ArticleMolecular and cellular biology2010
Epidermal growth factor receptor activation remodels the plasma membrane lipid environment to induce nanocluster formation.
Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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.
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.
Who cites it
51 citing papers in PubMed, 90 citations in OpenAlex.
- EGFR does not directly interact with cortical actin: A SRRF'n'TIRF study.Biophysical journal · 2024Article
- Dysregulation of cellular membrane homeostasis as a crucial modulator of cancer risk.The FEBS journal · 2024Review
- Review
- The dependence of EGFR oligomerization on environment and structure: A camera-based N&B study.Biophysical journal · 2022Article
- Multivalent Ligand-Nanoparticle Conjugates Amplify Reactive Oxygen Species Second Messenger Generation and Enhance Epidermal Growth Factor Receptor Phosphorylation.Bioconjugate chemistry · 2022Article
- Osimertinib-resistant NSCLC cells activate ERBB2 and YAP/TAZ and are killed by neratinib.Biochemical pharmacology · 2021Article
- Influenza A viruses use multivalent sialic acid clusters for cell binding and receptor activation.PLoS pathogens · 2020Article
- Deficiency of GABARAP but not its Paralogs Causes Enhanced EGF-induced EGFR Degradation.Cells · 2020Article
- Receptor tyrosine kinase activation: From the ligand perspective.Current opinion in cell biology · 2020Review
- A Brief History of Single-Particle Tracking of the Epidermal Growth Factor Receptor.Methods and protocols · 2019Review
- Functional link between plasma membrane spatiotemporal dynamics, cancer biology, and dietary membrane-altering agents.Cancer metastasis reviews · 2018Review
- The tyrosine phosphorylated pro-survival form of Fas intensifies the EGF-induced signal in colorectal cancer cells through the nuclear EGFR/STAT3-mediated pathway.Scientific reports · 2018Article
- Phosphorylated EGFR Dimers Are Not Sufficient to Activate Ras.Cell reports · 2018Article
- Bile acids target proteolipid nano-assemblies of EGFR and phosphatidic acid in the plasma membrane for stimulation of MAPK signaling.PloS one · 2018Article
- Intrinsic protein disorder in oncogenic KRAS signaling.Cellular and molecular life sciences : CMLS · 2017Review
- EGF and NRG induce phosphorylation of HER3/ERBB3 by EGFR using distinct oligomeric mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Probing the Heterogeneity of Protein Kinase Activation in Cells by Super-resolution Microscopy.ACS nano · 2017Article
- Article
- Article
- The Epidermal Growth Factor Receptor Forms Location-Dependent Complexes in Resting Cells.Biophysical journal · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
Signal transduction is regulated by the lateral segregation of proteins into nanodomains on the plasma membrane. However, the molecular mechanisms that regulate the lateral segregation of cell surface receptors, such as receptor tyrosine kinases, upon ligand binding are unresolved. Here we used high-resolution spatial mapping to investigate the plasma membrane nanoscale organization of the epidermal growth factor (EGF) receptor (EGFR). Our data demonstrate that in serum-starved cells, the EGFR exists in preformed, cholesterol-dependent, actin-independent nanoclusters. Following stimulation with EGF, the number and size of EGFR nanoclusters increase in a time-dependent manner. Our data show that the formation of EGFR nanoclusters requires receptor tyrosine kinase activity. Critically, we show for the first time that production of phosphatidic acid by phospholipase D2 (PLD2) is essential for ligand-induced EGFR nanocluster formation. In accordance with its crucial role in regulating EGFR nanocluster formation, we demonstrate that modulating PLD2 activity tunes the degree of EGFR nanocluster formation and mitogen-activated protein kinase signal output. Together, these data show that EGFR activation drives the formation of signaling domains by regulating the production of critical second-messenger lipids and modifying the local membrane lipid environment.
Indexed as
Identifiers
What Socratic holds
Registered trials
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 Socratic graph.