Evidence map›Paper›PMID 26303532›Full record

ArticleMolecular and cellular biology2015

Evidence for Homodimerization of the c-Fos Transcription Factor in Live Cells Revealed by Fluorescence Microscopy and Computer Modeling.

Nikoletta Szalóki, Jan Wolfgang Krieger, István Komáromi, Katalin Tóth, György Vámosi

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.1field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 46 citations in OpenAlex.

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  9. Cell-specific expression of theFrontiers in molecular biosciences · 2023
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  12. Review
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  14. Variants Within GenesFrontiers in genetics · 2022
    Article
  15. The AscidiaFrontiers in cell and developmental biology · 2021
    Article
  16. Article
  17. Review
  18. Detecting protein-protein interactions by Xe-129 NMR.Chemical communications (Cambridge, England) · 2020
    Article
  19. Review
  20. A strategy for designing allosteric modulators of transcription factor dimerization.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 3 countries.

Nikoletta SzalókiDepartment of Biophysics and Cell Biology, Research Center for Molecular Medicine, University of Debrecen, Debrecen, Hungary.
Jan Wolfgang KriegerGerman Cancer Research Center (DKFZ), Biophysics of Macromolecules, Heidelberg, Germany.
István KomáromiHAS-UD Vascular Biology, Thrombosis and Hemostasis Research Group, Hungarian Academy of Sciences, Debrecen, Hungary Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.
Katalin TóthGerman Cancer Research Center (DKFZ), Biophysics of Macromolecules, Heidelberg, Germany.
György VámosiDepartment of Biophysics and Cell Biology, Research Center for Molecular Medicine, University of Debrecen, Debrecen, Hungary Sanford Burnham Prebys Medical Discovery Institute at Lake Nona, Orlando, Florida, USA vamosig@med.unideb.hu.
Heidelberg University · DEDiscovery Institute · USHungarian Academy of Sciences · HUUniversity of Debrecen · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Molecular Dynamics SimulationChromatinDNAFluorescence Resonance Energy TransferHeLa CellsHumansMicroscopy, FluorescenceMolecular Docking SimulationProtein BindingProtein MultimerizationProto-Oncogene Proteins c-fosProto-Oncogene Proteins c-junTranscription Factor AP-1ChromatinDNAProto-Oncogene Proteins c-fosProto-Oncogene Proteins c-junTranscription Factor AP-1

Identifiers

PMID26303532
PMCPMC4589601
OpenAlexW2238978610

What OpenQuestion holds

Textmetadata
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.