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@ARTICLE{Szalki:127594,
      author       = {N. Szalóki and J. W. Krieger$^*$ and I. Komáromi and K.
                      Tóth$^*$ and G. Vámosi},
      title        = {{E}vidence for {H}omodimerization of the c-{F}os
                      {T}ranscription {F}actor in {L}ive {C}ells {R}evealed by
                      {F}luorescence {M}icroscopy and {C}omputer {M}odeling.},
      journal      = {Molecular and cellular biology},
      volume       = {35},
      number       = {21},
      issn         = {1098-5549},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {DKFZ-2017-03617},
      pages        = {3785 - 3798},
      year         = {2015},
      abstract     = {The c-Fos and c-Jun transcription factors, members of the
                      activator protein 1 (AP-1) complex, form heterodimers and
                      bind to DNA via a basic leucine zipper and regulate the cell
                      cycle, apoptosis, differentiation, etc. Purified c-Jun
                      leucine zipper fragments could also form stable homodimers,
                      whereas c-Fos leucine zipper homodimers were found to be
                      much less stable in earlier in vitro studies. The importance
                      of c-Fos overexpression in tumors and the controversy in the
                      literature concerning c-Fos homodimerization prompted us to
                      investigate Fos homodimerization. Förster resonance energy
                      transfer (FRET) and molecular brightness analysis of
                      fluorescence correlation spectroscopy data from live HeLa
                      cells transfected with fluorescent-protein-tagged c-Fos
                      indicated that c-Fos formed homodimers. We developed a
                      method to determine the absolute concentrations of
                      transfected and endogenous c-Fos and c-Jun, which allowed us
                      to determine dissociation constants of c-Fos homodimers (Kd
                      = 6.7 ± 1.7 μM) and c-Fos-c-Jun heterodimers (on the order
                      of 10 to 100 nM) from FRET titrations. Imaging fluorescence
                      cross-correlation spectroscopy (SPIM-FCCS) and molecular
                      dynamics modeling confirmed that c-Fos homodimers were
                      stably associated and could bind to the chromatin. Our
                      results establish c-Fos homodimers as a novel form of the
                      AP-1 complex that may be an autonomous transcription factor
                      in c-Fos-overexpressing tissues and could contribute to
                      tumor development.},
      keywords     = {Chromatin (NLM Chemicals) / Proto-Oncogene Proteins c-fos
                      (NLM Chemicals) / Proto-Oncogene Proteins c-jun (NLM
                      Chemicals) / Transcription Factor AP-1 (NLM Chemicals) / DNA
                      (NLM Chemicals)},
      cin          = {B160},
      ddc          = {570},
      cid          = {I:(DE-He78)B160-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:26303532},
      pmc          = {pmc:PMC4589601},
      doi          = {10.1128/MCB.00346-15},
      url          = {https://inrepo02.dkfz.de/record/127594},
}