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024 7 _ |a 10.1242/jcs.229252
|2 doi
024 7 _ |a pmid:31138677
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024 7 _ |a pmc:PMC6602300
|2 pmc
024 7 _ |a 0021-9533
|2 ISSN
024 7 _ |a 0370-2952
|2 ISSN
024 7 _ |a 1477-9137
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037 _ _ |a DZNE-2020-07104
041 _ _ |a English
082 _ _ |a 570
100 1 _ |a Das, Richa
|0 P:(DE-2719)2811341
|b 0
|e First author
|u dzne
245 _ _ |a New roles for the de-ubiquitylating enzyme OTUD4 in an RNA-protein network and RNA granules.
260 _ _ |a Cambridge
|c 2019
|b Company of Biologists Limited
264 _ 1 |3 online
|2 Crossref
|b The Company of Biologists
|c 2019-05-28
264 _ 1 |3 print
|2 Crossref
|b The Company of Biologists
|c 2019-06-15
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
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336 7 _ |a JOURNAL_ARTICLE
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336 7 _ |a Journal Article
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520 _ _ |a Mechanisms 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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542 _ _ |i 2019-06-17
|2 Crossref
|u http://creativecommons.org/licenses/by/4.0
588 _ _ |a Dataset connected to CrossRef, PubMed,
650 _ 2 |a Amyotrophic Lateral Sclerosis: metabolism
|2 MeSH
650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a Cytoplasmic Granules: metabolism
|2 MeSH
650 _ 2 |a DNA Helicases: genetics
|2 MeSH
650 _ 2 |a DNA-Binding Proteins: metabolism
|2 MeSH
650 _ 2 |a HeLa Cells
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Mice, Inbred C57BL
|2 MeSH
650 _ 2 |a Mutation: genetics
|2 MeSH
650 _ 2 |a Neurodegenerative Diseases: genetics
|2 MeSH
650 _ 2 |a Neurodegenerative Diseases: metabolism
|2 MeSH
650 _ 2 |a Neurons: metabolism
|2 MeSH
650 _ 2 |a RNA Recognition Motif Proteins: metabolism
|2 MeSH
650 _ 2 |a Ubiquitin-Specific Proteases: genetics
|2 MeSH
650 _ 2 |a Ubiquitin-Specific Proteases: metabolism
|2 MeSH
700 1 _ |a Schwintzer, Lukas
|0 P:(DE-2719)2810987
|b 1
|u dzne
700 1 _ |a Vinopal, Stanislav
|0 P:(DE-2719)2810898
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700 1 _ |a Aguado Roca, Eva
|0 P:(DE-2719)2810320
|b 3
|u dzne
700 1 _ |a Sylvester, Marc
|b 4
700 1 _ |a Oprisoreanu, Ana-Maria
|b 5
700 1 _ |a Schoch, Susanne
|b 6
700 1 _ |a Bradke, Frank
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700 1 _ |a Broemer, Meike
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773 1 8 |a 10.1242/jcs.229252
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|t Journal of Cell Science
|v 132
|y 2019
|x 0021-9533
773 _ _ |a 10.1242/jcs.229252
|g Vol. 132, no. 12, p. jcs229252 -
|0 PERI:(DE-600)1483099-1
|n 12
|q 132:12|p jcs229252
|t Journal of cell science
|v 132
|y 2019
|x 0021-9533
856 4 _ |u https://journals.biologists.com/jcs/article/132/12/jcs229252/179/New-roles-for-the-de-ubiquitylating-enzyme-OTUD4
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6602300
909 C O |p VDB
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LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21