Recent developments in understanding RIG-I's activation and oligomerization

Sci Prog. 2024 Jul-Sep;107(3):368504241265182. doi: 10.1177/00368504241265182.

Abstract

Insights into mechanisms driving either activation or inhibition of immune response are crucial in understanding the pathology of various diseases. The differentiation of viral from endogenous RNA in the cytoplasm by pattern-recognition receptors, such as retinoic acid-inducible gene I (RIG-I), is one of the essential paths for timely activation of an antiviral immune response through induction of type I interferons (IFN). In this mini-review, we describe the most recent developments centered around RIG-I's structure and mechanism of action. We summarize the paradigm-changing work over the past few years that helped us better understand RIG-I's monomeric and oligomerization states and their role in conveying immune response. We also discuss potential applications of the modulation of the RIG-I pathway in preventing autoimmune diseases or induction of immunity against viral infections. Overall, our review aims to summarize innovative research published in the past few years to help clarify questions that have long persisted around RIG-I.

Keywords: RIG-I; RNA; RNA-binding proteins; antiviral immune response; structural flexibility of RIG-I.

Publication types

  • Review

MeSH terms

  • Animals
  • DEAD Box Protein 58* / chemistry
  • DEAD Box Protein 58* / genetics
  • DEAD Box Protein 58* / immunology
  • DEAD Box Protein 58* / metabolism
  • Humans
  • Immunity, Innate
  • Interferon Type I / immunology
  • Interferon Type I / metabolism
  • Protein Multimerization
  • Receptors, Immunologic* / chemistry
  • Receptors, Immunologic* / metabolism
  • Signal Transduction
  • Virus Diseases / immunology

Substances

  • DEAD Box Protein 58
  • Receptors, Immunologic
  • RIGI protein, human
  • Interferon Type I