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@ARTICLE{Das:140782,
      author       = {Das, Richa and Schwintzer, Lukas and Vinopal, Stanislav and
                      Aguado Roca, Eva and Sylvester, Marc and Oprisoreanu,
                      Ana-Maria and Schoch, Susanne and Bradke, Frank and Broemer,
                      Meike},
      title        = {{N}ew roles for the de-ubiquitylating enzyme {OTUD}4 in an
                      {RNA}-protein network and {RNA} granules.},
      journal      = {Journal of cell science},
      volume       = {132},
      number       = {12},
      issn         = {0021-9533},
      address      = {Cambridge},
      publisher    = {Company of Biologists Limited},
      reportid     = {DZNE-2020-07104},
      pages        = {jcs229252},
      year         = {2019},
      abstract     = {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.},
      keywords     = {Amyotrophic Lateral Sclerosis: metabolism / Animals /
                      Cytoplasmic Granules: metabolism / DNA Helicases: genetics /
                      DNA-Binding Proteins: metabolism / HeLa Cells / Humans /
                      Mice, Inbred C57BL / Mutation: genetics / Neurodegenerative
                      Diseases: genetics / Neurodegenerative Diseases: metabolism
                      / Neurons: metabolism / RNA Recognition Motif Proteins:
                      metabolism / Ubiquitin-Specific Proteases: genetics /
                      Ubiquitin-Specific Proteases: metabolism},
      cin          = {AG Brömer 1 ; AG Brömer 1 / AG Bradke ; AG Bradke},
      ddc          = {570},
      cid          = {I:(DE-2719)5000021 / I:(DE-2719)1013002},
      pnm          = {341 - Molecular Signaling (POF3-341)},
      pid          = {G:(DE-HGF)POF3-341},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31138677},
      pmc          = {pmc:PMC6602300},
      doi          = {10.1242/jcs.229252},
      url          = {https://pub.dzne.de/record/140782},
}