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000140782 0247_ $$2doi$$a10.1242/jcs.229252
000140782 0247_ $$2pmid$$apmid:31138677
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000140782 0247_ $$2ISSN$$a0370-2952
000140782 0247_ $$2ISSN$$a1477-9137
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000140782 037__ $$aDZNE-2020-07104
000140782 041__ $$aEnglish
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000140782 1001_ $$0P:(DE-2719)2811341$$aDas, Richa$$b0$$eFirst author$$udzne
000140782 245__ $$aNew roles for the de-ubiquitylating enzyme OTUD4 in an RNA-protein network and RNA granules.
000140782 260__ $$aCambridge$$bCompany of Biologists Limited$$c2019
000140782 264_1 $$2Crossref$$3online$$bThe Company of Biologists$$c2019-05-28
000140782 264_1 $$2Crossref$$3print$$bThe Company of Biologists$$c2019-06-15
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000140782 3367_ $$2BibTeX$$aARTICLE
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000140782 520__ $$aMechanisms that regulate the formation of membrane-less cellular organelles, such as neuronal RNA granules and stress granules, have gained increasing attention over the past years. These granules consist of RNA and a plethora of RNA-binding proteins. Mutations in RNA-binding proteins have been found in neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). By performing pulldown experiments and subsequent mass spectrometry on mouse brain lysates, we discovered that the de-ubiquitylating enzyme OTU domain-containing protein 4 (OTUD4) unexpectedly is part of a complex network of multiple RNA-binding proteins, including core stress granule factors, such as FMRP (also known as FMR1), SMN1, G3BP1 and TIA1. We show that OTUD4 binds RNA, and that several of its interactions with RNA-binding proteins are RNA dependent. OTUD4 is part of neuronal RNA transport granules in rat hippocampal neurons under physiological conditions, whereas upon cellular stress, OTUD4 is recruited to cytoplasmic stress granules. Knockdown of OTUD4 in HeLa cells resulted in defects in stress granule formation and led to apoptotic cell death. Together, we characterize OTUD4 as a new RNA-binding protein with a suggested function in regulation of translation.
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000140782 542__ $$2Crossref$$i2019-06-17$$uhttp://creativecommons.org/licenses/by/4.0
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000140782 650_2 $$2MeSH$$aAmyotrophic Lateral Sclerosis: metabolism
000140782 650_2 $$2MeSH$$aAnimals
000140782 650_2 $$2MeSH$$aCytoplasmic Granules: metabolism
000140782 650_2 $$2MeSH$$aDNA Helicases: genetics
000140782 650_2 $$2MeSH$$aDNA-Binding Proteins: metabolism
000140782 650_2 $$2MeSH$$aHeLa Cells
000140782 650_2 $$2MeSH$$aHumans
000140782 650_2 $$2MeSH$$aMice, Inbred C57BL
000140782 650_2 $$2MeSH$$aMutation: genetics
000140782 650_2 $$2MeSH$$aNeurodegenerative Diseases: genetics
000140782 650_2 $$2MeSH$$aNeurodegenerative Diseases: metabolism
000140782 650_2 $$2MeSH$$aNeurons: metabolism
000140782 650_2 $$2MeSH$$aRNA Recognition Motif Proteins: metabolism
000140782 650_2 $$2MeSH$$aUbiquitin-Specific Proteases: genetics
000140782 650_2 $$2MeSH$$aUbiquitin-Specific Proteases: metabolism
000140782 7001_ $$0P:(DE-2719)2810987$$aSchwintzer, Lukas$$b1$$udzne
000140782 7001_ $$0P:(DE-2719)2810898$$aVinopal, Stanislav$$b2$$udzne
000140782 7001_ $$0P:(DE-2719)2810320$$aAguado Roca, Eva$$b3$$udzne
000140782 7001_ $$aSylvester, Marc$$b4
000140782 7001_ $$aOprisoreanu, Ana-Maria$$b5
000140782 7001_ $$aSchoch, Susanne$$b6
000140782 7001_ $$0P:(DE-2719)2810270$$aBradke, Frank$$b7$$udzne
000140782 7001_ $$0P:(DE-2719)2810307$$aBroemer, Meike$$b8$$eLast author$$udzne
000140782 77318 $$2Crossref$$3journal-article$$a10.1242/jcs.229252$$b : The Company of Biologists, 2019-05-28$$n12$$pjcs229252$$tJournal of Cell Science$$v132$$x0021-9533$$y2019
000140782 773__ $$0PERI:(DE-600)1483099-1$$a10.1242/jcs.229252$$gVol. 132, no. 12, p. jcs229252 -$$n12$$pjcs229252$$q132:12<jcs229252 -$$tJournal of cell science$$v132$$x0021-9533$$y2019
000140782 8564_ $$uhttps://journals.biologists.com/jcs/article/132/12/jcs229252/179/New-roles-for-the-de-ubiquitylating-enzyme-OTUD4
000140782 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC6602300
000140782 909CO $$ooai:pub.dzne.de:140782$$pVDB
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