USP38 Couples Histone Ubiquitination and Methylation via KDM5B to Resolve Inflammation

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Abstract: Chromatin modifications, such as histone acetylation, ubiquitination, and methylation, play fundamental roles in maintaining chromatin architecture and regulating gene transcription. Although their crosstalk in chromatin remodeling has been gradually uncovered, the functional relationship between histone ubiquitination and methylation in regulating immunity and inflammation remains unclear. Here, it is reported that USP38 is a novel histone deubiquitinase that works together with the histone H3K4 modifier KDM5B to orchestrate inflammatory responses. USP38 specifically removes the monoubiquitin on H2B at lysine 120, which functions as a prerequisite for the subsequent recruitment of demethylase KDM5B to the promoters of proinflammatory cytokines Il6 and Il23a during LPS stimulation. KDM5B in turn inhibits the binding of NF‐κB transcription factors to the Il6 and Il23a promoters by reducing H3K4 trimethylation. Furthermore, USP38 can bind to KDM5B and prevent it from proteasomal degradation, which further enhances the function of KDM5B in the regulation of inflammation‐related genes. Loss of Usp38 in mice markedly enhances susceptibility to endotoxin shock and acute colitis, and these mice display a more severe inflammatory phenotype compared to wild‐type mice. The studies identify USP38‐KDM5B as a distinct chromatin modification complex that restrains inflammatory responses through manipulating the crosstalk of histone ubiquitination and methylation.

Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: USP38 Couples Histone Ubiquitination and Methylation via KDM5B to Resolve Inflammation ; volume:7 ; number:22 ; year:2020 ; extent:14
Advanced science ; 7, Heft 22 (2020) (gesamt 14)

Creator: Zhao, Zhiyao
Su, Zexiong
Liang, Puping
Liu, Di
Yang, Shuai
Wu, Yaoxing
Ma, Ling
Feng, Junyan
Zhang, Xiya
Wu, Chenglei
Huang, Junjiu
Cui, Jun

DOI: 10.1002/advs.202002680

URN: urn:nbn:de:101:1-2022052707225652769585

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:30 AM CEST

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Associated

Zhao, Zhiyao
Su, Zexiong
Liang, Puping
Liu, Di
Yang, Shuai
Wu, Yaoxing
Ma, Ling
Feng, Junyan
Zhang, Xiya
Wu, Chenglei
Huang, Junjiu
Cui, Jun

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