Evidence map›Paper›PMID 11408594›Full record

ArticleMolecular biology of the cell2001

Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking.

P Burke, K Schooler, H S Wiley

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 155 papers.

0numbers the graph read from it
0cells of the map it votes in
155citing papers in PubMed
21.0field-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

155 citing papers in PubMed, 384 citations in OpenAlex.

  1. Review
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  5. Clustering of Membrane Receptors: Insights from DNA Origami-Based Approaches.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Review
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95 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

P BurkeDepartment of Pathology, Division of Cell Biology and Immunology, University of Utah, Salt Lake City, Utah 84132, USA.
K Schooler
H S Wiley
Pacific Northwest National Laboratory · USUniversity of Utah · US

Funding

USE OF GENETICALLY MODIFIED SKIN TO TREAT DISEASEP01HD028528 · NICHD · UNIVERSITY OF UTAH · PI KRUEGER, GERALD · 1992 to 2003
$4.6M
NICHD NIH HHS P01-HD28528
6 · The paper itself

Abstract

Ligand activation of the epidermal growth factor receptor (EGFR) leads to its rapid internalization and eventual delivery to lysosomes. This process is thought to be a mechanism to attenuate signaling, but signals could potentially be generated after endocytosis. To directly evaluate EGFR signaling during receptor trafficking, we developed a technique to rapidly and selectively isolate internalized EGFR and associated molecules with the use of reversibly biotinylated anti-EGFR antibodies. In addition, we developed antibodies specific to tyrosine-phosphorylated EGFR. With the use of a combination of fluorescence imaging and affinity precipitation approaches, we evaluated the state of EGFR activation and substrate association during trafficking in epithelial cells. We found that after internalization, EGFR remained active in the early endosomes. However, receptors were inactivated before degradation, apparently due to ligand removal from endosomes. Adapter molecules, such as Shc, were associated with EGFR both at the cell surface and within endosomes. Some molecules, such as Grb2, were primarily found associated with surface EGFR, whereas others, such as Eps8, were found only with intracellular receptors. During the inactivation phase, c-Cbl became EGFR associated, consistent with its postulated role in receptor attenuation. We conclude that the association of the EGFR with different proteins is compartment specific. In addition, ligand loss is the proximal cause of EGFR inactivation. Thus, regulated trafficking could potentially influence the pattern as well as the duration of signal transduction.

Indexed as

Adaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportEndocytosisSignal TransductionCell LineEndosomesEnzyme ActivationEpithelial CellsErbB ReceptorsHumansIntracellular Signaling Peptides and ProteinsLigandsMicroscopy, FluorescenceModels, BiologicalPhosphorylationPhosphotyrosineAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportEPS8 protein, humanErbB ReceptorsIntracellular Signaling Peptides and ProteinsLigandsPhosphotyrosineProteinsSHC1 protein, humanShc Signaling Adaptor ProteinsSrc Homology 2 Domain-Containing, Transforming Protein 1Tyrosine

Identifiers

PMID11408594
PMCPMC37350
OpenAlexW2143891754

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.