ArticleBulletin of mathematical biology2012
A "trimer of dimers"-based model for the chemotactic signal transduction network in bacterial chemotaxis.
Article in Bulletin of mathematical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Identification of the governing equation of stimulus-response data for run-and-tumble dynamics.PLoS computational biology · 2025Article
- Individual based models exhibiting Lévy-flight type movement induced by intracellular noise.Journal of mathematical biology · 2021Article
- Comparative Genomic Analysis of ThreeMicroorganisms · 2021Article
- Review
- The role of intracellular signaling in the stripe formation in engineered Escherichia coli populations.PLoS computational biology · 2018Article
- Mathematical Analysis of the Escherichia coli Chemotaxis Signalling Pathway.Bulletin of mathematical biology · 2018Article
- Derivation of the bacterial run-and-tumble kinetic equation from a model with biochemical pathway.Journal of mathematical biology · 2016Article
- Progress and perspectives in signal transduction, actin dynamics, and movement at the cell and tissue level: lessons fromInterface focus · 2016Review
- Moment-flux models for bacterial chemotaxis in large signal gradients.Journal of mathematical biology · 2016Article
- Macroscopic equations for bacterial chemotaxis: integration of detailed biochemistry of cell signaling.Journal of mathematical biology · 2015Article
- Excitation and adaptation in bacteria-a model signal transduction system that controls taxis and spatial pattern formation.International journal of molecular sciences · 2013Article
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Authors and funding
2 authors.
Funding
Abstract
The network that controls chemotaxis in Escherichia coli is one of the most completely characterized signal transduction systems to date. Receptor clustering accounts for characteristics such as high sensitivity, precise adaptation over a wide dynamic range of ligand concentrations, and robustness to variations in the amounts of intracellular proteins. To gain insights into the structure-function relationship of receptor clusters and understand the mechanism behind the high-performance signaling, we develop and analyze a model for a single trimer of dimers. This new model extends an earlier model (Spiro et al. in Proc. Natl. Acad. Sci. 94:7263-7268, 1997) to incorporate the recent experimental findings that the core structure of receptor clusters is the trimer of receptor dimers. We show that the model can reproduce most of the experimentally-observed behaviors, including excitation, adaptation, high sensitivity, and robustness to parameter variations. In addition, the model makes a number of new predictions as to how the adaptation time varies with the expression level of various proteins involved in signal transduction. Our results provide a more mechanistically-based description of the structure-function relationship for the signaling system, and show the key role of the interaction among dimer members of the trimer in the chemotactic response of cells.
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