Evidence map›Paper›PMID 19168031›Full record

ArticleBiochemical and biophysical research communications2009

A lipid binding domain in sphingosine kinase 2.

Anthony S Don, Hugh Rosen

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Review
  3. Classification of domains in predicted structures of the human proteome.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Sphingolipids and mitochondrial apoptosis.Journal of bioenergetics and biomembranes · 2016
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Roles of sphingosine 1-phosphate on tumorigenesis.World journal of biological chemistry · 2011
    Article
  19. Article
  20. Sphingosine 1-phosphate and cancer.Nature reviews. Cancer · 2010
    Review
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 2 institutions in 2 countries.

Anthony S DonCancer Research Centre, Faculty of Medicine, University of New South Wales, Sydney, NSW, Australia.
Hugh Rosen
Scripps Research Institute · USUNSW Sydney · AU

Funding

Scripps Research Institute Molecular Screen Center(RMI)U54MH074404 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI ROSEN, HUGH · 2005 to 2007
$11.6M
S1P Receptor subtypes: Regulating lymphocyte traffickingR01AI055509 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI ROSEN, HUGH · 2004 to 2008
$2.3M
NIAID NIH HHS AI055509NIAID NIH HHS R01 AI055509NIMH NIH HHS MH-074404NIMH NIH HHS U54 MH074404
6 · The paper itself

Abstract

The lipid second messenger sphingosine 1-phosphate (S1P) is a critical mediator of cellular proliferation and survival signals, and is essential for vasculogenesis and neurogenesis. S1P formation is catalysed by sphingosine kinases 1 and 2 (Sphk1 and Sphk2). We have found that the endogenous glycolipid sulfatide (3-O-sulfogalactosylceramide) binds to and inhibits the activity of Sphk2 and the closely related ceramide kinase (Cerk), but not Sphk1. Using sulfatide as a probe, we mapped the lipid binding domain to the N-terminus of Sphk2 (residues 1-175), a region of sequence that is absent in Sphk1, but aligns with a pleckstrin homology domain in Cerk. Accordingly, Sphk2 bound to phosphatidylinositol monophosphates but not to abundant cellular phospholipids. Deleting the N-terminal domain reduced Sphk2 membrane localisation in cells. We have therefore identified a lipid binding domain in Sphk2 that is important for the enzyme's sub-cellular localisation.

Indexed as

Catalytic DomainCell LineCell MembraneHumansPhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)Protein Structure, TertiarySphingosine KinaseSulfoglycosphingolipidsceramide kinasePhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)Sphingosine KinaseSulfoglycosphingolipids

Identifiers

PMID19168031
PMCPMC2657340
OpenAlexW2084296106

What OpenQuestion holds

Textmetadata
LicenceTDM
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.