ArticleProceedings of the National Academy of Sciences of the United States of America2012
Dynamically varying interactions between heregulin and ErbB proteins detected by single-molecule analysis in living cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 47 citations in OpenAlex.
- Single molecule tracking based drug screening.Nature communications · 2024Article
- Four-color single-molecule imaging system for tracking GPCR dynamics with fluorescent HiBiT peptide.Biophysics and physicobiology · 2024Article
- Application of single-molecule analysis to singularity phenomenon of cells.Biophysics and physicobiology · 2024Article
- Technologies for whole-cell modeling: Genome-wide reconstruction of a cell in silico.Development, growth & differentiation · 2023Review
- Cell-Based Sensors for the Detection of EGF and EGF-Stimulated CaBiosensors · 2023Article
- Workflows of the Single-Molecule Imaging Analysis in Living Cells: Tutorial Guidance to the Measurement of the Drug Effects on a GPCR.Methods in molecular biology (Clifton, N.J.) · 2021Article
- In-Cell Single-Molecule Analysis of Molecular State and Reaction Kinetics Coupling.Advances in experimental medicine and biology · 2021Article
- Heterogeneity in VEGF Receptor-2 Mobility and Organization on the Endothelial Cell Surface Leads to Diverse Models of Activation by VEGF.Cell reports · 2020Article
- Measuring the affinity of protein-protein interactions on a single-molecule level by mass photometry.Analytical biochemistry · 2020Article
- Automated single-molecule imaging in living cells.Nature communications · 2018Article
- Single-molecule fluorescence-based analysis of protein conformation, interaction, and oligomerization in cellular systems.Biophysical reviews · 2018Review
- A mechanistic pan-cancer pathway model informed by multi-omics data interprets stochastic cell fate responses to drugs and mitogens.PLoS computational biology · 2018Article
- Lipid-Protein Interplay in Dimerization of Juxtamembrane Domains of Epidermal Growth Factor Receptor.Biophysical journal · 2018Article
- Transcriptionally inducible Pleckstrin homology-like domain, family A, member 1, attenuates ErbB receptor activity by inhibiting receptor oligomerization.The Journal of biological chemistry · 2018Article
- Imaging of anticancer drug action in single cells.Nature reviews. Cancer · 2017Review
- Robustness analysis of the detailed kinetic model of an ErbB signaling network by using dynamic sensitivity.PloS one · 2017Article
- Single-molecule fluorescence imaging of RalGDS on cell surfaces during signal transduction from Ras to Ral.Biophysics and physicobiology · 2017Article
- Exploring in vivo cholesterol-mediated interactions between activated EGF receptors in plasma membrane with single-molecule optical tracking.BMC biophysics · 2016Article
- Switching of the positive feedback for RAS activation by a concerted function of SOS membrane association domains.Biophysics and physicobiology · 2016Article
- The significance of membrane fluidity of feeder cell-derived substrates for maintenance of iPS cell stemness.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heregulin (HRG) belongs to the family of EGFs and activates the receptor proteins ErbB3 and ErbB4 in a variety of cell types to regulate cell fate. The interactions between HRG and ErbB3/B4 are important to the pathological mechanisms underlying schizophrenia and some cancers. Here, we observed the reaction kinetics between fluorescently labeled single HRG molecules and ErbB3/B4 on the surfaces of MCF-7 human breast cancer cells. The equilibrium association and the dissociation from equilibrium were also measured using single-molecule imaging techniques. The unitary association processes mirrored the EGF and ErbB1 interactions in HeLa cells [Teramura Y, et al. (2006) EMBO J 25:4215-4222], suggesting that the predimerization of the receptors, followed by intermediate formation (between the first and second ligand-binding events to a receptor dimer), accelerated the formation of doubly liganded signaling dimers of the receptor molecules. However, the dissociation analysis suggested that the first HRG dissociation from the doubly liganded dimer was rapid, but the second dissociation from the singly liganded dimer was slow. The dissociation rate constant from the liganded monomer was intermediate. The dynamic changes in the association and dissociation kinetics in relation to the dimerization of ErbB displayed negative cooperativity, which resulted in apparent low- and high-affinity sites of HRG association on the cell surface.
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