Evidence map›Paper›PMID 9199300›Full record

ArticleMolecular and cellular biology1997

Comparison of the transactivation domains of Stat5 and Stat6 in lymphoid cells and mammary epithelial cells.

R Moriggl, S Berchtold, K Friedrich, G J Standke, W Kammer, M Heim, M Wissler, E Stöcklin, F Gouilleux, B Groner

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

28 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Redox Regulation of STAT1 and STAT3 Signaling.International journal of molecular sciences · 2020
    Review
  6. Article
  7. Review
  8. Transcriptional regulation by STAT6.Immunologic research · 2011
    Review
  9. Article
  10. Article
  11. Article
  12. Selective potentiation of Stat-dependent gene expression by collaborator of Stat6 (CoaSt6), a transcriptional cofactor.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  13. Article
  14. The DNA replication factor MCM5 is essential for Stat1-mediated transcriptional activation.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  15. Article
  16. Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphorylation in response to IFN-gamma.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

10 authors at 5 institutions in 6 countries.

R MorigglTumor Biology Center, and Dept. of Biology, University of Freiburg, Germany.
S Berchtold
K Friedrich
G J Standke
W Kammer
M Heim
M Wissler
E Stöcklin
F Gouilleux
B Groner
University of Freiburg · DEInstitut für ökologische Wirtschaftsforschung · ATInserm · FRNovartis (Switzerland) · CHUniversity Medical Center Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Stat (signal transducers and activators of transcription) and Jak (Janus kinases) proteins are central components in the signal transduction events in hematopoietic and epithelial cells. They are rapidly activated by various cytokines, hormones, and growth factors. Upon ligand binding and cytokine receptor dimerization, Stat proteins are phosphorylated on tyrosine residues by Jak kinases. Activated Stat proteins form homo- or heterodimers, translocate to the nucleus, and induce transcription from responsive genes. Stat5 and Stat6 are transcription factors active in mammary epithelial cells and immune cells. Prolactin activates Stat5, and interleukin-4 (IL-4) activates Stat6. Both cytokines are able to stimulate cell proliferation, differentiation, and survival. We investigated the transactivation potential of Stat6 and found that it is not restricted to lymphocytes. IL-4-dependent activation of Stat6 was also observed in HC11 mammary epithelial cells. In these cells, Stat6 activation led to the induction of the beta-casein gene promoter. The induction of this promoter was confirmed in COS7 cells. The glucocorticoid receptor was able to further enhance IL-4-induced gene transcription through the action of Stat6. Deletion analysis of the carboxyl-terminal region of Stat6 and recombination of this region with a heterologous DNA binding domain allowed the delimitation and characterization of the transactivation domain of Stat6. The potencies of the transactivation domains of Stat5, Stat6, and viral protein VP16 were compared. Stat6 had a transactivation domain which was about 10-fold stronger than that of Stat5. In pre-B cells (Ba/F3), the transactivation domain of Stat6 was IL-4 regulated, independently from its DNA binding function.

Indexed as

Milk ProteinsAmino Acid SequenceAnimalsCaseinsCells, CulturedDNA-Binding ProteinsEpitheliumGene Expression RegulationHumansImmediate-Early ProteinsInterleukin-4LymphocytesMammary Glands, AnimalMiceMolecular Sequence DataOncostatin MCaseinsDNA-Binding ProteinsImmediate-Early ProteinsInterleukin-4Milk ProteinsOncostatin MOSM protein, humanOsm protein, mousePeptidesProlactinReceptors, GlucocorticoidSTAT5 Transcription FactorSTAT6 protein, humanStat6 protein, mouseSTAT6 Transcription FactorSuppressor of Cytokine Signaling ProteinsTrans-Activators

Identifiers

PMID9199300
PMCPMC232218
OpenAlexW2120464397

What OpenQuestion holds

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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.