Premium
The E3 ubiquitin ligase HOIL‐1 induces the polyubiquitination and degradation of SOCS6 associated proteins
Author(s) -
Bayle Julie,
Lopez Sophie,
Iwaï Kazuhiro,
Dubreuil Patrice,
De Sepulveda Paulo
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.093
Subject(s) - ubiquitin ligase , ubiquitin , chemistry , degradation (telecommunications) , microbiology and biotechnology , ubiquitin protein ligases , biochemistry , biology , gene , computer science , telecommunications
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.