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New role of E3 ubiquitin ligase in the regulation of necroptosis
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  • Journal title : BMB Reports
  • Volume 49, Issue 5,  2016, pp.247-248
  • Publisher : Korean Society for Biochemistry and Molecular Biology
  • DOI : 10.5483/BMBRep.2016.49.5.067
 Title & Authors
New role of E3 ubiquitin ligase in the regulation of necroptosis
Seo, Jinho; Lee, Eun-Woo; Song, Jaewhan;
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Necroptosis is a well-known form of caspase-independent cell death. Necroptosis can be triggered by various extrinsic stimuli, including death ligands in the presence of receptorinteracting protein kinase 3 (RIPK3), a key mediator of necroptosis induction. Our recent studies have revealed that C-terminus HSC-70 interacting protein (CHIP), an E3 ligase, can function as an inhibitor of necroptosis. CHIP−/− mouse embryonic fibroblast showed higher sensitivity to necrotic stimuli than wild-type mouse embryonic fibroblast cells. Deleterious effects of CHIP knockout MEFs were retrieved by RIPK3 depletion. We found that CHIP negatively regulated RIPK3 and RIPK1 by ubiquitylation- and lysosome- dependent degradation. In addition, CHIP−/− mice showed postnatal lethality with intestinal defects that could be rescued by crossing with RIPK3−/− mice. These results suggest that CHIP is a negative regulator of RIPK1 and RIPK3, thus inhibiting necroptosis.
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