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NIK-dependent p100 processing into p52 with RelB binding and IkBd degradation, mass action, SBML 2v4

ABSTRACT: This model represents NIK-dependent p100 processing into p52 followed by binding to RelB and NIK-dependent IkBd degradation. This model assesses the impact of substrate complex competition on RelB-p52.

SUBMITTER: Simon Mitchell

PROVIDER: BIOMD0000000871 | BioModels | 2024-09-02

REPOSITORIES: BioModels

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			Action	DRS
	BIOMD0000000871?filename=MA-p52-IkBd-Fig3B.xml	Xml
	BIOMD0000000871?filename=Simon2019_Figure3b.cps	Other
	BIOMD0000000871?filename=Simon2019_Figure3b.sedml	Other
	BIOMD0000000871?filename=Simon2019_Figure3b.xml	Xml

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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]

PMID: 31048505

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Simon2019 - NIK-dependent p100 processing into p52, Mass Action, SBML 2v4

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

2024-09-02 | BIOMD0000000868 | BioModels

Simon2019 - NIK-dependent p100 processing into p52 and IkBd degradation, mass action, SBML 2v4

Project description:This model represents NIK-dependent p100 processing into p52 and NIK-dependent IkBd degradation with mass action kinetics. Compare this mass action representation to the Michaelis-Menten model. In this model the dose-response to increasing p100 mRNA is not monotonic due to substrate complex competition.

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Project description: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.

2024-09-02 | BIOMD0000000866 | BioModels

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

Project description:This model represents NIK-dependent p100 processing into p52 and NIK-dependent IkBd degradation with Michaelis-Menten kinetics. Compare this Michaelis-Menten representation to the mass action model in which the dose-response to increasing p100 mRNA is no longer monotonic due to substrate complex competition.

2024-09-02 | BIOMD0000000869 | BioModels

NIK expression stimulated G6PD phosphorylation

Project description:Our findings establish NIK as a pivotal regulator of T cell metabolism in anti-tumor immunity and highlight a posttranslational mechanism of metabolic regulation involving the G6PD-NADPH redox system. CoIP assays revealed a strong physical interaction between NIK and G6PD in both T cells and transiently transfected 293 cells, suggesting G6PD to be a direct target of NIK. Using a phosphoprotein gel analysis approach, we demonstrated that NIK expression stimulated G6PD phosphorylation. To further study the mechanism, we performed mass spectrometry identify phosphorylation sites of G6PD stimulated by NIK

2020-10-05 | PXD020943 | Pride

Rhodococcus sp. p52

Project description:Rhodococcus sp. p52 Genome sequencing

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Comparasion between MCF7-NIK overexpressing cells, MCF7-control cells and MCF7-NIK depleted cells

Project description:Analysis of differentially expressed genes in MCF7 cancer cells transfected with an expression vector containing the ORF of NIK, a shRNA of NIK and a control shRNA. Transient transfections were performed in triplicates . We use micorarrays to elucidate the machanisms by which NIK regulates stem cells biology

2015-11-30 | GSE63382 | GEO

RNA-seq Analysis of Transcriptomes in β-Gal-overexpressing, NIK-overexpressing, and NIK(KA)-overexpressing αTC1-6 cells

Project description:Purpose: The goal of this study is to determine the molecular mechanisms involved in the NIK regulation of α cell function. Methods: mRNA profiles of β-Gal control, NIK, and NIK(KA) overexpressed αTC1-6 cells were generated by deep sequencing using an Illumina Hiseq platform. Paired-end clean reads were aligned to the mouse reference genome(Ensemble_GRCm38.89) with TopHat (version 2.0.12), and the aligned reads were used to quantify mRNA expression by using HTSeq-count (version 0.6.1). Conclusion: Our study represents the first detailed analysis of NIK-overexpressing aTC1-6 cell transcriptomes, generated by RNA-seq technology. Our results show that 328 genes were upregulated and 48 genes were downregulated following NIK overexpression. GO analysis indicated that the upregulated genes were primarily related to the immune response. KEGG pathway enrichment analysis showed that immune signaling pathways, including the TNF, NF-κB, and chemokine signaling pathways, were significantly activated by NIK overexpression in aTC1-6 cells, while genes related to metabolism-associated signal pathways were significantly decreased. NIK(KA), the dominant-negative mutant of NIK, does not affect gene expression in aTC1-6 cells.

2018-12-30 | GSE112511 | GEO

p52 transgenic expression with or without LPS in mouse lungs

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2017-11-22 | GSE71648 | GEO

NIK/NF-kappaB2 regulated gene products.

Project description:This study aims at identifying genes that are NIK/NF-kappaB2 responsive in murine dendritic cells matured in vivo. Keywords: NIK/NF-kappaB2 responsive genes in dendritic cells after TLR/CD40 signaling

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