Literature DB >> 21961584

Integrating multiple signals into cell decisions by networks of protein modification cycles.

Luca Cerone1, Javier Muñoz-Garcia, Zoltán Neufeld.   

Abstract

Posttranslational protein modifications play a key role in regulating cellular processes. We present a general model of reversible protein modification networks and demonstrate that a single protein modified by several enzymes is capable of integrating multiple signals into robust digital decisions by switching between multiple forms that can activate distinct cellular processes. First we consider two competing protein modification cycles and show that in the saturated regime, the protein is concentrated into a single form determined by the enzyme activities. We generalize this to protein modification networks with tree structure controlled by multiple enzymes that can be characterized by their phase diagram, which is a partition of the space of enzyme activities into regions corresponding to different dominant forms. We show that the phase diagram can be obtained analytically from the wiring diagram of the modification network by recursively solving a set of balance equations for the steady-state distributions and then applying a positivity condition to determine the regions corresponding to different responses. We also implement this method in a computer algebra system that automatically generates the phase diagram as a set of inequalities. Based on this theoretical framework, we determine some general properties of protein modification systems.
Copyright © 2011 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Year:  2011        PMID: 21961584      PMCID: PMC3183812          DOI: 10.1016/j.bpj.2011.08.046

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  29 in total

1.  A positive-feedback-based bistable 'memory module' that governs a cell fate decision.

Authors:  Wen Xiong; James E Ferrell
Journal:  Nature       Date:  2003-11-27       Impact factor: 49.962

2.  Detection of multistability, bifurcations, and hysteresis in a large class of biological positive-feedback systems.

Authors:  David Angeli; James E Ferrell; Eduardo D Sontag
Journal:  Proc Natl Acad Sci U S A       Date:  2004-02-06       Impact factor: 11.205

Review 3.  Sniffers, buzzers, toggles and blinkers: dynamics of regulatory and signaling pathways in the cell.

Authors:  John J Tyson; Katherine C Chen; Bela Novak
Journal:  Curr Opin Cell Biol       Date:  2003-04       Impact factor: 8.382

4.  A mechanism for memory storage insensitive to molecular turnover: a bistable autophosphorylating kinase.

Authors:  J E Lisman
Journal:  Proc Natl Acad Sci U S A       Date:  1985-05       Impact factor: 11.205

5.  Control of Smad7 stability by competition between acetylation and ubiquitination.

Authors:  Eva Grönroos; Ulf Hellman; Carl-Henrik Heldin; Johan Ericsson
Journal:  Mol Cell       Date:  2002-09       Impact factor: 17.970

Review 6.  Protein molecules as computational elements in living cells.

Authors:  D Bray
Journal:  Nature       Date:  1995-07-27       Impact factor: 49.962

7.  An amplified sensitivity arising from covalent modification in biological systems.

Authors:  A Goldbeter; D E Koshland
Journal:  Proc Natl Acad Sci U S A       Date:  1981-11       Impact factor: 11.205

8.  The rational parameterization theorem for multisite post-translational modification systems.

Authors:  Matthew Thomson; Jeremy Gunawardena
Journal:  J Theor Biol       Date:  2009-09-16       Impact factor: 2.691

9.  Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades.

Authors:  Nick I Markevich; Jan B Hoek; Boris N Kholodenko
Journal:  J Cell Biol       Date:  2004-01-26       Impact factor: 10.539

Review 10.  Bistability by multiple phosphorylation of regulatory proteins.

Authors:  Orsolya Kapuy; Debashis Barik; Maria Rosa Domingo Sananes; John J Tyson; Béla Novák
Journal:  Prog Biophys Mol Biol       Date:  2009-06-11       Impact factor: 3.667

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