Research Progress on the Structure and Function of G3BP

Front Immunol. 2021 Aug 30;12:718548. doi: 10.3389/fimmu.2021.718548. eCollection 2021.

Abstract

Ras-GTPase-activating protein (SH3 domain)-binding protein (G3BP) is an RNA binding protein. G3BP is a key component of stress granules (SGs) and can interact with many host proteins to regulate the expression of SGs. As an antiviral factor, G3BP can interact with viral proteins to regulate the assembly of SGs and thus exert antiviral effects. However, many viruses can also use G3BP as a proximal factor and recruit translation initiation factors to promote viral proliferation. G3BP regulates mRNA translation and attenuation to regulate gene expression; therefore, it is closely related to diseases, such as cancer, embryonic death, arteriosclerosis, and neurodevelopmental disorders. This review discusses the important discoveries and developments related G3BP in the biological field over the past 20 years, which includes the formation of SGs, interaction with viruses, stability of RNA, and disease progression.

Keywords: G3BP; cancer; stress granules; translation regulation; virus proliferation.

Publication types

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

MeSH terms

  • Animals
  • Cytoplasmic Granules / metabolism
  • DNA Helicases / chemistry*
  • DNA Helicases / genetics
  • DNA Helicases / metabolism*
  • Gene Expression Regulation
  • Host-Pathogen Interactions
  • Humans
  • Poly-ADP-Ribose Binding Proteins / chemistry*
  • Poly-ADP-Ribose Binding Proteins / genetics
  • Poly-ADP-Ribose Binding Proteins / metabolism*
  • Protein Binding
  • Protein Domains
  • Protein Interaction Domains and Motifs
  • RNA Helicases / chemistry*
  • RNA Helicases / genetics
  • RNA Helicases / metabolism*
  • RNA Recognition Motif Proteins / chemistry*
  • RNA Recognition Motif Proteins / genetics
  • RNA Recognition Motif Proteins / metabolism*
  • RNA Viruses / physiology
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Research
  • Stress, Physiological
  • Structure-Activity Relationship
  • Virus Replication

Substances

  • Poly-ADP-Ribose Binding Proteins
  • RNA Recognition Motif Proteins
  • RNA, Messenger
  • DNA Helicases
  • G3BP1 protein, human
  • RNA Helicases