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Simon2019 - NIK-dependent p100 processing into p52, Michaelis-Menten, SBML 2v4

ABSTRACT: This model represents NIK-dependent p100 processing into p52 with Michaelis-Menten kinetics. While this model shows identical dose-response to the mass action representation, when IkBd degradation is included the dose-response is no-longer monotonic in mass action models due to substrate complex competition.

SUBMITTER: Simon Mitchell  

PROVIDER: BIOMD0000000866 | BioModels | 2024-09-02

REPOSITORIES: BioModels

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BIOMD0000000866?filename=MM-p52-biopax2.owl Owl
BIOMD0000000866?filename=MM-p52-biopax3.owl Owl
BIOMD0000000866?filename=MM-p52.xml Xml
BIOMD0000000866?filename=Simon2019-biopax2.owl Owl
BIOMD0000000866?filename=Simon2019-biopax3.owl Owl
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Publications

Substrate complex competition is a regulatory motif that allows NFκB RelA to license but not amplify NFκB RelB.

Mitchell Simon S   Hoffmann Alexander A  

Proceedings of the National Academy of Sciences of the United States of America 20190502 21

Signaling pathways often share molecular components, tying the activity of one pathway to the functioning of another. In the NFκB signaling system, distinct kinases mediate inflammatory and developmental signaling via RelA and RelB, respectively. Although the substrates of the developmental, so-called noncanonical, pathway are induced by inflammatory/canonical signaling, crosstalk is limited. Through dynamical systems modeling, we identified the underlying regulatory mechanism. We found that as  ...[more]

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