publication . Other literature type . Article . 2011

SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis

Panchali Goswami; Ivan Dikic; Ivan Dikic; Ariadne Androulidaki; Janoš Terzić; Katrin Rittinger; Liliana Schaefer; John P. Sundberg; Boris Macek; Tomoko Nakagawa; ...
Open Access
  • Published: 30 Mar 2011
  • Publisher: Springer Science and Business Media LLC
Abstract
SHARPIN is a ubiquitin-binding and ubiquitin-like-domain-containing protein which, when mutated in mice, results in immune system disorders and multi-organ inflammation. Here we report that SHARPIN functions as a novel component of the linear ubiquitin chain assembly complex (LUBAC) and that the absence of SHARPIN causes dysregulation of NF-κB and apoptotic signalling pathways, explaining the severe phenotypes displayed by chronic proliferative dermatitis (cpdm) in SHARPIN-deficient mice. Upon binding to the LUBAC subunit HOIP (also known as RNF31), SHARPIN stimulates the formation of linear ubiquitin chains in vitro and in vivo. Coexpression of SHARPIN and HOIP...
Subjects
free text keywords: Article, Ubiquitin ligase, biology.protein, biology, IKBKG, Cell biology, NFKB1, NF-κB, chemistry.chemical_compound, chemistry, Ubiquitin, Caspase 8, FADD, Ubiquitin ligase complex
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Europe PubMed Central
Other literature type . 2011
Nature
Article
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Nature
Article . 2011
Provider: Crossref
Abstract
SHARPIN is a ubiquitin-binding and ubiquitin-like-domain-containing protein which, when mutated in mice, results in immune system disorders and multi-organ inflammation. Here we report that SHARPIN functions as a novel component of the linear ubiquitin chain assembly complex (LUBAC) and that the absence of SHARPIN causes dysregulation of NF-κB and apoptotic signalling pathways, explaining the severe phenotypes displayed by chronic proliferative dermatitis (cpdm) in SHARPIN-deficient mice. Upon binding to the LUBAC subunit HOIP (also known as RNF31), SHARPIN stimulates the formation of linear ubiquitin chains in vitro and in vivo. Coexpression of SHARPIN and HOIP...
Subjects
free text keywords: Article, Ubiquitin ligase, biology.protein, biology, IKBKG, Cell biology, NFKB1, NF-κB, chemistry.chemical_compound, chemistry, Ubiquitin, Caspase 8, FADD, Ubiquitin ligase complex
Download fromView all 4 versions
Europe PubMed Central
Other literature type . 2011
Nature
Article
Provider: UnpayWall
Nature
Article . 2011
Provider: Crossref
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