Open AccessInflammatory Response: USP38 Couples Histone Ubiquitination and Methylation via KDM5B to Resolve Inflammation (Adv. Sci. 22/2020)
Author(s) -
Zhao Zhiyao,
Su Zexiong,
Liang Puping,
Liu Di,
Yang Shuai,
Wu Yaoxing,
Ma Ling,
Feng Junyan,
Zhang Xiya,
Wu Chenglei,
Huang Junjiu,
Cui Jun
Publication year - 2020
Publication title -
advanced science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.388
H-Index - 100
ISSN - 2198-3844
DOI - 10.1002/advs.202070122
Subject(s) - histone , ubiquitin , methylation , histone methylation , epigenetics , inflammation , histone methyltransferase , microbiology and biotechnology , chemistry , cancer research , biology , dna methylation , gene , gene expression , biochemistry , immunology
In article number 2002680, Jun Cui and co‐workers identify a new histone modifier‐USP38, that modulates histone ubiquitination and methylation to resolve inflammatory response. USP38 acts as a “Safety Machine” which shuts down the inflammation by de‐ubiquitinating histone H2B and stabilizes KDM5B to de‐methylate H3K4, which blocks the transcription of pro‐inflammatory genes. The USP38‐KDM5B complex might be a potential clinical target for therapy against inflammatory diseases.