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Unlimited multistability in multisite phosphorylation systems

Author

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  • Matthew Thomson

    (Biophysics Program, Harvard University, Cambridge, Massachusetts 02138, USA)

  • Jeremy Gunawardena

    (Harvard Medical School, Boston, Massachusetts 02115, USA)

Abstract

Cellular information processing While naked DNA has a relatively static and easy to grasp information capacity — 2 bits per nucleotide—reversible chemical modification at multiple sites in even a single protein encodes a potentially large and so far untractable amount of information. Here Matthew Thomson and Jeremy Gunawardena reduce the 3 × 2n nonlinear differential equations describing dynamic phosphorylation at n sites on a given protein (n varying from less than 7 in bacteria to more than 150 in eukaryotes) to just two algebraic equations. The method allows them to estimate the information capacity of a signalling protein as a function of varying amounts of modifying enzymes (kinases and phosphatases). Algebraic geometry could extend the method to diverse and parallel enzymatic modifications such as those governing the 'histone code' of gene regulation.

Suggested Citation

  • Matthew Thomson & Jeremy Gunawardena, 2009. "Unlimited multistability in multisite phosphorylation systems," Nature, Nature, vol. 460(7252), pages 274-277, July.
    • Handle: RePEc:nat:nature:v:460:y:2009:i:7252:d:10.1038_nature08102
    DOI: 10.1038/nature08102
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    Cited by:

    1. Carlo Chan & Xinfeng Liu & Liming Wang & Lee Bardwell & Qing Nie & Germán Enciso, 2012. "Protein Scaffolds Can Enhance the Bistability of Multisite Phosphorylation Systems," PLOS Computational Biology, Public Library of Science, vol. 8(6), pages 1-9, June.
    2. Li, Chunbiao & Sprott, Julien Clinton & Kapitaniak, Tomasz & Lu, Tianai, 2018. "Infinite lattice of hyperchaotic strange attractors," Chaos, Solitons & Fractals, Elsevier, vol. 109(C), pages 76-82.
    3. Löb, Daniel & Priester, Christopher & Drossel, Barbara, 2016. "Multistability and sustained oscillations in a model for protein complex formation," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 445(C), pages 85-101.
    4. Andreas Petrides & Glenn Vinnicombe, 2018. "Enzyme sequestration by the substrate: An analysis in the deterministic and stochastic domains," PLOS Computational Biology, Public Library of Science, vol. 14(5), pages 1-23, May.

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