Unlimited multistability in multisite phosphorylation systems

Matthew Thomson and Jeremy Gunawardena ()
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Matthew Thomson: Biophysics Program, Harvard University, Cambridge, Massachusetts 02138, USA
Jeremy Gunawardena: Harvard Medical School, Boston, Massachusetts 02115, USA

Nature, 2009, vol. 460, issue 7252, 274-277

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.

Date: 2009
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DOI: 10.1038/nature08102

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