Markevich2004_MAPK_orderedElementary
Ontology highlight
ABSTRACT:
SUBMITTER: 
Nicolas Le Novère
PROVIDER: BIOMD0000000026 | BioModels | 2005-05-23
REPOSITORIES: BioModels
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]
Similar Datasets
Project description:The model corresponds to the schema 3 of Markevich et al 2004, as described in the figure 2 and the supplementary table S2. Phosphorylations follow distributive random kinetics, while dephosphorylations follow an ordered mechanism. The phosphorylations are modeled with three elementary reactions:
E+SES->E+P
The dephosphorylations are modeled with five elementary reactions:
E+SES->EPE+P
The model reproduces figure 5 in the main article.
The model is further described in:
Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades.
Markevich NI, Hoek JB, Kholodenko BN. J Cell Biol. 2004 Feb 2;164(3):353-9.
PMID: 14744999
; DOI: 10.1083/jcb.200308060
Abstract:
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 reported kinetic properties of the kinase (MEK) and phosphatase (MKP3) of extracellular signal-regulated kinase (ERK) fulfill the essential requirements for generating a bistable switch at a single MAPK cascade level. Likewise, a cycle where multisite phosphorylations are performed by different kinases, but dephosphorylation reactions are catalyzed by the same phosphatase, can also exhibit bistability and hysteresis. Hence, bistability induced by multisite covalent modification may be a widespread mechanism of the control of protein activity.
This model originates from BioModels Database: A Database of Annotated Published Models (http://www.ebi.ac.uk/biomodels/). It is copyright (c) 2005-2010 The BioModels.net Team.
For more information see the terms of use
.
To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.
2005-05-23 | BIOMD0000000028 | BioModels
Project description:The model corresponds to the schema 3 of Markevich et al 2004, as described in the figure 2 and the supplementary table S3, and modelled using Michaelis-Menten like kinetics. Phosphorylations follow distributive random kinetics, while dephosphorylations follow an ordered mechanism.
This model originates from BioModels Database: A Database of Annotated Published Models. It is copyright (c) 2005-2007 The BioModels Team.
For more information see the terms of use
.
2005-05-24 | BIOMD0000000029 | BioModels
Project description:Markevich2004 - MAPK double phosphorylation,
ordered Michaelis-Menton
The model corresponds to the schemas 1
and 2 of Markevich et al 2004, as described in the figure 1 and
modelled using Michaelis-Menten like kinetics. Phosphorylations and
dephosphorylations follow distributive ordered kinetics. It
reproduces figure 3 of the main article.
This model is described in the article:
Signaling switches and
bistability arising from multisite phosphorylation in protein
kinase cascades.
Markevich NI, Hoek JB, Kholodenko
BN.
J. Cell Biol. 2004 Feb; 164(3):
353-359
Abstract:
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 reported kinetic properties of the kinase
(MEK) and phosphatase (MKP3) of extracellular signal-regulated
kinase (ERK) fulfill the essential requirements for generating
a bistable switch at a single MAPK cascade level. Likewise, a
cycle where multisite phosphorylations are performed by
different kinases, but dephosphorylation reactions are
catalyzed by the same phosphatase, can also exhibit bistability
and hysteresis. Hence, bistability induced by multisite
covalent modification may be a widespread mechanism of the
control of protein activity.
This model is hosted on
BioModels Database
and identified by:
BIOMD0000000027.
To cite BioModels Database, please use:
BioModels Database:
An enhanced, curated and annotated resource for published
quantitative kinetic models.
To the extent possible under law, all copyright and related or
neighbouring rights to this encoded model have been dedicated to
the public domain worldwide. Please refer to
CC0
Public Domain Dedication for more information.
2005-05-23 | BIOMD0000000027 | BioModels
Project description:The model describes the double phosphorylation of MAP kinase by an ordered mechanism using the Michaelis-Menten formalism. Two different enzymes, MAPKK1 and MAPKK2, successively phosphorylate the MAP kinase, but one and the same phosphatase dephosphorylates both sites.
The model reproduces figure S9
in the supplemental material of the article.
The model is further described in:
Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades.
Markevich NI, Hoek JB, Kholodenko BN. J Cell Biol. 2004 Feb 2;164(3):353-9.
PMID: 14744999
; DOI: 10.1083/jcb.200308060
Abstract:
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 reported kinetic properties of the kinase (MEK) and phosphatase (MKP3) of extracellular signal-regulated kinase (ERK) fulfill the essential requirements for generating a bistable switch at a single MAPK cascade level. Likewise, a cycle where multisite phosphorylations are performed by different kinases, but dephosphorylation reactions are catalyzed by the same phosphatase, can also exhibit bistability and hysteresis. Hence, bistability induced by multisite covalent modification may be a widespread mechanism of the control of protein activity.
This model originates from BioModels Database: A Database of Annotated Published Models (http://www.ebi.ac.uk/biomodels/). It is copyright (c) 2005-2010 The BioModels.net Team.
For more information see the terms of use
.
To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.
2005-06-30 | BIOMD0000000031 | BioModels
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