Signaling cascades: consequences of varying substrate and phosphatase levels

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 -