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@ARTICLE{GarcaMorato:269004,
      author       = {García Morato, Jorge and Gloeckner, Christian Johannes and
                      Kahle, Philipp},
      title        = {{P}roteomics elucidating physiological and pathological
                      functions of {TDP}‐43},
      journal      = {Proteomics},
      volume       = {23},
      number       = {23-24},
      issn         = {1615-9853},
      address      = {Weinheim},
      publisher    = {Wiley VCH},
      reportid     = {DZNE-2024-00438},
      pages        = {2200410},
      year         = {2023},
      abstract     = {Trans-activation response DNA binding protein of 43 kDa
                      (TDP-43) regulates a great variety of cellular processes in
                      the nucleus and cytosol. In addition, a defined subset of
                      neurodegenerative diseases is characterized by nuclear
                      depletion of TDP-43 as well as cytosolic mislocalization and
                      aggregation. To perform its diverse functions TDP-43 can
                      associate with different ribonucleoprotein complexes.
                      Combined with transcriptomics, MS interactome studies have
                      unveiled associations between TDP-43 and the spliceosome
                      machinery, polysomes and RNA granules. Moreover, the highly
                      dynamic, low-valency interactions regulated by its
                      low-complexity domain calls for innovative proximity
                      labeling methodologies. In addition to protein partners, the
                      analysis of post-translational modifications showed that
                      they may play a role in the nucleocytoplasmic shuttling, RNA
                      binding, liquid-liquid phase separation and protein
                      aggregation of TDP-43. Here we review the various TDP-43
                      ribonucleoprotein complexes characterized so far, how they
                      contribute to the diverse functions of TDP-43, and roles of
                      post-translational modifications. Further understanding of
                      the fluid dynamic properties of TDP-43 in ribonucleoprotein
                      complexes, RNA granules, and self-assemblies will advance
                      the understanding of RNA processing in cells and perhaps
                      help to develop novel therapeutic approaches for
                      TDPopathies.},
      subtyp        = {Review Article},
      keywords     = {Proteomics / Protein Aggregates / DNA-Binding Proteins:
                      genetics / Ribonucleoproteins},
      cin          = {AG Gasser / AG Gloeckner},
      ddc          = {540},
      cid          = {I:(DE-2719)1210000 / I:(DE-2719)1210007},
      pnm          = {353 - Clinical and Health Care Research (POF4-353) / 352 -
                      Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-353 / G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37671599},
      doi          = {10.1002/pmic.202200410},
      url          = {https://pub.dzne.de/record/269004},
}