4.7 Article

PSMD13 inhibits NF-κB pathway by targeting TAK1 for K63-linked ubiquitination in miiuy croaker (Miichthys miiuy)

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FISH & SHELLFISH IMMUNOLOGY
卷 138, 期 -, 页码 -

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ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.fsi.2023.108857

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Innate immune; TAK1; PSMD13; Ubiquitination

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PSMD13 inhibits the activation of the NF-κB pathway by targeting TAK1 in mammalian innate immune regulation. This discovery enriches the research of the PSMD family in regulating the innate immune response and provides a new idea for studying the mechanism of mammalian innate immune regulation.
Transforming growth factor-& beta; activated kinase 1 (TAK1) is an adaptor molecular in the TLR-mediated NF-& kappa;B pathway which has been implicated in the regulation of a wide range of physiological and pathological processes. Proteasome 26S subunit, non-ATPase (PSMD) 13 is essential for the structural maintenance and function of the 26S proteasome. However, the mechanism of PSMD13 in innate immune regulation is not clear. In this study, the expression of PSMD13 mRNA was significantly increased under Vibrio harveyi stimulation, and PSMD13 inhibited the NF-& kappa;B pathway by targeting TAK1. Mechanically, PSMD13 significantly inhibited the K63-linked ubiquiti-nation of TAK1, thereby inhibiting the expression of TAK1. Moreover, this discovery enriches the research of the PSMD family in regulating the innate immune response and provides a new idea for the study of the mammalian innate immune regulation mechanism.

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