title: Signaling cascades: consequences of varying substrate and phosphatase levels.
abstract: We study signaling cascades with an arbitrary number of layers of one-site phosphorylation cycles. Such cascades are abundant in nature and integrated parts of many pathways. Based on the Michaelis-Menten model of enzyme kinetics and the law of mass-action, we derive explicit analytic expressions for how the steady state concentrations and the total amounts of substrates, kinase, and phosphatates depend on each other. In particular, we use these to study how the responses (the activated substrates) vary as a function of the available amounts of substrates, kinase, and phosphatases. Our results provide insight into how the cascade response is affected by crosstalk and external regulation.
authors.affiliation: Bioinformatics Research Centre, Aarhus University, Aarhus, Denmark. efeliu@birc.au.dk
authors.forename: Elisenda
authors.initials: E
authors.lastname: Feliu
authors.forename: Michael
authors.initials: M
authors.lastname: Knudsen
authors.forename: Carsten
authors.initials: C
authors.lastname: Wiuf
mesh_terms: D000465:Algorithms; D000818:Animals; D003198:Computer Simulation; D006801:Humans; D007700:Kinetics; D008954:Models, Biological; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D015398:Signal Transduction; D013379:Substrate Specificity
chemical_list: D011494:Protein Kinases; D010744:Phosphoric Monoester Hydrolases