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 English
  • Published: 30 Mar 2011
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
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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