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Usp21 deubiquitinase regulates aim2 inflammasome activation

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Title
Usp21 deubiquitinase regulates aim2 inflammasome activation
Author(s)
Yujin Hong; Seong-Ok Lee; Changhoon Oh; Kang, Kwonyoon; Ryoo, Jeongmin; Dongyoung Kim; Kwangseog Ahn
Publication Date
2021-10-01
Journal
Journal of Immunology, v.207, no.7, pp.1926 - 1936
Publisher
American Association of Immunologists
Abstract
© 2021 by TheAmericanAssociation of Immunologists, Inc.Innate immune sensing of cytosolic DNA via absent in melanoma 2 (AIM2) is a key mechanism leading to inflammatory responses. As aberrant immune responses by dysregulated AIM2 are associated with autoinflammatory diseases, activation of the AIM2 inflammasome should be tightly controlled. In this study, we discovered that ubiquitination and deubiquitination of AIM2 are critical events that regulate AIM2 inflammasome activation. In resting human macrophage cells, AIM2 is constitutively ubiquitinated and undergoes proteasomal degradation to avoid autoinflammation. Upon DNA stimulation, USP21 binds to AIM2 and deubiquitinates it, thereby increasing its protein stability. In addition to the role of USP21 in regulating AIM2 turnover, we uncovered that USP21-mediated deubiquitination of AIM2 is required for the assembly of the AIM2 inflammasome. Depletion of USP21 does not affect the DNA-binding ability of AIM2 but inhibits the formation of the AIM2-ASC complex. Our findings establish that fine-tuning of AIM2 by the ubiquitin system is important for regulating AIM2 inflammasome activation.
URI
https://pr.ibs.re.kr/handle/8788114/10364
DOI
10.4049/jimmunol.2100449
ISSN
0022-1767
Appears in Collections:
Center for RNA Research(RNA 연구단) > 1. Journal Papers (저널논문)
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