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@ARTICLE{Neumann:136656,
      author       = {Neumann, Manuela and Valori, Chiara Flora and Ansorge, Olaf
                      and Kretzschmar, Hans and Munoz, David G and Kusaka,
                      Hirofumi and Yokota, Osamu and Ishihara, Kenji and Ang,
                      Lee-Cyn and Bilbao, Juan M and Mackenzie, Ian R.A.},
      title        = {{T}ransportin 1 accumulates specifically with {FET}
                      proteins but no other transportin cargos in {FTLD}-{FUS} and
                      is absent in {FUS} inclusions in {ALS} with {FUS}
                      mutations.},
      journal      = {Acta neuropathologica},
      volume       = {124},
      number       = {5},
      issn         = {0001-6322},
      address      = {Heidelberg},
      publisher    = {Springer},
      reportid     = {DZNE-2020-02978},
      pages        = {705-716},
      year         = {2012},
      abstract     = {Accumulation of the DNA/RNA binding protein fused in
                      sarcoma (FUS) as inclusions in neurons and glia is the
                      pathological hallmark of amyotrophic lateral sclerosis
                      patients with mutations in FUS (ALS-FUS) as well as in
                      several subtypes of frontotemporal lobar degeneration
                      (FTLD-FUS), which are not associated with FUS mutations.
                      Despite some overlap in the phenotype and neuropathology of
                      FTLD-FUS and ALS-FUS, significant differences of potential
                      pathomechanistic relevance were recently identified in the
                      protein composition of inclusions in these conditions. While
                      ALS-FUS showed only accumulation of FUS, inclusions in
                      FTLD-FUS revealed co-accumulation of all members of the FET
                      protein family, that include FUS, Ewing's sarcoma (EWS) and
                      TATA-binding protein-associated factor 15 (TAF15) suggesting
                      a more complex disturbance of transportin-mediated nuclear
                      import of proteins in FTLD-FUS compared to ALS-FUS. To gain
                      more insight into the mechanisms of inclusion body
                      formation, we investigated the role of Transportin 1 (Trn1)
                      as well as 13 additional cargo proteins of Transportin in
                      the spectrum of FUS-opathies by immunohistochemistry and
                      biochemically. FUS-positive inclusions in six ALS-FUS cases
                      including four different mutations did not label for Trn1.
                      In sharp contrast, the FET-positive pathology in all
                      FTLD-FUS subtypes was also strongly labeled for Trn1 and
                      often associated with a reduction in the normal nuclear
                      staining of Trn1 in inclusion bearing cells, while no
                      biochemical changes of Trn1 were detectable in FTLD-FUS.
                      Notably, despite the dramatic changes in the subcellular
                      distribution of Trn1 in FTLD-FUS, alterations of its cargo
                      proteins were restricted to FET proteins and no changes in
                      the normal physiological staining of 13 additional Trn1
                      targets, such as hnRNPA1, PAPBN1 and Sam68, were observed in
                      FTLD-FUS. These data imply a specific dysfunction in the
                      interaction between Trn1 and FET proteins in the inclusion
                      body formation in FTLD-FUS. Moreover, the absence of Trn1 in
                      ALS-FUS provides further evidence that ALS-FUS and FTLD-FUS
                      have different underlying pathomechanisms.},
      keywords     = {Adaptor Proteins, Signal Transducing: metabolism /
                      Amyotrophic Lateral Sclerosis: genetics / Amyotrophic
                      Lateral Sclerosis: metabolism / Brain: metabolism / Brain:
                      pathology / DNA-Binding Proteins: metabolism / Female /
                      Frontotemporal Lobar Degeneration: genetics / Frontotemporal
                      Lobar Degeneration: metabolism / Gene Expression Regulation:
                      genetics / Heterogeneous Nuclear Ribonucleoprotein A1 /
                      Heterogeneous-Nuclear Ribonucleoprotein Group A-B:
                      metabolism / Humans / Inclusion Bodies: metabolism /
                      Inclusion Bodies: pathology / Male / Mutation: genetics /
                      Poly(A)-Binding Protein I: metabolism / RNA-Binding Protein
                      EWS: metabolism / RNA-Binding Protein FUS: genetics /
                      RNA-Binding Protein FUS: metabolism / RNA-Binding Proteins:
                      metabolism / TATA-Binding Protein Associated Factors:
                      metabolism / beta Karyopherins: metabolism / Adaptor
                      Proteins, Signal Transducing (NLM Chemicals) / DNA-Binding
                      Proteins (NLM Chemicals) / Heterogeneous Nuclear
                      Ribonucleoprotein A1 (NLM Chemicals) / Heterogeneous-Nuclear
                      Ribonucleoprotein Group A-B (NLM Chemicals) / KHDRBS1
                      protein, human (NLM Chemicals) / PABPN1 protein, human (NLM
                      Chemicals) / Poly(A)-Binding Protein I (NLM Chemicals) /
                      RNA-Binding Protein EWS (NLM Chemicals) / RNA-Binding
                      Protein FUS (NLM Chemicals) / RNA-Binding Proteins (NLM
                      Chemicals) / TAF15 protein, human (NLM Chemicals) /
                      TATA-Binding Protein Associated Factors (NLM Chemicals) /
                      TNPO1 protein, human (NLM Chemicals) / beta Karyopherins
                      (NLM Chemicals) / hnRNPA1 protein, human (NLM Chemicals)},
      cin          = {AG Neumann},
      ddc          = {610},
      cid          = {I:(DE-2719)1210003},
      pnm          = {344 - Clinical and Health Care Research (POF3-344)},
      pid          = {G:(DE-HGF)POF3-344},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22842875},
      doi          = {10.1007/s00401-012-1020-6},
      url          = {https://pub.dzne.de/record/136656},
}