Identification of new IκBα complexes by an iterative experimental and mathematical modeling approach.

The transcription factor nuclear factor kappa-B (NFκB) is a key regulator of pro-inflammatory and pro-proliferative processes. Accordingly, uncontrolled NFκB activity may contribute to the development of severe diseases when the regulatory system is impaired. Since NFκB can be triggered by a huge va...

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Main Authors: Fabian Konrath, Johannes Witt, Thomas Sauter, Dagmar Kulms
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-03-01
Series:PLoS Computational Biology
Online Access:https://journals.plos.org/ploscompbiol/article/file?id=10.1371/journal.pcbi.1003528&type=printable
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author Fabian Konrath
Johannes Witt
Thomas Sauter
Dagmar Kulms
author_facet Fabian Konrath
Johannes Witt
Thomas Sauter
Dagmar Kulms
author_sort Fabian Konrath
collection DOAJ
description The transcription factor nuclear factor kappa-B (NFκB) is a key regulator of pro-inflammatory and pro-proliferative processes. Accordingly, uncontrolled NFκB activity may contribute to the development of severe diseases when the regulatory system is impaired. Since NFκB can be triggered by a huge variety of inflammatory, pro-and anti-apoptotic stimuli, its activation underlies a complex and tightly regulated signaling network that also includes multi-layered negative feedback mechanisms. Detailed understanding of this complex signaling network is mandatory to identify sensitive parameters that may serve as targets for therapeutic interventions. While many details about canonical and non-canonical NFκB activation have been investigated, less is known about cellular IκBα pools that may tune the cellular NFκB levels. IκBα has so far exclusively been described to exist in two different forms within the cell: stably bound to NFκB or, very transiently, as unbound protein. We created a detailed mathematical model to quantitatively capture and analyze the time-resolved network behavior. By iterative refinement with numerous biological experiments, we yielded a highly identifiable model with superior predictive power which led to the hypothesis of an NFκB-lacking IκBα complex that contains stabilizing IKK subunits. We provide evidence that other but canonical pathways exist that may affect the cellular IκBα status. This additional IκBα:IKKγ complex revealed may serve as storage for the inhibitor to antagonize undesired NFκB activation under physiological and pathophysiological conditions.
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spelling doaj-art-dc042349a89c4c7887cbf6fdb2b89a8b2025-08-20T02:15:20ZengPublic Library of Science (PLoS)PLoS Computational Biology1553-734X1553-73582014-03-01103e100352810.1371/journal.pcbi.1003528Identification of new IκBα complexes by an iterative experimental and mathematical modeling approach.Fabian KonrathJohannes WittThomas SauterDagmar KulmsThe transcription factor nuclear factor kappa-B (NFκB) is a key regulator of pro-inflammatory and pro-proliferative processes. Accordingly, uncontrolled NFκB activity may contribute to the development of severe diseases when the regulatory system is impaired. Since NFκB can be triggered by a huge variety of inflammatory, pro-and anti-apoptotic stimuli, its activation underlies a complex and tightly regulated signaling network that also includes multi-layered negative feedback mechanisms. Detailed understanding of this complex signaling network is mandatory to identify sensitive parameters that may serve as targets for therapeutic interventions. While many details about canonical and non-canonical NFκB activation have been investigated, less is known about cellular IκBα pools that may tune the cellular NFκB levels. IκBα has so far exclusively been described to exist in two different forms within the cell: stably bound to NFκB or, very transiently, as unbound protein. We created a detailed mathematical model to quantitatively capture and analyze the time-resolved network behavior. By iterative refinement with numerous biological experiments, we yielded a highly identifiable model with superior predictive power which led to the hypothesis of an NFκB-lacking IκBα complex that contains stabilizing IKK subunits. We provide evidence that other but canonical pathways exist that may affect the cellular IκBα status. This additional IκBα:IKKγ complex revealed may serve as storage for the inhibitor to antagonize undesired NFκB activation under physiological and pathophysiological conditions.https://journals.plos.org/ploscompbiol/article/file?id=10.1371/journal.pcbi.1003528&type=printable
spellingShingle Fabian Konrath
Johannes Witt
Thomas Sauter
Dagmar Kulms
Identification of new IκBα complexes by an iterative experimental and mathematical modeling approach.
PLoS Computational Biology
title Identification of new IκBα complexes by an iterative experimental and mathematical modeling approach.
title_full Identification of new IκBα complexes by an iterative experimental and mathematical modeling approach.
title_fullStr Identification of new IκBα complexes by an iterative experimental and mathematical modeling approach.
title_full_unstemmed Identification of new IκBα complexes by an iterative experimental and mathematical modeling approach.
title_short Identification of new IκBα complexes by an iterative experimental and mathematical modeling approach.
title_sort identification of new iκbα complexes by an iterative experimental and mathematical modeling approach
url https://journals.plos.org/ploscompbiol/article/file?id=10.1371/journal.pcbi.1003528&type=printable
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AT thomassauter identificationofnewikbacomplexesbyaniterativeexperimentalandmathematicalmodelingapproach
AT dagmarkulms identificationofnewikbacomplexesbyaniterativeexperimentalandmathematicalmodelingapproach