Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies.
- Author:
Un Yung CHOI
1
;
Won Young CHOI
;
Ji Yeon HUR
;
Young Joon KIM
Author Information
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- MeSH: 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
- From:Experimental & Molecular Medicine 2015;47(4):e159-
- CountryRepublic of Korea
- Language:Korean
- 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.
