ArticleMolecular biology of the cell2015
Orchestration of ErbB3 signaling through heterointeractions and homointeractions.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 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
16 citing papers in PubMed, 26 citations in OpenAlex.
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- HER4 is a high-affinity dimerization partner for all EGFR/HER/ErbB family proteins.Protein science : a publication of the Protein Society · 2024Article
- Multiscale imaging and quantitative analysis of plasma membrane protein-cortical actin interplay.Biophysical journal · 2023Article
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- Signalling dynamics, cell decisions, and homeostatic control in health and disease.Current opinion in cell biology · 2022Review
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- Modeling the Cluster Size Distribution of Vascular Endothelial Growth Factor (VEGF) Receptors.Bioinformatics and biology insights · 2022Article
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- Multisite EGFR phosphorylation is regulated by adaptor protein abundances and dimer lifetimes.Molecular biology of the cell · 2020Article
- Homo- and Heteroassociations Drive Activation of ErbB3.Biophysical journal · 2019Article
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- Transcriptionally inducible Pleckstrin homology-like domain, family A, member 1, attenuates ErbB receptor activity by inhibiting receptor oligomerization.The Journal of biological chemistry · 2018Article
- Effect of Spatial Inhomogeneities on the Membrane Surface on Receptor Dimerization and Signal Initiation.Frontiers in cell and developmental biology · 2016Article
- Spatial Stochastic Model of the Pre-B Cell Receptor.IEEE/ACM transactions on computational biology and bioinformaticsArticle
Corrections and comments
- Erratum issuedCorrection.2016 · Hanien, Dorit [corrected to Hanein, Dorit]
Authors and funding
14 authors at 5 institutions in 1 country.
Funding
Abstract
Members of the ErbB family of receptor tyrosine kinases are capable of both homointeractions and heterointeractions. Because each receptor has a unique set of binding sites for downstream signaling partners and differential catalytic activity, subtle shifts in their combinatorial interplay may have a large effect on signaling outcomes. The overexpression and mutation of ErbB family members are common in numerous human cancers and shift the balance of activation within the signaling network. Here we report the development of a spatial stochastic model that addresses the dynamics of ErbB3 homodimerization and heterodimerization with ErbB2. The model is based on experimental measures for diffusion, dimer off-rates, kinase activity, and dephosphorylation. We also report computational analysis of ErbB3 mutations, generating the prediction that activating mutations in the intracellular and extracellular domains may be subdivided into classes with distinct underlying mechanisms. We show experimental evidence for an ErbB3 gain-of-function point mutation located in the C-lobe asymmetric dimerization interface, which shows enhanced phosphorylation at low ligand dose associated with increased kinase activity.
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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.