Evidence map›Paper›PMID 15908575›Full record

ArticleBiophysical journal2005

Cholesterol dictates the freedom of EGF receptors and HER2 in the plane of the membrane.

Galya Orr, Dehong Hu, Serdar Ozçelik, Lee K Opresko, H Steven Wiley, Steven D Colson

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

65 citing papers in PubMed, 131 citations in OpenAlex.

  1. Emergent eukaryotic directional sensing via receptor degradation and diffusion.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  7. Immuno-PET Detects Antibody-Drug Potency on Coadministration with Statins.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2023
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  16. Acute Statin Treatment Improves Antibody Accumulation in EGFR- and PSMA-Expressing Tumors.Clinical cancer research : an official journal of the American Association for Cancer Research · 2020
    Article
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  19. Review
  20. Article

5 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

6 authors at 1 institution in 1 country.

Galya OrrChemical and Biological Sciences Divisions, Pacific Northwest National Laboratory, Richland, Washington 99354, USA. galya.orr@pnl.gov
Dehong Hu
Serdar Ozçelik
Lee K Opresko
H Steven Wiley
Steven D Colson
Pacific Northwest National Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The flow of information through the epidermal growth factor receptor (EGFR) is shaped by molecular interactions in the plasma membrane. The EGFR is associated with lipid rafts, but their role in modulating receptor mobility and subsequent interactions is unclear. To investigate the role of nanoscale rafts in EGFR dynamics, we used single-molecule fluorescence imaging to track individual receptors and their dimerization partner, human epidermal growth factor receptor 2 (HER2), in the membrane of human mammary epithelial cells. We found that the motion of both receptors was interrupted by dwellings within nanodomains. EGFR was significantly less mobile than HER2. This difference was likely due to F-actin because its depolymerization led to similar diffusion patterns between the EGFR and HER2. Manipulations of membrane cholesterol content dramatically altered the diffusion pattern of both receptors. Cholesterol depletion led to almost complete confinement of the receptors, whereas cholesterol enrichment extended the boundaries of the restricted areas. Interestingly, F-actin depolymerization partially restored receptor mobility in cholesterol-depleted membranes. Our observations suggest that membrane cholesterol provides a dynamic environment that facilitates the free motion of EGFR and HER2, possibly by modulating the dynamic state of F-actin. The association of the receptors with lipid rafts could therefore promote their rapid interactions only upon ligand stimulation.

Indexed as

Cell LineCell MembraneCholesterolEpithelial CellsErb-b2 Receptor Tyrosine KinasesErbB ReceptorsHumansMammary Glands, HumanMembrane MicrodomainsMotionProtein TransportCholesterolErb-b2 Receptor Tyrosine KinasesErbB Receptors

Identifiers

PMID15908575
PMCPMC1366621
OpenAlexW2017615656

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.