ArticleBiophysical journal2008
Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 65 citations in OpenAlex.
- Article
- Fluorescence Anisotropy for Detailed Analysis of Doxorubicin Loading into DNA Origami Nanocarriers for Drug Delivery.ACS applied nano materials · 2025Article
- Review
- Determining the Stoichiometry of Small Protein Oligomers Using Steady-State Fluorescence Anisotropy.Biophysical journal · 2020Article
- Influenza A viruses use multivalent sialic acid clusters for cell binding and receptor activation.PLoS pathogens · 2020Article
- Comprehensive Model for Epidermal Growth Factor Receptor Ligand Binding Involving Conformational States of the Extracellular and the Kinase Domains.Frontiers in cell and developmental biology · 2020Article
- Homo- and Heteroassociations Drive Activation of ErbB3.Biophysical journal · 2019Article
- Characterizing Large-Scale Receptor Clustering on the Single Cell Level: A Comparative Plasmon Coupling and Fluorescence Superresolution Microscopy Study.The journal of physical chemistry. B · 2019Article
- Single molecule localization microscopy coupled with touch preparation for the quantification of trastuzumab-bound HER2.Scientific reports · 2018Article
- The Effect of Fluorophore Conjugation on Antibody Affinity and the Photophysical Properties of Dyes.Biophysical journal · 2018Article
- Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models.PloS one · 2017Article
- The Epidermal Growth Factor Receptor Forms Location-Dependent Complexes in Resting Cells.Biophysical journal · 2016Article
- The Dipole Potential Modifies the Clustering and Ligand Binding Affinity of ErbB Proteins and Their Signaling Efficiency.Scientific reports · 2016Article
- EGFP oligomers as natural fluorescence and hydrodynamic standards.Scientific reports · 2016Article
- Regulation of PKR by RNA: formation of active and inactive dimers.Biochemistry · 2015Article
- Understanding FRET as a research tool for cellular studies.International journal of molecular sciences · 2015Review
- Time-domain microfluidic fluorescence lifetime flow cytometry for high-throughput Förster resonance energy transfer screening.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2015Article
- Structure-function relationships of ErbB RTKs in the plasma membrane of living cells.Cold Spring Harbor perspectives in biology · 2014Review
- Manipulating the lateral diffusion of surface-anchored EGF demonstrates that receptor clustering modulates phosphorylation levels.Integrative biology : quantitative biosciences from nano to macro · 2013Article
- Mathematical simulation of membrane protein clustering for efficient signal transduction.Annals of biomedical engineering · 2012Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The association of receptor tyrosine kinases is a key step in the initiation of growth factor-mediated signaling. Although the ligand-induced dimerization of inactive, monomeric receptors was the central dogma of receptor tyrosine kinase activation for decades, the existence of larger oligomers is now accepted. Both homoassociations and heteroassociations are of extreme importance in the epidermal growth factor (EGF) receptor family, leading to diverse and robust signaling. We present a statistically reliable, flow-cytometric homo-fluorescence resonance energy transfer method for the quantitative characterization of large-scale receptor clusters. We assumed that a fraction of a certain protein species is monomeric, whereas the rest are present in homoclusters of N-mers. We measured fluorescence anisotropy as a function of the saturation of fluorescent antibody binding, and fitted the model to the anisotropy data yielding the fraction of monomers and the cluster size. We found that ErbB2 formed larger homoclusters than ErbB1. Stimulation with EGF and heregulin led to a decrease in ErbB2 homocluster size, whereas ErbB1 homoclusters became larger after EGF stimulation. The activation level of ErbB2 was inversely proportional to its homocluster size. We conclude that homoclusters of ErbB1 and ErbB2 behave in a fundamentally different way. Whereas huge ErbB2 clusters serve as a reservoir of inactive coreceptors and dissociate upon stimulation, small ErbB1 homoclusters form higher-order oligomers after ligand binding.
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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 OpenQuestion graph.