ArticleBiophysical journal2013
Dynamic transition states of ErbB1 phosphorylation predicted by spatial stochastic modeling.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Multisite EGFR phosphorylation is regulated by adaptor protein abundances and dimer lifetimes.Molecular biology of the cell · 2020Article
- Spatial EGFR Dynamics and Metastatic Phenotypes Modulated by Upregulated EphB2 and Src Pathways in Advanced Prostate Cancer.Cancers · 2019Article
- Assessing metastatic potential of breast cancer cells based on EGFR dynamics.Scientific reports · 2019Article
- Effect of Spatial Inhomogeneities on the Membrane Surface on Receptor Dimerization and Signal Initiation.Frontiers in cell and developmental biology · 2016Article
- Orchestration of ErbB3 signaling through heterointeractions and homointeractions.Molecular biology of the cell · 2015Article
- Effect of phosphorylation on EGFR dimer stability probed by single-molecule dynamics and FRET/FLIM.Biophysical journal · 2015Article
- Pinning down the EGF receptor.Biophysical journal · 2014Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
ErbB1 overexpression is strongly linked to carcinogenesis, motivating better understanding of erbB1 dimerization and activation. Recent single-particle-tracking data have provided improved measures of dimer lifetimes and strong evidence that transient receptor coconfinement promotes repeated interactions between erbB1 monomers. Here, spatial stochastic simulations explore the potential impact of these parameters on erbB1 phosphorylation kinetics. This rule-based mathematical model incorporates structural evidence for conformational flux of the erbB1 extracellular domains, as well as asymmetrical orientation of erbB1 cytoplasmic kinase domains during dimerization. The asymmetric dimer model considers the theoretical consequences of restricted transactivation of erbB1 receptors within a dimer, where the N-lobe of one monomer docks with the C-lobe of the second monomer and triggers its catalytic activity. The dynamic nature of the erbB1 phosphorylation state is shown by monitoring activation states of individual monomers as they diffuse, bind, and rebind after ligand addition. The model reveals the complex interplay between interacting liganded and nonliganded species and the influence of their distribution and abundance within features of the membrane landscape.
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