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dc.contributor.authorCsikász-Nagy, Attilaen_GB
dc.contributor.authorCardelli, Lucaen_GB
dc.contributor.authorSoyer, Orkun S.en_GB
dc.date.accessioned2012-08-16T15:24:00Zen_GB
dc.date.accessioned2013-03-20T12:38:19Z
dc.date.issued2011en_GB
dc.description.abstractPhosphorelays are extended two-component signalling systems found in diverse bacteria, lower eukaryotes and plants. Only few of these systems are characterized, and we still lack a full understanding of their signalling abilities. Here, we aim to achieve a global understanding of phosphorelay signalling and its dynamical properties. We develop a generic model, allowing us to systematically analyse response dynamics under different assumptions. Using this model, we find that the steady-state concentration of phosphorylated protein at the final layer of a phosphorelay is a linearly increasing, but eventually saturating function of the input. In contrast, the intermediate layers can display ultrasensitivity. We find that such ultrasensitivity is a direct result of the phosphorelay biochemistry; shuttling of a single phosphate group from the first to the last layer. The response dynamics of the phosphorelay results in tolerance of cross-talk, especially when it occurs as cross-deactivation. Further, it leads to a high signal-to-noise ratio for the final layer. We find that a relay length of four, which is most commonly observed, acts as a saturating point for these dynamic properties. These findings suggest that phosphorelays could act as a mechanism to reduce noise and effects of cross-talk on the final layer of the relay and enforce its input-response relation to be linear. In addition, our analysis suggests that middle layers of phosphorelays could embed thresholds. We discuss the consequence of these findings in relation to why cells might use phosphorelays along with enzymatic kinase cascades.en_GB
dc.identifier.citationVol. 8 (57), pp. 480 - 488en_GB
dc.identifier.doi10.1098/rsif.2010.0336en_GB
dc.identifier.urihttp://hdl.handle.net/10036/3699en_GB
dc.language.isoenen_GB
dc.publisherThe Royal Societyen_GB
dc.relation.urlhttp://dx.doi.org/10.1098/rsif.2010.0336en_GB
dc.subjectPhosphoproteinsen_GB
dc.subjectPhosphorylationen_GB
dc.subjectProtein Kinasesen_GB
dc.subjectSignal Transductionen_GB
dc.subjectBiological modelsen_GB
dc.subjectUltrasensitivityen_GB
dc.subjectComputational modellingen_GB
dc.subjectCross-talken_GB
dc.subjectNoiseen_GB
dc.subjectTwo-component signallingen_GB
dc.titleResponse dynamics of phosphorelays suggest their potential utility in cell signallingen_GB
dc.typeArticleen_GB
dc.date.available2012-08-16T15:24:00Zen_GB
dc.date.available2013-03-20T12:38:19Z
exeter.place-of-publicationEnglanden_GB
dc.descriptionCopyright © 2010 The Royal Societyen_GB
dc.identifier.eissn1742-5662en_GB
dc.identifier.journalJournal of the Royal Society Interfaceen_GB


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