Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies.
Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies.
Exp Mol Med. 2015;47:e159
Authors: Choi UY, Choi WY, Hur JY, Kim YJ
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.
PMID: 25882191 [PubMed - in process]
Source: exp Mol Med - Category: Molecular Biology Authors: Choi UY, Choi WY, Hur JY, Kim YJ Tags: Exp Mol Med Source Type: research
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