to-digital conversion in endosomes.

Roberto Villaseñor, Hidenori Nonaka, Perla Del Conte-Zerial, Yannis Kalaidzidis, Marino Zerial

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
22.4field-weighted citation impact, top 1% 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

53 citing papers in PubMed, 110 citations in OpenAlex.

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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

5 authors at 2 institutions in 2 countries.

Roberto VillaseñorMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Hidenori NonakaMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Perla Del Conte-ZerialMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Yannis KalaidzidisMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Marino ZerialMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Max Planck Institute of Molecular Cell Biology and Genetics · DELomonosov Moscow State University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An outstanding question is how receptor tyrosine kinases (RTKs) determine different cell-fate decisions despite sharing the same signalling cascades. Here, we uncovered an unexpected mechanism of RTK trafficking in this process. By quantitative high-resolution FRET microscopy, we found that phosphorylated epidermal growth factor receptor (p-EGFR) is not randomly distributed but packaged at constant mean amounts in endosomes. Cells respond to higher EGF concentrations by increasing the number of endosomes but keeping the mean p-EGFR content per endosome almost constant. By mathematical modelling, we found that this mechanism confers both robustness and regulation to signalling output. Different growth factors caused specific changes in endosome number and size in various cell systems and changing the distribution of p-EGFR between endosomes was sufficient to reprogram cell-fate decision upon EGF stimulation. We propose that the packaging of p-RTKs in endosomes is a general mechanism to ensure the fidelity and specificity of the signalling response.

Indexed as

Signal TransductionEndosomesErbB ReceptorsHeLa CellsHumansMicroscopy, ConfocalProtein TransportErbB Receptorscell biologyendocytosishumanmembrane transportmouseratsignal transduction

Identifiers

PMID25650738
PMCPMC4384751
OpenAlexW2111309386

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.