The E3 ubiquitin ligase HOIL-1 induces the polyubiquitination and degradation of SOCS6 associated proteins |
| |
Authors: | Bayle Julie Lopez Sophie Iwaï Kazuhiro Dubreuil Patrice De Sepulveda Paulo |
| |
Affiliation: | INSERM UMR599, Laboratoire d'hématopo?èse moléculaire et fonctionnelle, Marseille, France. |
| |
Abstract: | 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. |
| |
Keywords: | SOCS Protein regulation Proteasome RBCK UIP28 |
本文献已被 ScienceDirect PubMed 等数据库收录! |