TY - JOUR
T1 - Signaling cascades
T2 - consequences of varying substrate and phosphatase levels
AU - Feliu, Elisenda
AU - Knudsen, Michael
AU - Wiuf, Carsten
PY - 2012
Y1 - 2012
N2 - 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.
AB - 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.
U2 - 10.1007/978-1-4419-7210-1_4
DO - 10.1007/978-1-4419-7210-1_4
M3 - Journal article
C2 - 22161323
SN - 0065-2598
VL - 736
SP - 81
EP - 94
JO - Advances in Experimental Medicine and Biology
JF - Advances in Experimental Medicine and Biology
ER -