The plot thickens: OTULIN regulation in cell death.

Molecular & cellular oncology Pub Date : 2020-04-16 eCollection Date: 2020-01-01 DOI:10.1080/23723556.2020.1740541
Todd Douglas, Maya Saleh
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引用次数: 0

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.

图变厚:OTULIN在细胞死亡中的调控。
我们最近证明了OTU去泛素酶的翻译后修饰与线性连锁特异性(OTULIN)调节其在细胞死亡中的功能。OTULIN超磷酸化通过锁定环指蛋白31 (RNF31,也称为HOIP)远离圆柱状瘤病(CYLD)复合体来促进坏死下垂,导致受体相互作用丝氨酸/苏氨酸激酶1 (RIPK1)泛素化改变。此外,我们确定了双特异性磷酸酶14 (DUSP14)作为OTULIN磷酸酶,限制坏死性下垂。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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