Academic
Publications
Identification of TRIM22 as a RING finger E3 ubiquitin ligase

Identification of TRIM22 as a RING finger E3 ubiquitin ligase,10.1016/j.bbrc.2008.07.070,Biochemical and Biophysical Research Communications,Zhijian D

Identification of TRIM22 as a RING finger E3 ubiquitin ligase   (Citations: 11)
BibTex | RIS | RefWorks Download
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.
Cumulative Annual
View Publication
The following links allow you to view full publications. These links are maintained by other sources not affiliated with Microsoft Academic Search.
    • ...Previous studies have demonstrated that the RING finger domain of many TRIM proteins, including that of TRIM5a, TRIM22, and TRIM25, possesses an E3 ubiquitin ligase activity, which can catalyze ubiquitin to cellular proteins or viral proteins [7-10]...
    • ...Some such E3 ligases are RING finger proteins [7,8]...
    • ...The RING-domain, which is located at the N-terminus of TRIMs, is critical to the activity of most E3 ligase [7,8]...
    • ...TRIM38 functions as an E3 enzyme and self-ubiquitinates ex vivo Many RING finger domain-containing proteins have been shown to bind ubiquitin enzymes or their substrates, hence functioning as E3 ligases [7-9]...
    • ...Recently, several groups reported that E3 ubiquitin ligases are ubiquitinated by themselves [7,9]...
    • ...RING domain is important for ubiquitin activity of TRIM38 Many RING-finger proteins have been identified as E3 ubiquitin ligases [7-9]...
    • ...TRIM22 functions as an E3 ubiquitin ligase in a RING finger dependent manner [7], and is required to...

    Xinlei Liuet al. Enterovirus 71 induces degradation of TRIM38, a potential E3 ubiquitin...

    • ...In contrast, a c-myc-tagged protein product linked to TRIM22 coding sequence amplified from human peripheral blood mononuclear cells localized TRIM22 exclusively in the nucleus (Duan et al. 2008)...

    Anna Kajaste-Rudnitskiet al. Restriction factors of retroviral replication: the example of Triparti...

Sort by: