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@ARTICLE{Schwintzer:140619,
      author       = {Schwintzer, Lukas and Aguado Roca, Eva and Broemer, Meike},
      title        = {{TRIAD}3/{RNF}216 {E}3 ligase specifically synthesises
                      {K}63-linked ubiquitin chains and is inactivated by
                      mutations associated with {G}ordon {H}olmes syndrome.},
      journal      = {Cell death discovery},
      volume       = {5},
      number       = {1},
      issn         = {2058-7716},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {DZNE-2020-06941},
      pages        = {75},
      year         = {2019},
      abstract     = {TRIAD3/RNF216 is a ubiquitin ligase of the
                      RING-in-between-RING family. Recent publications identified
                      TRIAD3 mutations in patients with neurological diseases,
                      including Gordon Holmes syndrome and Huntington-like
                      disorder. To understand the functional relevance of these
                      disease-associated mutations, we have tested the ubiquitin
                      ligase activity of mutated TRIAD3 in vitro. Several of these
                      point mutations completely abrogated TRIAD3's catalytic
                      activity. Using mass spectrometry, we identified new
                      TRIAD3-interacting proteins/substrates from mouse brain
                      lysate, which provide a new link between TRIAD3 and
                      processes involving clathrin-mediated endocytosis.
                      Strikingly, we found that TRIAD3 synthesises specifically
                      lysine-63 (K63)-linked poly-ubiquitin chains in vitro, a
                      chain type that usually plays a role in mediating signalling
                      events rather than triggering proteasomal degradation.
                      Therefore, this finding is of great importance to further
                      understand TRIAD3's cellular role and loss-of-function in
                      disease.},
      cin          = {AG Brömer 1},
      ddc          = {610},
      cid          = {I:(DE-2719)5000021},
      pnm          = {341 - Molecular Signaling (POF3-341)},
      pid          = {G:(DE-HGF)POF3-341},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30886743},
      pmc          = {pmc:PMC6411869},
      doi          = {10.1038/s41420-019-0158-6},
      url          = {https://pub.dzne.de/record/140619},
}