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@ARTICLE{Floros:305653,
      author       = {K. V. Floros and C. K. Fairchild and J. Li and K. Zhang and
                      J. L. Roberts and R. Kurupi and D. Paudel and Y. Xing and B.
                      Hu and V. Kraskauskiene and N. Hosseini and S. Shen and M.
                      M. Inge and K. Smith-Fry and L. Li and A. Sotiriou$^*$ and
                      K. M. Dalton and A. Jose and E. I. Abdelfadiel and R. D.
                      Hill and J. M. Slaughter and M. Shende and M. R. Lorenz and
                      N. Tanaka and T. Kajino and M. L. Nelson and M. R. Hinojosa
                      and V. A. Kehinde and B. R. Belvin and F. G. Sugiokto and Z.
                      Lai and A. C. Dimopoulos and S. A. Boikos and A. M.
                      Stamatouli and J. P. Lewis and M. H. Manjili and H. Ebi and
                      K. Valerie and R. Li and A. Poklepovic and J. E. Koblinski
                      and T. Siggers and A. Banito$^*$ and M. G. Dozmorov and K.
                      B. Jones and S. K. Radhakrishnan and A. C. Faber},
      title        = {{T}argeting {SUMO}ylation promotes c{BAF} complex
                      stabilization and disruption of the {SS}18::{SSX}
                      transcriptome in synovial sarcoma.},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {DKFZ-2025-02285},
      pages        = {9761},
      year         = {2025},
      abstract     = {Synovial Sarcoma (SS) is driven by the SS18::SSX fusion
                      oncoprotein and is ultimately refractory to therapeutic
                      approaches. SS18::SSX alters ATP-dependent chromatin
                      remodeling BAF (mammalian SWI/SNF) complexes, leading to the
                      degradation of canonical (cBAF) complexes and amplified
                      expression of SS18::SSX-containing non-canonical BAF (ncBAF
                      or GBAF) complexes that drive an SS-specific transcription
                      program and tumorigenesis. We demonstrate that SS18::SSX
                      activates the SUMOylation program. The small molecule
                      SUMOylation inhibitor, TAK-981, de-SUMOylates the cBAF/PBAF
                      component, SMARCE1, stabilizing and restoring cBAF on
                      chromatin, shifting SS models away from SS18::SSX-driven
                      transcription. The result is DNA damage, cell death and
                      tumor inhibition across both human and mouse SS tumor
                      models. TAK-981 synergizes with cytotoxic chemotherapy
                      through increased DNA damage, leading to tumor regression.
                      Targeting the SUMOylation pathway in SS restores cBAF
                      complexes and blocks the SS18::SSX transcriptome,
                      identifying an unappreciated role of SUMOylation in SS and a
                      subsequent therapeutic vulnerability.},
      keywords     = {Sarcoma, Synovial: genetics / Sarcoma, Synovial: metabolism
                      / Sarcoma, Synovial: drug therapy / Sarcoma, Synovial:
                      pathology / Humans / Sumoylation: drug effects / Animals /
                      Mice / Cell Line, Tumor / Transcriptome / Oncogene Proteins,
                      Fusion: genetics / Oncogene Proteins, Fusion: metabolism /
                      Gene Expression Regulation, Neoplastic: drug effects / DNA
                      Damage: drug effects / Transcription Factors: metabolism /
                      Transcription Factors: genetics / DNA-Binding Proteins:
                      metabolism / DNA-Binding Proteins: genetics / Neoplasm
                      Proteins: metabolism / Neoplasm Proteins: genetics /
                      Chromosomal Proteins, Non-Histone: metabolism / Chromosomal
                      Proteins, Non-Histone: genetics / Repressor Proteins:
                      metabolism / Repressor Proteins: genetics / Chromatin
                      Assembly and Disassembly / Oncogene Proteins, Fusion (NLM
                      Chemicals) / Transcription Factors (NLM Chemicals) /
                      DNA-Binding Proteins (NLM Chemicals) / SS18-SSX1 fusion
                      protein (NLM Chemicals) / Neoplasm Proteins (NLM Chemicals)
                      / Chromosomal Proteins, Non-Histone (NLM Chemicals) /
                      Repressor Proteins (NLM Chemicals)},
      cin          = {B380},
      ddc          = {500},
      cid          = {I:(DE-He78)B380-20160331},
      pnm          = {312 - Funktionelle und strukturelle Genomforschung
                      (POF4-312)},
      pid          = {G:(DE-HGF)POF4-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:41193430},
      doi          = {10.1038/s41467-025-64665-8},
      url          = {https://inrepo02.dkfz.de/record/305653},
}