Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies

Exp Mol Med. 2015 Apr 17;47:e159. doi: 10.1038/emm.2015.12.

Abstract

Viral infection induces numerous tripartite motif (TRIM) proteins to control antiviral immune signaling and viral replication. Particularly, SPRY-containing TRIM proteins are found only in vertebrates and they control target protein degradation by their RING-finger and SPRY domains, and proper cytoplasmic localization. To understand TRIM30 function, we analyzed its localization pattern and putative roles of its RING-finger and SPRY domains. We found that TRIM30 is located in actin-mediated cytoplasmic bodies and produces colocalized ubiquitin chains in SPRY domain- and RING-finger domain-dependent ways that are degraded by autophagy and the proteasome. These results suggest a TRIM protein-dependent degradation mechanism by cytoplasmic body formation with actin networks.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Autophagy
  • Cell Line
  • Inclusion Bodies / metabolism*
  • Intracellular Signaling Peptides and Proteins / chemistry
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Mice
  • Molecular Sequence Data
  • Polyubiquitin / metabolism*
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Interaction Domains and Motifs
  • Protein Transport
  • Proteolysis
  • RING Finger Domains

Substances

  • Intracellular Signaling Peptides and Proteins
  • TRIM30 alpha protein, mouse
  • Polyubiquitin
  • Proteasome Endopeptidase Complex