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| Home > Publications database > Evidence for Homodimerization of the c-Fos Transcription Factor in Live Cells Revealed by Fluorescence Microscopy and Computer Modeling. > print |
| Home > Publications database > Evidence for Homodimerization of the c-Fos Transcription Factor in Live Cells Revealed by Fluorescence Microscopy and Computer Modeling. > print |
| 001 | 127594 | ||
| 005 | 20240228140938.0 | ||
| 024 | 7 | _ | |a 10.1128/MCB.00346-15 |2 doi |
| 024 | 7 | _ | |a pmid:26303532 |2 pmid |
| 024 | 7 | _ | |a pmc:PMC4589601 |2 pmc |
| 024 | 7 | _ | |a 0270-7306 |2 ISSN |
| 024 | 7 | _ | |a 1098-5549 |2 ISSN |
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| 037 | _ | _ | |a DKFZ-2017-03617 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Szalóki, Nikoletta |b 0 |
| 245 | _ | _ | |a Evidence for Homodimerization of the c-Fos Transcription Factor in Live Cells Revealed by Fluorescence Microscopy and Computer Modeling. |
| 260 | _ | _ | |a Washington, DC |c 2015 |b Soc. |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1508853768_29226 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a 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. |
| 536 | _ | _ | |a 312 - Functional and structural genomics (POF3-312) |0 G:(DE-HGF)POF3-312 |c POF3-312 |f POF III |x 0 |
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| 650 | _ | 7 | |a Chromatin |2 NLM Chemicals |
| 650 | _ | 7 | |a Proto-Oncogene Proteins c-fos |2 NLM Chemicals |
| 650 | _ | 7 | |a Proto-Oncogene Proteins c-jun |2 NLM Chemicals |
| 650 | _ | 7 | |a Transcription Factor AP-1 |2 NLM Chemicals |
| 650 | _ | 7 | |a DNA |0 9007-49-2 |2 NLM Chemicals |
| 700 | 1 | _ | |a Krieger, Jan Wolfgang |0 P:(DE-He78)f19ec6784f8068e5d4b51b33afc7ae6a |b 1 |u dkfz |
| 700 | 1 | _ | |a Komáromi, István |b 2 |
| 700 | 1 | _ | |a Tóth, Katalin |0 P:(DE-He78)ae1ffa194e5a8191ce2346491e4e828d |b 3 |u dkfz |
| 700 | 1 | _ | |a Vámosi, György |b 4 |
| 773 | _ | _ | |a 10.1128/MCB.00346-15 |g Vol. 35, no. 21, p. 3785 - 3798 |0 PERI:(DE-600)1474919-1 |n 21 |p 3785 - 3798 |t Molecular and cellular biology |v 35 |y 2015 |x 1098-5549 |
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