Journal
SCIENCE CHINA-LIFE SCIENCES
Volume 64, Issue 6, Pages 957-965Publisher
SCIENCE PRESS
DOI: 10.1007/s11427-020-1796-0
Keywords
IRFs; ubiquitination; E3 ubiquitin ligase; viral proteins; activation; degradation
Categories
Funding
- National Key Research and Development Program of China [2018YFA0800503, 2018YFD0500100]
- excellent young scientist foundation of NSFC [31822017]
- Zhejiang Provincial Natural Science Foundation of China [LR19C080001]
- National Natural Science Foundation of China [81572651, 81771675]
- Fundamental Research Funds for the Central Universities
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IRFs play critical roles in immune responses, with their stability and activities regulated by ubiquitination of endogenous and exogenous proteins. Understanding how these proteins interact with IRFs may provide potential targets for drug development.
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.
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