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000153412 0247_ $$2doi$$a10.1038/s41467-020-15059-5
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000153412 1001_ $$aDietachmayr, Michael$$b0
000153412 245__ $$aAntagonistic activities of CDC14B and CDK1 on USP9X regulate WT1-dependent mitotic transcription and survival.
000153412 260__ $$a[London]$$bNature Publishing Group UK$$c2020
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000153412 520__ $$aRegulation of mitosis secures cellular integrity and its failure critically contributes to the development, maintenance, and treatment resistance of cancer. In yeast, the dual phosphatase Cdc14 controls mitotic progression by antagonizing Cdk1-mediated protein phosphorylation. By contrast, specific mitotic functions of the mammalian Cdc14 orthologue CDC14B have remained largely elusive. Here, we find that CDC14B antagonizes CDK1-mediated activating mitotic phosphorylation of the deubiquitinase USP9X at serine residue 2563, which we show to be essential for USP9X to mediate mitotic survival. Starting from an unbiased proteome-wide screening approach, we specify Wilms' tumor protein 1 (WT1) as the relevant substrate that becomes deubiquitylated and stabilized by serine 2563-phosphorylated USP9X in mitosis. We further demonstrate that WT1 functions as a mitotic transcription factor and specify CXCL8/IL-8 as a target gene of WT1 that conveys mitotic survival. Together, we describe a ubiquitin-dependent signaling pathway that directs a mitosis-specific transcription program to regulate mitotic survival.
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000153412 650_7 $$2NLM Chemicals$$aCXCL8 protein, human
000153412 650_7 $$2NLM Chemicals$$aInterleukin-8
000153412 650_7 $$2NLM Chemicals$$aTranscription Factors
000153412 650_7 $$2NLM Chemicals$$aUSP9X protein, human
000153412 650_7 $$2NLM Chemicals$$aWT1 Proteins
000153412 650_7 $$2NLM Chemicals$$aWT1 protein, human
000153412 650_7 $$0EC 2.7.11.22$$2NLM Chemicals$$aCDC2 Protein Kinase
000153412 650_7 $$0EC 2.7.11.22$$2NLM Chemicals$$aCDK1 protein, human
000153412 650_7 $$0EC 3.1.3.48$$2NLM Chemicals$$aCDC14B protein, human
000153412 650_7 $$0EC 3.1.3.48$$2NLM Chemicals$$aDual-Specificity Phosphatases
000153412 650_7 $$0EC 3.4.19.12$$2NLM Chemicals$$aUbiquitin Thiolesterase
000153412 650_2 $$2MeSH$$aA549 Cells
000153412 650_2 $$2MeSH$$aApoptosis
000153412 650_2 $$2MeSH$$aCDC2 Protein Kinase: antagonists & inhibitors
000153412 650_2 $$2MeSH$$aDual-Specificity Phosphatases: antagonists & inhibitors
000153412 650_2 $$2MeSH$$aGene Knockdown Techniques
000153412 650_2 $$2MeSH$$aHEK293 Cells
000153412 650_2 $$2MeSH$$aHeLa Cells
000153412 650_2 $$2MeSH$$aHumans
000153412 650_2 $$2MeSH$$aInterleukin-8: metabolism
000153412 650_2 $$2MeSH$$aMitosis: physiology
000153412 650_2 $$2MeSH$$aPhosphorylation
000153412 650_2 $$2MeSH$$aTranscription Factors
000153412 650_2 $$2MeSH$$aUbiquitin Thiolesterase: drug effects
000153412 650_2 $$2MeSH$$aUbiquitin Thiolesterase: genetics
000153412 650_2 $$2MeSH$$aUbiquitin Thiolesterase: metabolism
000153412 650_2 $$2MeSH$$aWT1 Proteins: genetics
000153412 650_2 $$2MeSH$$aWT1 Proteins: metabolism
000153412 7001_ $$aRathakrishnan, Abirami$$b1
000153412 7001_ $$aKarpiuk, Oleksandra$$b2
000153412 7001_ $$0P:(DE-2719)2811552$$avon Zweydorf, Felix$$b3$$udzne
000153412 7001_ $$aEngleitner, Thomas$$b4
000153412 7001_ $$aFernández-Sáiz, Vanesa$$b5
000153412 7001_ $$aSchenk, Petra$$b6
000153412 7001_ $$aUeffing, Marius$$b7
000153412 7001_ $$aRad, Roland$$b8
000153412 7001_ $$0P:(DE-HGF)0$$aEilers, Martin$$b9
000153412 7001_ $$0P:(DE-2719)2811291$$aGloeckner, Christian Johannes$$b10$$udzne
000153412 7001_ $$0P:(DE-HGF)0$$aClemm von Hohenberg, Katharina$$b11$$eCorresponding author
000153412 7001_ $$aBassermann, Florian$$b12
000153412 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/s41467-020-15059-5$$gVol. 11, no. 1, p. 1268$$n1$$p1268$$tNature Communications$$v11$$x2041-1723$$y2020
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