Journal
EXPERIMENTAL AND MOLECULAR MEDICINE
Volume 47, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/emm.2015.12
Keywords
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Funding
- Global Research Laboratory Program of the National Research Foundation (NRF) - Ministry of Science, ICT and Future Planning (MEST) [K20705000006-12A0500-00610]
- Bio and Medical Technology Development Program of the National Research Foundation (NRF) - Ministry of Science, ICT and Future Planning (MEST) [2012028272]
- Korea Health Technology R&D Project through Korea Health Industry Development Institute (KHIDI) - Ministry of Health and Welfare, Republic of Korea [HI13C08470200]
- Introduced Innovative R&D Team Leadership of Guangdong Province, People's Republic of China
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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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