Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation - PubMed (original) (raw)
doi: 10.1038/ncb1821. Epub 2009 Jan 11.
Shin-ichi Sakata, Yasushi Saeki, Yoshinori Satomi, Takayoshi Kirisako, Kiyoko Kamei, Tomoko Nakagawa, Michiko Kato, Shigeo Murata, Shoji Yamaoka, Masahiro Yamamoto, Shizuo Akira, Toshifumi Takao, Keiji Tanaka, Kazuhiro Iwai
Affiliations
- PMID: 19136968
- DOI: 10.1038/ncb1821
Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation
Fuminori Tokunaga et al. Nat Cell Biol. 2009 Feb.
Abstract
Nuclear factor-kappaB (NF-kappaB) is a key transcription factor in inflammatory, anti-apoptotic and immune processes. The ubiquitin pathway is crucial in regulating the NF-kappaB pathway. We have found that the LUBAC ligase complex, composed of the two RING finger proteins HOIL-1L and HOIP, conjugates a head-to-tail-linked linear polyubiquitin chain to substrates. Here, we demonstrate that LUBAC activates the canonical NF-kappaB pathway by binding to NEMO (NF-kappaB essential modulator, also called IKKgamma) and conjugates linear polyubiquitin chains onto specific Lys residues in the CC2-LZ domain of NEMO in a Ubc13-independent manner. Moreover, in HOIL-1 knockout mice and cells derived from these mice, NF-kappaB signalling induced by pro-inflammatory cytokines such as TNF-alpha and IL-1beta was suppressed, resulting in enhanced TNF-alpha-induced apoptosis in hepatocytes of HOIL-1 knockout mice. These results indicate that LUBAC is involved in the physiological regulation of the canonical NF-kappaB activation pathway through linear polyubiquitylation of NEMO.
Comment in
- Linear polyubiquitylation: the missing link in NF-kappaB signalling.
Haas AL. Haas AL. Nat Cell Biol. 2009 Feb;11(2):116-8. doi: 10.1038/ncb0209-116. Nat Cell Biol. 2009. PMID: 19188917 No abstract available.
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