Identification of TRIM22 as a RING finger E3 ubiquitin ligase
- Institute for Immunobiology, Department of Immunology, Shanghai Medical College of Fudan University, 138 Yi Xue Yuan Road, Shanghai 200032 (China)
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.
- OSTI ID:
- 21143881
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 374, Issue 3; Other Information: DOI: 10.1016/j.bbrc.2008.07.070; PII: S0006-291X(08)01388-0; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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