Structural Analysis of SHARPIN, a Subunit of a Large Multi-protein E3 Ubiquitin Ligase, Reveals a Novel Dimerization Function for the Pleckstrin Homology Superfold-Reference-Cited by-同舟云学术

Structural Analysis of SHARPIN, a Subunit of a Large Multi-protein E3 Ubiquitin Ligase, Reveals a Novel Dimerization Function for the Pleckstrin Homology Superfold

Published:2012-06 Issue:25 Volume:287 Page:20823-20829
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Stieglitz Benjamin,Haire Lesley F.,Dikic Ivan,Rittinger Katrin

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference33 articles.

1. Sharpin, a novel postsynaptic density protein that directly interacts with the shank family of proteins;Lim;Mol. Cell Neurosci.,2001

2. Spontaneous mutations in the mouse Sharpin gene result in multiorgan inflammation, immune system dysregulation and dermatitis;Seymour;Genes Immun.,2007

3. SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis;Ikeda;Nature,2011

4. Linear ubiquitination prevents inflammation and regulates immune signaling;Gerlach;Nature,2011

5. SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex;Tokunaga;Nature,2011

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