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@ARTICLE{Zhang:13100,
      author       = {Zhang, G. and Yanamala, N. and Lathrop, KL. and Zhang, L.
                      and Klein-Seetharaman, J. and Srinivas, H.},
      title        = {{L}igand-independent antiapoptotic function of estrogen
                      receptor-beta in lung cancer cells},
      journal      = {Molecular endocrinology},
      volume       = {24},
      issn         = {0888-8809},
      address      = {Bethesda, Md.},
      publisher    = {Endocrine Society},
      reportid     = {PreJuSER-13100},
      pages        = {1737 - 1747},
      year         = {2010},
      note         = {This work was supported by the Career Development Award
                      from the University of Pittsburgh Specialized Program of
                      Research Excellence (SPORE) in Lung Cancer and by the Core
                      Grant for Vision Research EY08098.},
      abstract     = {Recent studies have demonstrated the presence of estrogen
                      receptor (ER)beta in the mitochondria in various cell types
                      and tissues, but the exact function of this localization
                      remains unclear. In this study, we have examined the
                      function of mitochondrial ERbeta in non-small-cell lung
                      cancer (NSCLC) cells. Down-regulation of ERbeta by short
                      hairpin RNA constructs sensitized NSCLC cells to various
                      apoptosis-inducing agents such as cisplatin, taxol, and
                      etoposide. The increased growth inhibition and induction of
                      apoptosis in ERbeta-knockdown cells was observed
                      irrespective of estrogen treatment, suggesting a
                      ligand-independent role of ERbeta in regulating the
                      intrinsic apoptotic pathway. Further, ERbeta from the
                      mitochondrial fraction physically interacted with the
                      proapoptotic protein Bad, in a ligand-independent manner.
                      Glutathione-S-transferase pull-down assays and molecular
                      modeling studies revealed that the DNA-binding domain and
                      hinge region of ERbeta, and the BH3 domain of Bad were
                      involved in these interactions. Further investigations
                      revealed that ERbeta inhibited Bad function by disrupting
                      Bad-Bcl-X(L) and Bad-Bcl-2 interactions. Reintroduction of
                      ERbeta in the mitochondria of ERbeta knockdown cells
                      reversed their sensitivity to cisplatin. Overall, our
                      results demonstrate a ligand-independent role of ERbeta in
                      regulating apoptosis, revealing a novel function for ERbeta
                      in the mitochondria.},
      keywords     = {Apoptosis: drug effects / Carcinoma, Non-Small-Cell Lung:
                      metabolism / Carcinoma, Non-Small-Cell Lung: pathology /
                      Cell Line, Tumor / Cell Survival: drug effects / Cisplatin:
                      pharmacology / Estrogen Receptor beta: chemistry / Estrogen
                      Receptor beta: metabolism / Gene Knockdown Techniques /
                      Humans / Immunoprecipitation / Inhibitory Concentration 50 /
                      Ligands / Lung Neoplasms: metabolism / Lung Neoplasms:
                      pathology / Mitochondria: drug effects / Mitochondria:
                      metabolism / Models, Biological / Models, Molecular /
                      Protein Binding: drug effects / Protein Structure, Tertiary
                      / Protein Transport: drug effects / RNA, Small Interfering:
                      metabolism / bcl-Associated Death Protein: chemistry /
                      bcl-Associated Death Protein: metabolism / bcl-X Protein:
                      metabolism / Estrogen Receptor beta (NLM Chemicals) /
                      Ligands (NLM Chemicals) / RNA, Small Interfering (NLM
                      Chemicals) / bcl-Associated Death Protein (NLM Chemicals) /
                      bcl-X Protein (NLM Chemicals) / Cisplatin (NLM Chemicals) /
                      J (WoSType)},
      cin          = {ISB-2},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK505},
      shelfmark    = {Endocrinology $\&$ Metabolism},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20660297},
      pmc          = {pmc:PMC2940472},
      UT           = {WOS:000281387300005},
      doi          = {10.1210/me.2010-0125},
      url          = {https://juser.fz-juelich.de/record/13100},
}