ArticleThe Journal of biological chemistry2013
IκB kinase β (IKKβ) inhibits p63 isoform γ (TAp63γ) transcriptional activity.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Sustained activation of NF-κB through constitutively active IKKβ leads to senescence bypass in murine dermal fibroblasts.Cell cycle (Georgetown, Tex.) · 2024Article
- Pin1 and JNK1 cooperatively modulate TAp63γ.FEBS open bio · 2021Article
- Review
- Inhibition of tumor suppressor p73 by nerve growth factor receptor via chaperone-mediated autophagy.Journal of molecular cell biology · 2020Article
- A Novel Hydroxamate-Based Compound WMJ-J-09 Causes Head and Neck Squamous Cell Carcinoma Cell Death via LKB1-AMPK-p38MAPK-p63-Survivin Cascade.Frontiers in pharmacology · 2018Article
- Context-Dependent Role of IKKβ in Cancer.Genes · 2017Review
- Ccdc3: A New P63 Target Involved in Regulation Of Liver Lipid Metabolism.Scientific reports · 2017Article
- Hepatic p63 regulates steatosis via IKKβ/ER stress.Nature communications · 2017Article
- TFIIS.h, a new target of p53, regulates transcription efficiency of pro-apoptotic bax gene.Scientific reports · 2016Article
- Bioinformatics study of cancer-related mutations within p53 phosphorylation site motifs.International journal of molecular sciences · 2014Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Previously, we reported that IκB kinase-β(IKKβ) phosphorylates and stabilizes TAp63γ. However, the effect of this phosphorylation on TAp63γ transcriptional activity remains unclear. In this study, we showed that overexpression of IKKβ, but not its kinase dead mutant and IKKα, can surprisingly inhibit TAp63γ transcriptional activity as measured by luciferase assays and real-time PCR analyses of p63 target genes. This inhibition was impaired by ACHP, an IKKβ inhibitor, and enhanced by TNFα that activates IKKβ. Consistently, IKKβ inhibited the binding between TAp63γ and p300, a co-activator of TAp63γ, and consequently counteracted the positive effect of p300 on TAp63γ transcriptional activity. Through phosphorylation site prediction and mass spectrometry, we identified that Ser-4 and Ser-12 of p63 are IKKβ-targeting residues. As expected, IKKβ fails to suppress the transcriptional activity of the S4A/S12A double mutant p63. These results indicate that IKKβ can suppress TAp63γ activity by interfering with the interaction between TAp63γ and p300.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.