ArticleCell research2014
Regulation of EGFR nanocluster formation by ionic protein-lipid interaction.
Article in Cell research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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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.
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Who cites it
73 citing papers in PubMed, 166 citations in OpenAlex.
- SRF3 couples cellular iron homeostasis and defense responses through ubiquitin-dependent nano-organization.Science advances · 2026Article
- Structural Basis of Lymphangiogenic Receptor VEGFR-3 Activation Mediated by Distinctive Clustering of the Ligand-Receptor Complex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- High-Fat Diet Remodels Plasma Membrane Rigidity to Potentiate Colonocyte Stemness in Mice.Cellular and molecular gastroenterology and hepatology · 2026Article
- A conserved basic motif mediates membrane anchoring and TRAF2 recruitment across costimulatory TNFRs.The EMBO journal · 2026Article
- Integrative structural and dynamics studies of epidermal growth factor receptor (EGFR).Experimental & molecular medicine · 2026Review
- Article
- Quantum Well-Enhanced Plasmonic Substrate to Enhance Spontaneously Blinking Fluorescence for Single-Molecule Localization Microscopy.Analytical chemistry · 2026Article
- Beyond the membrane: rethinking EGFR signaling in physiology and cancer.Cellular and molecular life sciences : CMLS · 2026Review
- Lipids regulate epidermal growth factor receptor activation by its ligands.Biochemical Society transactions · 2026Review
- Article
- ClusterNet: Classifying Single-Molecule Localization Microscopy Datasets with Graph-Based Deep Learning of Supracluster Structure.Small science · 2025Article
- Active regulation of the epidermal growth factor receptor by the membrane bilayer.bioRxiv : the preprint server for biology · 2025Article
- Article
- Building a dynamic model for EGFR-family dimerization using quantitative, live-cell fluorescence methods.Biophysical journal · 2025Review
- Ellagic Acid and Its Nanoparticles Mitigate Atherosclerosis by Elevating Low-Density Lipoprotein Receptor Levels Through Targeting of the Epidermal Growth Factor Receptor.FASEB bioAdvances · 2025Article
- Review
- Multivalent DNA Origami Enables Single-Molecule Dissection of Integrin αvβ6-Receptor Tyrosine Kinase Crosstalk in Cancer Biology.ACS nano · 2025Article
- Identification of TNFAIP2 as a unique cellular regulator of CSF-1 receptor activation.Life science alliance · 2025Article
- Application of EGFR-TKIs in brain tumors, a breakthrough in future?Journal of translational medicine · 2025Review
- Biomembrane structure at the molecular level and its application in precision medicine.Biophysics reviews · 2025Review
13 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The abnormal activation of epidermal growth factor receptor (EGFR) is strongly associated with a variety of human cancers but the underlying molecular mechanism is not fully understood. By using direct stochastic optical reconstruction microscopy (dSTORM), we find that EGFR proteins form nanoclusters in the cell membrane of both normal lung epithelial cells and lung cancer cells, but the number and size of clusters significantly increase in lung cancer cells. The formation of EGFR clusters is mediated by the ionic interaction between the anionic lipid phosphatidylinositol-4,5-bisphosphate (PIP2) in the plasma membrane and the juxtamembrane (JM) region of EGFR. Disruption of EGFR clustering by PIP2 depletion or JM region mutation impairs EGFR activation and downstream signaling. Furthermore, JM region mutation in constitutively active EGFR mutant attenuates its capability of cell transformation. Collectively, our findings highlight the key roles of anionic phospholipids in EGFR signaling and function, and reveal a novel mechanism to explain the aberrant activation of EGFR in cancers.
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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.