ArticleThe Journal of biological chemistry2008
Computational models of tandem SRC homology 2 domain interactions and application to phosphoinositide 3-kinase.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Biophysical assay for tethered signaling reactions reveals tether-controlled activity for the phosphatase SHP-1.Science advances · 2017Article
- Dimerization-based control of cooperativity.Molecular bioSystems · 2014Article
- Modeling the effect of APC truncation on destruction complex function in colorectal cancer cells.PLoS computational biology · 2013Article
- Systems model of T cell receptor proximal signaling reveals emergent ultrasensitivity.PLoS computational biology · 2013Article
- Modeling formalisms in Systems Biology.AMB Express · 2011Article
- Guidelines for visualizing and annotating rule-based models.Molecular bioSystems · 2011Article
- Quantifying intramolecular binding in multivalent interactions: a structure-based synergistic study on Grb2-Sos1 complex.PLoS computational biology · 2011Article
- In chemotaxing fibroblasts, both high-fidelity and weakly biased cell movements track the localization of PI3K signaling.Biophysical journal · 2011Article
- Hierarchical graphs for rule-based modeling of biochemical systems.BMC bioinformatics · 2011Article
- SH2 domains recognize contextual peptide sequence information to determine selectivity.Molecular & cellular proteomics : MCP · 2010Article
- RuleMonkey: software for stochastic simulation of rule-based models.BMC bioinformatics · 2010Article
- Computational models of the Notch network elucidate mechanisms of context-dependent signaling.PLoS computational biology · 2009Article
- A bipolar clamp mechanism for activation of Jak-family protein tyrosine kinases.PLoS computational biology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Intracellular signal transduction proteins typically utilize multiple interaction domains for proper targeting, and thus a broad diversity of distinct signaling complexes may be assembled. Considering the coordination of only two such domains, as in tandem Src homology 2 (SH2) domain constructs, gives rise to a kinetic scheme that is not adequately described by simple models used routinely to interpret in vitro binding measurements. To analyze the interactions between tandem SH2 domains and bisphosphorylated peptides, we formulated detailed kinetic models and applied them to the phosphoinositide 3-kinase p85 regulatory subunit/platelet-derived growth factor beta-receptor system. Data for this system from different in vitro assay platforms, including surface plasmon resonance, competition binding, and isothermal titration calorimetry, were reconciled to estimate the magnitude of the cooperativity characterizing the sequential binding of the high and low affinity SH2 domains (C-SH2 and N-SH2, respectively). Compared with values based on an effective volume approximation, the estimated cooperativity is 3 orders of magnitude lower, indicative of significant structural constraints. Homodimerization of full-length p85 was found to be an alternative mechanism for high avidity binding to phosphorylated platelet-derived growth factor receptors, which would render the N-SH2 domain dispensable for receptor binding.
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