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CHIP controls necroptosis through ubiquitylation- and lysosome-dependent degradation of RIPK3
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Seo, Jinho | - |
dc.contributor.author | Lee, Eun-Woo | - |
dc.contributor.author | Sung, Hyerim | - |
dc.contributor.author | Seong, Daehyeon | - |
dc.contributor.author | Dondelinger, Yves | - |
dc.contributor.author | Shin, Jihye | - |
dc.contributor.author | Jeong, Manhyung | - |
dc.contributor.author | Lee, Hae-Kyung | - |
dc.contributor.author | Kim, Jung-Hoon | - |
dc.contributor.author | Han, Su Yeon | - |
dc.contributor.author | Lee, Cheolju | - |
dc.contributor.author | Seong, Je Kyung | - |
dc.contributor.author | Vandenabeele, Peter | - |
dc.contributor.author | Song, Jaewhan | - |
dc.date.accessioned | 2024-08-08T01:37:16Z | - |
dc.date.available | 2024-08-08T01:37:16Z | - |
dc.date.created | 2018-01-10 | - |
dc.date.created | 2018-01-10 | - |
dc.date.issued | 2016-03 | - |
dc.identifier.citation | Nature Cell Biology, Vol.18 No.3, pp.291-302 | - |
dc.identifier.issn | 1465-7392 | - |
dc.identifier.uri | https://hdl.handle.net/10371/206997 | - |
dc.description.abstract | Receptor-interacting protein kinase 3 (RIPK3) functions as a key regulator of necroptosis. Here, we report that the RIPK3 expression level is negatively regulated by CHIP (carboxyl terminus of Hsp70-interacting protein; also known as STUB1) E3 ligase-mediated ubiquitylation. Chip(-/-) mouse embryonic fibroblasts and CHIP-depleted L929 and HT-29 cells exhibited higher levels of RIPK3 expression, resulting in increased sensitivity to necroptosis induced by TNF (also known as TNF alpha). These phenomena are due to the CHIP-mediated ubiquitylation of RIPK3, which leads to its lysosomal degradation. Interestingly, RIPK1 expression is also negatively regulated by CHIP-mediated ubiquitylation, validating the major role of CHIP in necrosome formation and sensitivity to TNF-mediated necroptosis. Chip(-/-) mice (C57BL/6) exhibit inflammation in the thymus and massive cell death and disintegration in the small intestinal tract, and die within a few weeks after birth. These phenotypes are rescued by crossing with Ripk3(-/-) mice. These results imply that CHIP is a bona fide negative regulator of the RIPK1-RIPK3 necrosome formation leading to desensitization of TNF-mediated necroptosis. | - |
dc.language | 영어 | - |
dc.publisher | Nature Publishing Group | - |
dc.title | CHIP controls necroptosis through ubiquitylation- and lysosome-dependent degradation of RIPK3 | - |
dc.type | Article | - |
dc.identifier.doi | 10.1038/ncb3314 | - |
dc.citation.journaltitle | Nature Cell Biology | - |
dc.identifier.wosid | 000371031300010 | - |
dc.identifier.scopusid | 2-s2.0-84959241995 | - |
dc.citation.endpage | 302 | - |
dc.citation.number | 3 | - |
dc.citation.startpage | 291 | - |
dc.citation.volume | 18 | - |
dc.description.isOpenAccess | Y | - |
dc.contributor.affiliatedAuthor | Seong, Je Kyung | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | MIXED LINEAGE KINASE | - |
dc.subject.keywordPlus | DOMAIN-LIKE PROTEIN | - |
dc.subject.keywordPlus | CELL-DEATH | - |
dc.subject.keywordPlus | PROGRAMMED NECROSIS | - |
dc.subject.keywordPlus | APOPTOSIS | - |
dc.subject.keywordPlus | MLKL | - |
dc.subject.keywordPlus | UBIQUITINATION | - |
dc.subject.keywordPlus | CASPASE-8 | - |
dc.subject.keywordPlus | ROLES | - |
dc.subject.keywordPlus | FADD | - |
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