journal article·2020-11Open access

Inflammatory Response: USP38 Couples Histone Ubiquitination and Methylation via KDM5B to Resolve Inflammation (Adv. Sci. 22/2020)

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

Advanced Science· Volume 7· Issue 22

Abstract

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. [Image: see text]
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Research context

OpenAlex topics: Ferroptosis and cancer prognosis · Circular RNAs in diseases

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