Ubiquitination modification: critical regulation of IRF family stability and activity
- PMID: 33141302
- PMCID: PMC7607542
- DOI: 10.1007/s11427-020-1796-0
Ubiquitination modification: critical regulation of IRF family stability and activity
Abstract
Interferon regulatory factors (IRFs) play pivotal and critical roles in innate and adaptive immune responses; thus, precise and stringent regulation of the stability and activation of IRFs in physiological processes is necessary. The stability and activities of IRFs are directly or indirectly targeted by endogenous and exogenous proteins in an ubiquitin-dependent manner. However, few reviews have summarized how host E3 ligases/DUBs or viral proteins regulate IRF stability and activity. Additionally, with recent technological developments, details about the ubiquitination of IRFs have been continuously revealed. As knowledge of how these proteins function and interact with IRFs may facilitate a better understanding of the regulation of IRFs in immune responses or other biological processes, we summarized current studies on the direct ubiquitination of IRFs, with an emphasis on how these proteins interact with IRFs and affect their activities, which may provide exciting targets for drug development by regulating the functions of specific E3 ligases.
Keywords: E3 ubiquitin ligase; IRFs; activation; degradation; ubiquitination; viral proteins.
Similar articles
-
Targeting IRFs by ubiquitination: regulating antiviral responses.Biochem Soc Trans. 2008 Jun;36(Pt 3):453-8. doi: 10.1042/BST0360453. Biochem Soc Trans. 2008. PMID: 18481980 Review.
-
The E3 Ubiquitin Ligase TBK1 Mediates the Degradation of Multiple Picornavirus VP3 Proteins by Phosphorylation and Ubiquitination.J Virol. 2019 Nov 13;93(23):e01438-19. doi: 10.1128/JVI.01438-19. Print 2019 Dec 1. J Virol. 2019. PMID: 31534043 Free PMC article.
-
Molecular and physiological roles of Pellino E3 ubiquitin ligases in immunity.Immunol Rev. 2015 Jul;266(1):93-108. doi: 10.1111/imr.12306. Immunol Rev. 2015. PMID: 26085209 Review.
-
Newcastle Disease Virus V Protein Degrades Mitochondrial Antiviral Signaling Protein To Inhibit Host Type I Interferon Production via E3 Ubiquitin Ligase RNF5.J Virol. 2019 Aug 28;93(18):e00322-19. doi: 10.1128/JVI.00322-19. Print 2019 Sep 15. J Virol. 2019. PMID: 31270229 Free PMC article.
-
Nonproteolytic K29-Linked Ubiquitination of the PB2 Replication Protein of Influenza A Viruses by Proviral Cullin 4-Based E3 Ligases.mBio. 2020 Apr 7;11(2):e00305-20. doi: 10.1128/mBio.00305-20. mBio. 2020. PMID: 32265326 Free PMC article.
Cited by
-
Targeting the ubiquitin-proteasome system: a novel therapeutic strategy for neuroblastoma.Front Oncol. 2024 Sep 26;14:1443256. doi: 10.3389/fonc.2024.1443256. eCollection 2024. Front Oncol. 2024. PMID: 39391247 Free PMC article. Review.
-
The Roles of Ubiquitination in Pathogenesis of Influenza Virus Infection.Int J Mol Sci. 2022 Apr 21;23(9):4593. doi: 10.3390/ijms23094593. Int J Mol Sci. 2022. PMID: 35562987 Free PMC article. Review.
-
The multiple roles of interferon regulatory factor family in health and disease.Signal Transduct Target Ther. 2024 Oct 9;9(1):282. doi: 10.1038/s41392-024-01980-4. Signal Transduct Target Ther. 2024. PMID: 39384770 Free PMC article. Review.
-
IRF4 Participates in Pulmonary Fibrosis Induced by Silica Particles through Regulating Macrophage Polarization and Fibroblast Activation.Inflammation. 2024 Feb;47(1):45-59. doi: 10.1007/s10753-023-01890-7. Epub 2023 Nov 8. Inflammation. 2024. PMID: 37938462
-
[Regulatory mechanism of interferon regulatory factor 1 by α-synuclein in mouse Parkinson's disease model].Nan Fang Yi Ke Da Xue Xue Bao. 2021 Nov 20;41(11):1641-1648. doi: 10.12122/j.issn.1673-4254.2021.11.07. Nan Fang Yi Ke Da Xue Xue Bao. 2021. PMID: 34916189 Free PMC article. Chinese.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials