Journal
FEBS LETTERS
Volume 580, Issue 11, Pages 2609-2614Publisher
WILEY
DOI: 10.1016/j.febslet.2006.03.093
Keywords
SOCS; protein regulation; proteasome; RBCK; UIP28
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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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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