Deubiquitination and stabilization of IL-33 by USP21.

Deubiquitination and stabilization of IL-33 by USP21.
Int J Clin Exp Pathol. 2014;7(8):4930-7
Authors: Tao L, Chen C, Song H, Piccioni M, Shi G, Li B
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.
PMID: 25197364 [PubMed - in process]

Source: International Journal of Clinical and Experimental Pathology - September 15, 2014 Category: Pathology Authors: Tao L, Chen C, Song H, Piccioni M, Shi G, Li B Tags: Int J Clin Exp Pathol Source Type: research