ArticleJournal of the Royal Society, Interface2014
Catalytic constants enable the emergence of bistability in dual phosphorylation.
Article in Journal of the Royal Society, Interface, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- In distributive phosphorylation catalytic constants enable non-trivial dynamics.Journal of mathematical biology · 2024Article
- Kinetics of diffusion-influenced multisite phosphorylation with enzyme reactivation.Biopolymers · 2024Article
- Article
- Topological descriptors of the parameter region of multistationarity: Deciding upon connectivity.PLoS computational biology · 2023Article
- Network regulation meets substrate modification chemistry.Journal of the Royal Society, Interface · 2023Article
- Article
- Symmetry breaking meets multisite modification.eLife · 2021Article
- Gain and loss of function mutations in biological chemical reaction networks: a mathematical model with application to colorectal cancer cells.Journal of mathematical biology · 2021Article
- Exploring cyclic networks of multisite modification reveals origins of information processing characteristics.Scientific reports · 2020Article
- Homo-Oligomerisation in Signal Transduction: Dynamics, Homeostasis, Ultrasensitivity, Bistability.Journal of theoretical biology · 2020Article
- Robustness and parameter geography in post-translational modification systems.PLoS computational biology · 2020Article
- Regions of multistationarity in cascades of Goldbeter-Koshland loops.Journal of mathematical biology · 2019Article
- Exploring the intrinsic behaviour of multisite phosphorylation systems as part of signalling pathways.Journal of the Royal Society, Interface · 2018Article
- Dynamics of Posttranslational Modification Systems: Recent Progress and Future Directions.Biophysical journal · 2018Review
- Identifying parameter regions for multistationarity.PLoS computational biology · 2017Article
- Kinase Inhibition Leads to Hormesis in a Dual Phosphorylation-Dephosphorylation Cycle.PLoS computational biology · 2016Article
- Core signalling motif displaying multistability through multi-state enzymes.Journal of the Royal Society, Interface · 2016Article
- Long-term dynamics of multisite phosphorylation.Molecular biology of the cell · 2016Article
- Mixed mechanisms of multi-site phosphorylation.Journal of the Royal Society, Interface · 2015Article
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2 authors.
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Abstract
Dual phosphorylation of proteins is a principal component of intracellular signalling. Bistability is considered an important property of such systems and its origin is not yet completely understood. Theoretical studies have established parameter values for multistationarity and bistability for many types of proteins. However, up to now no formal criterion linking multistationarity and bistability to the parameter values characterizing dual phosphorylation has been established. Deciding whether an unclassified protein has the capacity for bistability, therefore requires careful numerical studies. Here, we present two general algebraic conditions in the form of inequalities. The first employs the catalytic constants, and if satisfied guarantees multistationarity (and hence the potential for bistability). The second involves the catalytic and Michaelis constants, and if satisfied guarantees uniqueness of steady states (and hence absence of bistability). Our method also allows for the direct computation of the total concentration values such that multistationarity occurs. Applying our results yields insights into the emergence of bistability in the ERK-MEK-MKP system that previously required a delicate numerical effort. Our algebraic conditions present a practical way to determine the capacity for bistability and hence will be a useful tool for examining the origin of bistability in many models containing dual phosphorylation.
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