Selectivity in overlapping MAP kinase cascades
Date
2002
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Abstract
Some protein kinases operate in more than one mitogen-activated protein-kinase (MAPK) cascade. We here address the question whether specificity of the cascades necessitates physical sequestration of these "promiscuous" kinases (e.g. by binding to scaffolds). A model is constructed, in which two MAPK cascades depend on a single MAP-kinase kinase that is not sequestered in two subpopulations. We show that in this model selective signal transduction is possible provided that there is an additional interaction at the MAP-kinase level, there is no simultaneous activation of more than one response by either signal. We discuss a number of additional interactions that can generate the selectivity, as well as some kinetic features by which this mechanism may be recognized experimentally. © 2002 Elsevier Science Ltd. All rights reserved.
Description
Keywords
mitogen activated protein kinase, mitogen activated protein kinase kinase, mitogen activated protein kinase kinase kinase, enzyme, article, enzyme activation, enzyme activity, enzyme mechanism, enzyme phosphorylation, enzyme specificity, Michaelis constant, model, priority journal, signal transduction, Adaptation, Physiological, Animals, Enzyme Activation, MAP Kinase Signaling System, Mitogen-Activated Protein Kinase Kinases, Mitogen-Activated Protein Kinases, Models, Chemical
Citation
Journal of Theoretical Biology
218
3
218
3