Evidence map›Paper›PMID 12974672›Full record

ArticleThe Biochemical journal2004

Analysis of Stat3 (signal transducer and activator of transcription 3) dimerization by fluorescence resonance energy transfer in living cells.

Antje K Kretzschmar, Michaela C Dinger, Christian Henze, Katja Brocke-Heidrich, Friedemann Horn

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

44 citing papers in PubMed, 108 citations in OpenAlex.

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  8. Cytokines in Inflammatory Disease.International journal of molecular sciences · 2019
    Review
  9. Dynamic monitoring of STAT3 activation in live cells using a novel STAT3 Phospho-BRET sensor.American journal of nuclear medicine and molecular imaging · 2019
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Antje K KretzschmarInstitute of Clinical Immunology and Transfusion Medicine, University Hospital, Leipzig Johannisallee 30, D-04103 Leipzig, Germany.
Michaela C Dinger
Christian Henze
Katja Brocke-Heidrich
Friedemann Horn
University Hospital Leipzig · DELeipzig University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signal transducer and activator of transcription 3 (Stat3) dimerization is commonly thought to be triggered by its tyrosine phosphorylation in response to interleukin-6 (IL-6) or other cytokines. Accumulating evidence from in vitro studies, however, suggests that cytoplasmic Stat3 may be associated with high-molecular-mass protein complexes and/or dimerize prior to its activation. To directly study Stat3 dimerization and subcellular localization upon cytokine stimulation, we used live-cell fluorescence spectroscopy and imaging microscopy combined with fluorescence resonance energy transfer (FRET). Stat3 fusion proteins with spectral variants of green fluorescent protein (GFP), cyan fluorescent protein (CFP) and yellow fluorescent protein (YFP) were constructed and expressed in human hepatoma cells (HepG2) and human embryonic kidney cells (HEK-293). Like wild-type Stat3, the fusion proteins redistributed from a preferentially cytoplasmic to nuclear localization upon IL-6 stimulation and supported IL-6-dependent target gene expression. FRET studies in cells co-expressing Stat3-CFP and Stat3-YFP demonstrated that Stat3 dimers exist in the absence of tyrosine phosphorylation. IL-6 induced a 2-fold increase of this basal FRET signal, indicating that tyrosine phosphorylation either increases the dimer/monomer ratio of Stat3 or induces a conformational change of the dimer yielding a higher FRET efficiency. Studies using a mutated Stat3 with a non-functional src-homology 2 (SH2) domain showed that the SH2 domain is essential for dimer formation of phosphorylated as well as non-phosphorylated Stat3. Furthermore, our data show that visualization of normalized FRET signals allow insights into the spatiotemporal dynamics of Stat3 signal transduction.

Indexed as

Active Transport, Cell NucleusBacterial ProteinsCell LineDimerizationDNA-Binding ProteinsFluorescence Resonance Energy TransferGreen Fluorescent ProteinsHumansLuminescent ProteinsMicroscopy, FluorescenceModels, MolecularRecombinant Fusion ProteinsSTAT3 Transcription FactorTrans-ActivatorsBacterial ProteinsDNA-Binding ProteinsGreen Fluorescent ProteinsLuminescent ProteinsRecombinant Fusion ProteinsSTAT3 protein, humanSTAT3 Transcription FactorTrans-Activatorsyellow fluorescent protein, Bacteria

Identifiers

PMID12974672
PMCPMC1223859
OpenAlexW2051910047

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.