Evidence map›Paper›PMID 41417903›Full record

ArticleScience advances2025

EGFR activation requires cholesterol interaction at the inner leaflet of the plasma membrane.

Do-Hyeon Kim, Minh-Triet Hong, Eduard V Bocharov, Soyeon Park, Yaroslav V Bershatsky, Pavel E Volynsky, Eui Kim, Roman G Efremov, Wonhwa Cho, Seung-Yeol Park and 1 more

Abstract read
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

11 authors.

Do-Hyeon KimDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea.ORCID 0000-0002-0116-7756
Minh-Triet HongDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea.ORCID 0000-0002-9426-6832
Eduard V BocharovDepartment of Structural Biology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, Moscow 117997, Russian Federation.ORCID 0000-0002-3635-1609
Soyeon ParkDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea.ORCID 0000-0003-2769-333X
Yaroslav V BershatskyDepartment of Structural Biology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, Moscow 117997, Russian Federation.ORCID 0000-0001-9863-4666
Pavel E VolynskyDepartment of Structural Biology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, Moscow 117997, Russian Federation.ORCID 0000-0002-0471-4188
Eui KimDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea.ORCID 0009-0002-3143-0989
Roman G EfremovDepartment of Structural Biology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, Moscow 117997, Russian Federation.
Wonhwa ChoDepartment of Chemistry, University of Illinois at Chicago, Chicago, IL 60607, USA.
Seung-Yeol ParkDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea.ORCID 0000-0001-5061-4535
Sung Ho RyuDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea.ORCID 0000-0003-0913-3048

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signal transduction by the human epidermal growth factor receptor (EGFR) is modulated by its ligands as well as by the various compounds on the plasma membrane (PM), including cholesterol. Here, using single-molecule coimmunoimmobilization, we found that cholesterol in the inner leaflet of PM plays an essential role in ligand-dependent EGFR activation. This was done by direct and quantitative examination of the interaction between EGFR and cholesterol on the PM of a living cell. Structural analysis using molecular dynamics simulations and nuclear magnetic resonance spectroscopy further revealed that cholesterol in the inner leaflet is critically important for the transition of the dimeric transmembrane domain (TMD) of the receptor to the active conformation. We also identified the specific pattern of residues Ile

Indexed as

Cell MembraneCholesterolErbB ReceptorsEpidermal Growth FactorHumansLigandsMolecular Dynamics SimulationProtein BindingProtein DomainsSignal TransductionCholesterolEGFR protein, humanEpidermal Growth FactorErbB ReceptorsLigands

Identifiers

PMID41417903
PMCPMC12716419

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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.