Evidence map›Paper›PMID 9891076›Full record

ArticleMolecular and cellular biology1999

Regulation of ribosomal S6 protein kinase-p90(rsk), glycogen synthase kinase 3, and beta-catenin in early Xenopus development.

M A Torres, H Eldar-Finkelman, E G Krebs, R T Moon

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

16 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Review
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  6. Time-varying causal inference from phosphoproteomic measurements in macrophage cells.IEEE transactions on biomedical circuits and systems · 2014
    Article
  7. Review
  8. Article
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  11. Development of the upper lip: morphogenetic and molecular mechanisms.Developmental dynamics : an official publication of the American Association of Anatomists · 2006
    Review
  12. Article
  13. Review
  14. 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

4 authors at 2 institutions in 1 country.

M A TorresHoward Hughes Medical Institute and Department of Pharmacology, University of Washington School of Medicine, Seattle, Washington, USA.
H Eldar-Finkelman
E G Krebs
R T Moon
Howard Hughes Medical Institute · USUniversity of Washington · US

Funding

LINKING OF PROTEIN TYROSINE AND SERINE PHOSPHORYLATIONR01DK042528 · NIDDK · UNIVERSITY OF WASHINGTON · PI KREBS, EDWIN G. · 1990 to 1999
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NIDDK NIH HHS DK-42528
6 · The paper itself

Abstract

beta-Catenin is a multifunctional protein that binds cadherins at the plasma membrane, HMG box transcription factors in the nucleus, and several cytoplasmic proteins that are involved in regulating its stability. In developing embryos and in some human cancers, the accumulation of beta-catenin in the cytoplasm and subsequently the nuclei of cells may be regulated by the Wnt-1 signaling cascade and by glycogen synthase kinase 3 (GSK-3). This has increased interest in regulators of both GSK-3 and beta-catenin. Searching for kinase activities able to phosphorylate the conserved, inhibitory-regulatory GSK-3 residue serine 9, we found p90(rsk) to be a potential upstream regulator of GSK-3. Overexpression of p90(rsk) in Xenopus embryos leads to increased steady-state levels of total beta-catenin but not of the free soluble protein. Instead, p90(rsk) overexpression increases the levels of beta-catenin in a cell fraction containing membrane-associated cadherins. Consistent with the lack of elevation of free beta-catenin levels, ectopic p90(rsk) was unable to rescue dorsal cell fate in embryos ventralized by UV irradiation. We show that p90(rsk) is a downstream target of fibroblast growth factor (FGF) signaling during early Xenopus development, since ectopic FGF signaling activates both endogenous and overexpressed p90(rsk). Moreover, overexpression of a dominant negative FGF receptor, which blocks endogenous FGF signaling, leads to decreased p90(rsk) kinase activity. Finally, we report that FGF inhibits endogenous GSK-3 activity in Xenopus embryos. We hypothesize that FGF and p90(rsk) play heretofore unsuspected roles in modulating GSK-3 and beta-catenin.

Indexed as

Trans-ActivatorsAnimalsbeta CateninCalcium-Calmodulin-Dependent Protein KinasesCytoskeletal ProteinsFemaleFibroblast Growth FactorsGene Expression Regulation, DevelopmentalGene Expression Regulation, EnzymologicGlycogen Synthase Kinase 3Glycogen Synthase KinasesHumansIn Vitro TechniquesRibosomal Protein S6 KinasesSignal TransductionXenopusbeta CateninCalcium-Calmodulin-Dependent Protein KinasesCTNNB1 protein, humanCTNNB1 protein, XenopusCytoskeletal ProteinsFibroblast Growth FactorsGlycogen Synthase Kinase 3Glycogen Synthase KinasesRibosomal Protein S6 KinasesTrans-ActivatorsXenopus Proteins

Identifiers

PMID9891076
PMCPMC116071
OpenAlexW2098595332

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.