NDLI: Product dependence and bifunctionality compromise the ultrasensitivity of signal transduction cascades.

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Product dependence and bifunctionality compromise the ultrasensitivity of signal transduction cascades.

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Product dependence and bifunctionality compromise the ultrasensitivity of signal transduction cascades.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ortega, Fernando Mas, Francesc Westerhoff, Hans V. Acerenza, Luis Cascante, Marta
Description	Author Affiliation: Ortega F ( Centre de Química Teòrica at Parc Científic de Barcelona and Departament de Química Física, Facultat de Química, Universitat de Barcelona, C/Martí i Franquès, 1. E-08028 Barcelona, Spain.);
Abstract	Covalent modification cycles are ubiquitous. Theoretical studies have suggested that they serve to increase sensitivity. However, this suggestion has not been corroborated experimentally in vivo. Here, we demonstrate that the assumptions of the theoretical studies, i.e., irreversibility and absence of product inhibition, were not trivial: when the conversion reactions are close to equilibrium or saturated by their product, 'zero-order' ultrasensitivity disappears. For high sensitivities to arise, not only substrate saturation (zero-order) but also high equilibrium constants and low product saturation are required. Many covalent modification cycles are catalyzed by one bifunctional 'ambiguous' enzyme rather than by two independent proteins. This makes high substrate concentration and low product concentration for both reactions of the cycle inconsistent; such modification cycles cannot have high responses. Defining signal strength as ratios of modified (e.g., phosphorylated) over unmodified protein, signal-to-signal response sensitivity equals 1: signal strength should remain constant along a cascade of ambiguous modification cycles. We also show that the total concentration of a signalling effector protein cannot affect the signal emanating from a modification cycle catalyzed by an ambiguous enzyme if the ratio of the two forms of the effector protein is not altered. This finding may explain the experimental result that the pivotal signal transduction protein PII plus its paralogue GlnK do not control steady-state N-signal transduction in Escherichia coli. It also rationalizes the absence of strong phenotypes for many signal-transduction proteins. Emphasis on extent of modification of these proteins is perhaps more urgent than transcriptome analysis.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	3
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Signal Transduction Physiology Enzymes Metabolism Kinetics Models, Biological Sensitivity And Specificity Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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