Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies

Un Y.ung Choi, Won Y.oung Choi, Ji Y.eon Hur, Young Joon Kim

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)e159
JournalExperimental & molecular medicine
Publication statusPublished - 2015

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Clinical Biochemistry


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