کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1935449 | 1050665 | 2008 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Identification of TRIM22 as a RING finger E3 ubiquitin ligase Identification of TRIM22 as a RING finger E3 ubiquitin ligase](/preview/png/1935449.png)
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.
Journal: Biochemical and Biophysical Research Communications - Volume 374, Issue 3, 26 September 2008, Pages 502–506