Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 374, Issue 3, Pages 502-506Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2008.07.070
Keywords
TRIM22; RING finger; E3 ubiquitin ligase; nuclear protein
Categories
Funding
- Major State Basic Research Development Program of China [2007CB512401]
- China NSFC [30671952, 30872008]
- Shanghai STCSM [07QA14005, LJ06011]
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TRIM22, a member of the TRIM family proteins which contain RING finger, B-box, and coiled-coil domains, has been reported as a transcriptional regulator and involved in various cellular processes. In this study, the E3 ubiquitin ligase activity, a novel property of TRIM22, was demonstrated. It was found that TRIM22 underwent self-ubiquitylation in vitro in combination with the E2 enzyme UbcH5B and the ubiquitylation was dependent on its RING finger domain, Further evidences showed that TRIM22 Could also be self-ubiquitylated in vivo. Importantly, TRIM22 was Conjugated with poly-ubiquitin chains and stabilized by the proteasome inhibitor in 293T cells, suggesting that TRIM22 targeted itself for proteasomal degradation through the poly-ubiquitylation. We also found that TRIM22 was located in the nucleus, indicating that TRIM22 might function as a nuclear E3 ubiquitin ligase. (C) 2008 Elsevier Inc. All rights reserved.
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