| First Author | Kim EJ | Year | 2008 |
| Journal | Biochem Biophys Res Commun | Volume | 377 |
| Issue | 3 | Pages | 952-6 |
| PubMed ID | 18955028 | Mgi Jnum | J:144079 |
| Mgi Id | MGI:3829858 | Doi | 10.1016/j.bbrc.2008.10.092 |
| Citation | Kim EJ, et al. (2008) Ubc9-mediated sumoylation leads to transcriptional repression of IRF-1. Biochem Biophys Res Commun 377(3):952-6 |
| abstractText | To characterize the regulatory mechanism of the interferon regulatory factor (IRF) family, we performed yeast two-hybrid screening with IRF-2 and isolated the small ubiquitin-related modifier (SUMO)-conjugating enzyme Ubc9, which also interacts with other IRF family members IRF-1 and ICSBP. Subsequent assays indicated that among the IRF family members, only IRF-1 interacts with SUMO-1 through its transcriptional activation domain. The interaction between IRF-1 and SUMO-1 was confirmed in vitro by GST pull-down assays and in vivo by co-localization assays. Furthermore, this interaction led to the Ubc9-mediated sumoylation of IRF-1 in vitro and in vivo. Transient transfection assays revealed that Ubc9 or SUMO inhibits the transcriptional activity of IRF-1 in a dose-dependent manner. Finally, Ubc9 and SUMO cooperate in the transcriptional repression of IRF-1. Taken together, these observations suggest that Ubc9 functions as a transcriptional repressor of IRF-1 by inducing sumoylation, and that this effect may be required for the physiological activity of IRF-1. |
