Fine-tuning of antiviral innate immunity by ubiquitination

Adv Immunol. 2020:145:95-128. doi: 10.1016/bs.ai.2019.11.004. Epub 2019 Dec 9.

Abstract

The innate immune system represents the first defense line of the host following viral infection. The infection triggers the recognition of pathogen-associated molecular patterns (PAMPs) from the viruses by pattern recognition receptors (PRRs) of the host cell. The interaction between viral PAMPs and PRRs evokes a sophisticated signal transduction system and eventually promotes the expression of type I interferons (IFNs) and proinflammatory cytokines. Ubiquitination plays an indispensable role in fine-tuning almost every single step of this signaling cascade given on its versatile functions. Ubiquitin ligases and deubiquitinases (DUBs), which cooperatively and accurately regulate the dynamic and reversible ubiquitination process, are the master regulators of antiviral signaling. In this review, we concentrate on summarizing the ubiquitin ligases and DUBs that modulate the central signaling molecules in antiviral innate immunity. Especially, we emphasize the ones that were identified by the immunologists from China.

Keywords: Antiviral innate immunity; Deubiquitinase; E3 ubiquitin ligase; Signaling transduction; Ubiquitination.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cytokines / metabolism
  • Deubiquitinating Enzymes / metabolism
  • Humans
  • Immunity, Innate*
  • Interferon Type I / metabolism
  • Membrane Proteins / metabolism
  • Nucleotidyltransferases / metabolism
  • Receptors, Pattern Recognition / metabolism*
  • Signal Transduction / genetics
  • Signal Transduction / immunology*
  • Toll-Like Receptors / metabolism
  • Ubiquitin-Protein Ligases / metabolism
  • Ubiquitination / genetics
  • Ubiquitination / immunology*
  • Virus Diseases / immunology*

Substances

  • Cytokines
  • Interferon Type I
  • Membrane Proteins
  • Receptors, Pattern Recognition
  • STING1 protein, human
  • Toll-Like Receptors
  • Ubiquitin-Protein Ligases
  • Nucleotidyltransferases
  • cGAS protein, human
  • Deubiquitinating Enzymes