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Markevich2004_MAPK_orderedElementary


ABSTRACT: The model corresponds to the schemas 1 and 2 of Markevich et al 2004, as described in the figure 1 and the supplementary table S1. Phosphorylations and dephosphorylations follow distributive ordered kinetics. The phosphorylations are modeled with three elementary reactions: E+SES->E+P The dephosphorylations are modeled with five elementary reactions: E+SES->EPE+P

REANALYSED by: BIOMD0000000223

SUBMITTER: Nicolas Le Novère  

PROVIDER: BIOMD0000000026 | BioModels | 2005-05-23

REPOSITORIES: BioModels

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Publications

Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades.

Markevich Nick I NI   Hoek Jan B JB   Kholodenko Boris N BN  

The Journal of cell biology 20040126 3


Mitogen-activated protein kinase (MAPK) cascades can operate as bistable switches residing in either of two different stable states. MAPK cascades are often embedded in positive feedback loops, which are considered to be a prerequisite for bistable behavior. Here we demonstrate that in the absence of any imposed feedback regulation, bistability and hysteresis can arise solely from a distributive kinetic mechanism of the two-site MAPK phosphorylation and dephosphorylation. Importantly, the report  ...[more]

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