Evidence map›Paper›PMID 11494123›Full record

ArticleOncogene2001

Protein phosphatases 1 and 2A promote Raf-1 activation by regulating 14-3-3 interactions.

M Jaumot, J F Hancock

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

87 citing papers in PubMed, 196 citations in OpenAlex.

  1. Article
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  5. CRABP1-complexes in exosome secretion.Cell communication and signaling : CCS · 2024
    Article
  6. Article
  7. Review
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  10. Article
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  12. The phosphatase/kinase balance affects phytochrome A and its native pools, phyA' and phyA″, in etiolated maize roots: evidence from the induction of phyA' destruction by a protein phosphatase inhibitor sodium fluoride.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021
    Article
  13. Review
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  15. Review
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  17. Article
  18. Article
  19. Review
  20. Frontiers in cell and developmental biology · 2020
    Article

27 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

M JaumotLaboratory of Experimental Oncology, Department of Pathology, University of Queensland Medical School, Herston Road, Queensland 4006, Australia.
J F Hancock
University of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Raf-1 activation is a complex process which involves plasma membrane recruitment, phosphorylation, protein-protein and lipid-protein interactions. We now show that PP1 and PP2A serine-threonine phosphatases also have a positive role in Ras dependent Raf-1 activation. General serine-threonine phosphatase inhibitors such sodium fluoride, or ss-glycerophosphate and sodium pyrophosphate, or specific PP1 and PP2A inhibitors including microcystin-LR, protein phosphatase 2A inhibitor I(1) or protein phosphatase inhibitor 2 all abrogate H-Ras and K-Ras dependent Raf-1 activation in vitro. A critical Raf-1 target residue for PP1 and PP2A is S259. Serine phosphatase inhibitors block the dephosphorylation of S259, which accompanies Raf-1 activation, and Ras dependent activation of mutant Raf259A is relatively resistant to serine phosphatase inhibitors. Sucrose gradient analysis demonstrates that serine phosphatase inhibition increases the total amount of 14-3-3 and Raf-1 associated with the plasma membrane and significantly alters the distribution of 14-3-3 and Raf-1 across different plasma membrane microdomains. These observations suggest that dephosphorylation of S259 is a critical early step in Ras dependent Raf-1 activation which facilitates 14-3-3 displacement. Inhibition of PP1 and PP2A therefore causes plasma membrane accumulation of Raf-1/14-3-3 complexes which cannot be activated.

Indexed as

Carrier ProteinsIntracellular Signaling Peptides and Proteins14-3-3 ProteinsAmino Acid SubstitutionAnimalsBinding SitesCell MembraneChlorocebus aethiopsCOS CellsDiphosphatesEnzyme ActivationEnzyme InhibitorsGenes, rasGlycerophosphatesIsoenzymesMacromolecular Substances14-3-3 Proteinsbeta-glycerophosphoric acidCarrier Proteinscyanoginosin LRDiphosphatesEnzyme InhibitorsGlycerophosphatesIntracellular Signaling Peptides and ProteinsIsoenzymesMacromolecular SubstancesMarine ToxinsMicrocystinsPeptides, CyclicPhosphoprotein PhosphatasesProtein Phosphatase 2protein phosphatase inhibitor-1protein phosphatase inhibitor-2Protein Phosphatase Inhibitory ProteinsProteinsProto-Oncogene Proteins c-rafProto-Oncogene Proteins p21(ras)RNA-Binding ProteinsSodium Fluoridesodium pyrophosphateTyrosine 3-Monooxygenase

Identifiers

PMID11494123
OpenAlexW2009516619

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.