Deubiquitination and stabilization of IL-33 by USP21.
Year: 2014
Type: article
Abstract: Interleukin-33 (IL-33) is a dual-function protein that acts both as a secreted cytokine and as a nuclear factor regulating gene transcription. It has been demonstrated that IL-33 exerts its nuclear function in promoting the transcription of NF-κB p65. Here, we show that USP21-mediated deubiquitination of IL-33 affects the transcription of p65. IL-33 can be post-translationally modified by ubiquitination. Ubiquitin-specific protease 21 (USP21) interacts with IL-33 and also localizes in nucleus. The protein stability of IL-33 is maintained by USP21 through deubiquitination. Furthermore, depletion of USP21 reduces IL-33 protein levels and IL-33-mediated NF-κB p65 promoter activity. Our findings reveal the role of ubiquitination modification in regulating the protein stability and the nuclear function of IL-33.
Source: Europe PMC (PubMed Central)
Language: English
Topic: IL-33, ST2, and ILC Pathways
Subfield: Immunology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W1419940491