Evidence map›Paper›PMID 18852266›Full record

ArticleThe Journal of biological chemistry2008

Deactivation of sphingosine kinase 1 by protein phosphatase 2A.

Renae K Barr, Helen E Lynn, Paul A B Moretti, Yeesim Khew-Goodall, Stuart M Pitson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. FTY720 Inhibits Expansion of Breast Cancer Stem Cells via PP2A Activation.International journal of molecular sciences · 2021
    Article
  6. Article
  7. Molecular mechanisms of regulation of sphingosine kinase 1.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2018
    Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Sphingosine kinase 1 isoform-specific interactions in breast cancer.Molecular endocrinology (Baltimore, Md.) · 2014
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

5 authors at 1 institution in 1 country.

Renae K BarrHanson Institute, Division of Human Immunology, Institute of Medical and Veterinary Science, University of Adelaide, Adelaide, Australia.
Helen E Lynn
Paul A B Moretti
Yeesim Khew-Goodall
Stuart M Pitson
Hanson Institute · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sphingosine kinase 1 (SK1) is an important regulator of cellular signaling that has been implicated in a broad range of cellular processes. Cell exposure to a wide array of growth factors, cytokines, and other cell agonists can result in a rapid and transient increase in SK activity via an activating phosphorylation. We have previously identified extracellular signal-regulated kinases 1 and 2 (ERK1/2) as the kinases responsible for the phosphorylation of human SK1 at Ser(225), but the corresponding phosphatase targeting this phosphorylation has remained undefined. Here, we provide data to support a role for protein phosphatase 2A (PP2A) in the deactivation of SK1 through dephosphorylation of phospho-Ser(225). The catalytic subunit of PP2A (PP2Ac) was found to interact with SK1 using both GST-pulldown and coimmunoprecipitation analyses. Coexpression of PP2Ac with SK1 resulted in reduced Ser(225) phosphorylation of SK1 in human embryonic kidney (HEK293) cells. In vitro phosphatase assays showed that PP2Ac dephosphorylated both recombinant SK1 and a phosphopeptide based on the phospho-Ser(225) region of SK1. Finally, both basal and tumor necrosis factor-alpha-stimulated cellular SK1 activity were regulated by molecular manipulation of PP2Ac activity. Thus, PP2A appears to function as an endogenous regulator of SK1 phosphorylation.

Indexed as

AnimalsEnzyme ActivationExtracellular Signal-Regulated MAP KinasesGene SilencingGlutathione TransferaseHumansMuscle, SkeletalPhosphorylationPhosphotransferases (Alcohol Group Acceptor)Protein Phosphatase 2Protein Structure, TertiaryRabbitsSerineSphingosine KinaseSubcellular FractionsTumor Necrosis Factor-alphaExtracellular Signal-Regulated MAP KinasesGlutathione TransferasePhosphotransferases (Alcohol Group Acceptor)Protein Phosphatase 2SerineSphingosine KinaseTumor Necrosis Factor-alpha

Identifiers

PMID18852266
PMCPMC3259904
OpenAlexW1996785365

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.