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KMID : 0620920150470040004
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Experimental & Molecular Medicine
2015 Volume.47 No. 4 p.4 ~ p.4
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Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies
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Choi Un-Yung
Choi Won-Young
Hur Ji-Yeon
Kim Young-Joon
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Abstract
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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.
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KEYWORD
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