ArticlePloS one2008
The Goldbeter-Koshland switch in the first-order region and its response to dynamic disorder.
Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Protein-protein complexes can undermine ultrasensitivity-dependent biological adaptation.Journal of the Royal Society, Interface · 2023Article
- Ultrasensitivity and bistability in covalent-modification cycles with positive autoregulation.Proceedings. Mathematical, physical, and engineering sciences · 2021Article
- Crosstalk and ultrasensitivity in protein degradation pathways.PLoS computational biology · 2020Article
- Tunable ultrasensitivity: functional decoupling and biological insights.Scientific reports · 2016Article
- Article
- Dynamics and stability of a three-dimensional model of cell signal transduction.Journal of mathematical biology · 2013Article
- Bell-shaped and ultrasensitive dose-response in phosphorylation-dephosphorylation cycles: the role of kinase-phosphatase complex formation.BMC systems biology · 2012Article
- Induced fit, conformational selection and independent dynamic segments: an extended view of binding events.Trends in biochemical sciences · 2010Article
- Article
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2 authors.
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Abstract
In their classical work (Proc. Natl. Acad. Sci. USA, 1981, 78:6840-6844), Goldbeter and Koshland mathematically analyzed a reversible covalent modification system which is highly sensitive to the concentration of effectors. Its signal-response curve appears sigmoidal, constituting a biochemical switch. However, the switch behavior only emerges in the 'zero-order region', i.e. when the signal molecule concentration is much lower than that of the substrate it modifies. In this work we showed that the switching behavior can also occur under comparable concentrations of signals and substrates, provided that the signal molecules catalyze the modification reaction in cooperation. We also studied the effect of dynamic disorders on the proposed biochemical switch, in which the enzymatic reaction rates, instead of constant, appear as stochastic functions of time. We showed that the system is robust to dynamic disorder at bulk concentration. But if the dynamic disorder is quasi-static, large fluctuations of the switch response behavior may be observed at low concentrations. Such fluctuation is relevant to many biological functions. It can be reduced by either increasing the conformation interconversion rate of the protein, or correlating the enzymatic reaction rates in the network.
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