Please use this identifier to cite or link to this item: http://cmuir.cmu.ac.th/jspui/handle/6653943832/58341
Title: Exploring the intrinsic behaviour of multisite phosphorylation systems as part of signalling pathways
Authors: Thapanar Suwanmajo
J. Krishnan
Keywords: Biochemistry, Genetics and Molecular Biology
Chemical Engineering
Engineering
Materials Science
Issue Date: 1-Jan-2018
Abstract: © 2018 The Author(s). Multisite phosphorylation is a basic way of chemically encoding substrate function and a recurring feature of cell signalling pathways. A number of studies have explored information processing characteristics of multisite phosphorylation, through studies of the intrinsic kinetics. Many of these studies focus on the module in isolation. In this paper, we build a bridge to connect the behaviour of multisite modification in isolation to that as part of pathways. We study the effect of activation of the enzymes (which are basic ways in which the module may be regulated), as well the effects of the modified substrates being involved in further modifications or exiting reaction compartments. We find that these effects can induce multiple kinds of transitions, including to behaviour not seen intrinsically in the multisite modification module. We then build on these insights to investigate how these multisite modification systems can be tuned by enzyme activation to realize a range of information processing outcomes for the design of synthetic phosphorylation circuits. Connecting the complexity of multisite modification kinetics, with the pathways in which they are embedded, serves as a basis for teasing out many aspects of their interaction, providing insights of relevance in systems biology, synthetic biology/chemistry and chemical information processing.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85049640149&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/58341
ISSN: 17425662
17425689
Appears in Collections:CMUL: Journal Articles

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