| Literature DB >> 32944611 |
Todd Douglas1, Maya Saleh1,2,3.
Abstract
We recently demonstrated that post-translational modifications of the OTU deubiquitinase with linear linkage specificity (OTULIN) regulate its function in cell death. OTULIN hyper-phosphorylation promotes necroptosis by locking ring finger protein 31 (RNF31, also known as HOIP) away from the cylindromatosis (CYLD) complex, resulting in altered receptor interacting serine/threonine kinase 1 (RIPK1) ubiquitination. Further, we identified dual specificity phosphatase 14 (DUSP14) as an OTULIN phosphatase that limits necroptosis.Entities:
Keywords: CYLD; Cell death; DUSP14; LUBAC; OTULIN; RIPK1; apoptosis; necroptosis; phosphorylation; ubiquitination
Year: 2020 PMID: 32944611 PMCID: PMC7469471 DOI: 10.1080/23723556.2020.1740541
Source DB: PubMed Journal: Mol Cell Oncol ISSN: 2372-3556