| First Author | Bayle J | Year | 2006 |
| Journal | FEBS Lett | Volume | 580 |
| Issue | 11 | Pages | 2609-14 |
| PubMed ID | 16643902 | Mgi Jnum | J:200291 |
| Mgi Id | MGI:5508250 | Doi | 10.1016/j.febslet.2006.03.093 |
| Citation | Bayle J, et al. (2006) The E3 ubiquitin ligase HOIL-1 induces the polyubiquitination and degradation of SOCS6 associated proteins. FEBS Lett 580(11):2609-14 |
| abstractText | The suppressor of cytokine signaling (SOCS) proteins are thought to exert their function through the recruitment of interacting-proteins to the ubiquitin/proteasome degradation pathway. All SOCS proteins bind an Elongin BC E3 ubiquitin ligase complex through the common Socs-box. Here, we show that haem-oxidized IRP2 ubiquitin ligase-1 (HOIL-1), another E3 ubiquitin ligase, interacts with SOCS6. The Ubl domain of HOIL-1 and the SH2 and Socs-box domains of SOCS6 are required for the interaction. HOIL-1 expression stabilizes SOCS6 and induces the ubiquitination and degradation of proteins associated with SOCS6. These data suggest that SOCS proteins may interact with different E3 ubiquitin ligases in addition to a common Elongin BC E3 complex. |
