ArticleEMBO reports2021
Dynamic chromatin association of IκBα is regulated by acetylation and cleavage of histone H4.
Article in EMBO reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
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- Analogue information processing in NF-κB gene regulatory system.Royal Society open science · 2025Article
- Trp53 Deletion Promotes Exacerbated Colitis, Facilitates Lgr5+ Cancer Stem Cell Expansion, and Fuels Tumorigenesis in AOM/DSS-Induced Colorectal Cancer.International journal of molecular sciences · 2024Article
- Histone Tail Cleavage as a Mechanism for Epigenetic Regulation.International journal of molecular sciences · 2024Review
- IκBα controls dormancy in hematopoietic stem cells via retinoic acid during embryonic development.Nature communications · 2024Article
- Histone acylations as a mechanism for regulation of intestinal epithelial cells.Digestive medicine research · 2024Article
- Haploinsufficiency of NFKBIA reshapes the epigenome antipodal to the IDH mutation and imparts disease fate in diffuse gliomas.Cell reports. Medicine · 2023Article
- Long non-coding RNA ZFY-AS1 represses periodontitis tissue inflammation and oxidative damage via modulating microRNA-129-5p/DEAD-Box helicase 3 X-linked axis.Bioengineered · 2022Article
- GLP-1 Mediates Regulation of Colonic ACE2 Expression by the Bile Acid Receptor GPBAR1 in Inflammation.Cells · 2022Article
- NF-κB-Dependent and -Independent (Moonlighting) IκBα Functions in Differentiation and Cancer.Biomedicines · 2021Review
- Dynamic chromatin association of IκBα is regulated by acetylation and cleavage of histone H4.EMBO reports · 2021Article
- Histone clipping: the punctuation in the histone code.EMBO reports · 2021Article
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15 authors at 4 institutions in 2 countries.
Funding
Abstract
IκBs exert principal functions as cytoplasmic inhibitors of NF-kB transcription factors. Additional roles for IκB homologues have been described, including chromatin association and transcriptional regulation. Phosphorylated and SUMOylated IκBα (pS-IκBα) binds to histones H2A and H4 in the stem cell and progenitor cell compartment of skin and intestine, but the mechanisms controlling its recruitment to chromatin are largely unknown. Here, we show that serine 32-36 phosphorylation of IκBα favors its binding to nucleosomes and demonstrate that p-IκBα association with H4 depends on the acetylation of specific H4 lysine residues. The N-terminal tail of H4 is removed during intestinal cell differentiation by proteolytic cleavage by trypsin or chymotrypsin at residues 17-19, which reduces p-IκBα binding. Inhibition of trypsin and chymotrypsin activity in HT29 cells increases p-IκBα chromatin binding but, paradoxically, impaired goblet cell differentiation, comparable to IκBα deletion. Taken together, our results indicate that dynamic binding of IκBα to chromatin is a requirement for intestinal cell differentiation and provide a molecular basis for the understanding of the restricted nuclear distribution of p-IκBα in specific stem cell compartments.
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