Ubiquitin in the immune system

Abstract

Ubiquitination is a post-translational modification process that has been implicated in the regulation of innate and adaptive immune responses. There is increasing evidence that both ubiquitination and its reversal, deubiquitination, play crucial roles not only during the development of the immune system but also in the orchestration of an immune response by ensuring the proper functioning of the different cell types that constitute the immune system. Here, we provide an overview of the latest discoveries in this field and discuss how they impact our understanding of the ubiquitin system in host defence mechanisms as well as self-tolerance.

Cited by papers we hold 9

• The PB1 protein of influenza A virus inhibits the innate immune response by targeting MAVS for NBR1-mediated selective autophagic degradation · 2021
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• E3 ubiquitin ligases: styles, structures and functions · 2021
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• Ubiquitin-Mediated Regulation of RIPK1 Kinase Activity Independent of IKK and MK2 · 2018
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• TRIM25 in the Regulation of the Antiviral Innate Immunity · 2017
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• E3 ubiquitin ligase Nedd4 inhibits AP-1 activity and TNF-α production through targeting p38α for polyubiquitination and subsequent degradation · 2017
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• SPATA2-Mediated Binding of CYLD to HOIP Enables CYLD Recruitment to Signaling Complexes · 2016
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• Poly-ubiquitination in TNFR1-mediated necroptosis · 2016
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• Linear ubiquitination is involved in the pathogenesis of optineurin-associated amyotrophic lateral sclerosis · 2016
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• Linear ubiquitination in immunity · 2015
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