Exp Mol Med.  2015 Apr;47(4):e159. 10.1038/emm.2015.12.

Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies

• Choi UY
• Choi WY
• Hur JY
• Kim YJ

• KMID: 2070278
• DOI: http://doi.org/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.

MeSH Terms

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