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@ARTICLE{Adam:126010,
      author       = {M. G. Adam$^*$ and S. Matt and S. Christian and H.
                      Hess-Stumpp and A. Haegebarth and T. Hofmann$^*$ and C.
                      Algire},
      title        = {{SIAH} ubiquitin ligases regulate breast cancer cell
                      migration and invasion independent of the oxygen status.},
      journal      = {Cell cycle},
      volume       = {14},
      number       = {23},
      issn         = {1551-4005},
      address      = {Georgetown, Tex.},
      publisher    = {Landes Bioscience},
      reportid     = {DKFZ-2017-02125},
      pages        = {3734 - 3747},
      year         = {2015},
      abstract     = {Seven-in-absentia homolog (SIAH) proteins are evolutionary
                      conserved RING type E3 ubiquitin ligases responsible for the
                      degradation of key molecules regulating DNA damage response,
                      hypoxic adaptation, apoptosis, angiogenesis, and cell
                      proliferation. Many studies suggest a tumorigenic role for
                      SIAH2. In breast cancer patients SIAH2 expression levels
                      correlate with cancer aggressiveness and overall patient
                      survival. In addition, SIAH inhibition reduced metastasis in
                      melanoma. The role of SIAH1 in breast cancer is still
                      ambiguous; both tumorigenic and tumor suppressive functions
                      have been reported. Other studies categorized SIAH ligases
                      as either pro- or antimigratory, while the significance for
                      metastasis is largely unknown. Here, we re-evaluated the
                      effects of SIAH1 and SIAH2 depletion in breast cancer cell
                      lines, focusing on migration and invasion. We successfully
                      knocked down SIAH1 and SIAH2 in several breast cancer cell
                      lines. In luminal type MCF7 cells, this led to stabilization
                      of the SIAH substrate Prolyl Hydroxylase Domain protein 3
                      (PHD3) and reduced Hypoxia-Inducible Factor 1α (HIF1α)
                      protein levels. Both the knockdown of SIAH1 or SIAH2 led to
                      increased apoptosis and reduced proliferation, with
                      comparable effects. These results point to a tumor promoting
                      role for SIAH1 in breast cancer similar to SIAH2. In
                      addition, depletion of SIAH1 or SIAH2 also led to decreased
                      cell migration and invasion in breast cancer cells. SIAH
                      knockdown also controlled microtubule dynamics by markedly
                      decreasing the protein levels of stathmin, most likely via
                      p27(Kip1). Collectively, these results suggest that both
                      SIAH ligases promote a migratory cancer cell phenotype and
                      could contribute to metastasis in breast cancer.},
      keywords     = {CDKN1B protein, human (NLM Chemicals) / Nuclear Proteins
                      (NLM Chemicals) / Stathmin (NLM Chemicals) /
                      Cyclin-Dependent Kinase Inhibitor p27 (NLM Chemicals) /
                      Ubiquitin-Protein Ligases (NLM Chemicals) / seven in
                      absentia proteins (NLM Chemicals)},
      cin          = {A210},
      ddc          = {570},
      cid          = {I:(DE-He78)A210-20160331},
      pnm          = {311 - Signalling pathways, cell and tumor biology
                      (POF3-311)},
      pid          = {G:(DE-HGF)POF3-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:26654769},
      pmc          = {pmc:PMC4825722},
      doi          = {10.1080/15384101.2015.1104441},
      url          = {https://inrepo02.dkfz.de/record/126010},
}