Evidence map›Paper›PMID 27100999›Full record

ArticlePloS one2016

Sphingosine-1-Phosphate Lyase Deficient Cells as a Tool to Study Protein Lipid Interactions.

Mathias J Gerl, Verena Bittl, Susanne Kirchner, Timo Sachsenheimer, Hanna L Brunner, Christian Lüchtenborg, Cagakan Özbalci, Hannah Wiedemann, Sabine Wegehingel, Walter Nickel and 4 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Lipid Sorting and Organelle Identity.Cold Spring Harbor perspectives in biology · 2023
    Review
  5. Article
  6. Lysosome-targeted multifunctional lipid probes reveal the sterol transporter NPC1 as a sphingosine interactor.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Sphingosine-1-phosphate lyase (SGPL1) deficiency is associated with mitochondrial dysfunction.The Journal of steroid biochemistry and molecular biology · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Visualizing bioactive ceramides.Chemistry and physics of lipids · 2018
    Review
  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

14 authors at 3 institutions in 1 country.

Mathias J GerlHeidelberg University Biochemistry Center, Heidelberg, Germany.
Verena BittlHeidelberg University Biochemistry Center, Heidelberg, Germany.
Susanne KirchnerHeidelberg University Biochemistry Center, Heidelberg, Germany.
Timo SachsenheimerHeidelberg University Biochemistry Center, Heidelberg, Germany.
Hanna L BrunnerHeidelberg University Biochemistry Center, Heidelberg, Germany.
Christian LüchtenborgHeidelberg University Biochemistry Center, Heidelberg, Germany.
Cagakan ÖzbalciHeidelberg University Biochemistry Center, Heidelberg, Germany.
Hannah WiedemannHeidelberg University Biochemistry Center, Heidelberg, Germany.
Sabine WegehingelHeidelberg University Biochemistry Center, Heidelberg, Germany.
Walter NickelHeidelberg University Biochemistry Center, Heidelberg, Germany.
Per HaberkantEuropean Molecular Biology Laboratory, Heidelberg, Germany.
Carsten SchultzEuropean Molecular Biology Laboratory, Heidelberg, Germany.
Marcus KrügerCECAD, Cologne, Germany.
Britta BrüggerHeidelberg University Biochemistry Center, Heidelberg, Germany.
Heidelberg University · DEEuropean Molecular Biology Laboratory · DECologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell membranes contain hundreds to thousands of individual lipid species that are of structural importance but also specifically interact with proteins. Due to their highly controlled synthesis and role in signaling events sphingolipids are an intensely studied class of lipids. In order to investigate their metabolism and to study proteins interacting with sphingolipids, metabolic labeling based on photoactivatable sphingoid bases is the most straightforward approach. In order to monitor protein-lipid-crosslink products, sphingosine derivatives containing a reporter moiety, such as a radiolabel or a clickable group, are used. In normal cells, degradation of sphingoid bases via action of the checkpoint enzyme sphingosine-1-phosphate lyase occurs at position C2-C3 of the sphingoid base and channels the resulting hexadecenal into the glycerolipid biosynthesis pathway. In case the functionalized sphingosine looses the reporter moiety during its degradation, specificity towards sphingolipid labeling is maintained. In case degradation of a sphingosine derivative does not remove either the photoactivatable or reporter group from the resulting hexadecenal, specificity towards sphingolipid labeling can be achieved by blocking sphingosine-1-phosphate lyase activity and thus preventing sphingosine derivatives to be channeled into the sphingolipid-to-glycerolipid metabolic pathway. Here we report an approach using clustered, regularly interspaced, short palindromic repeats (CRISPR)-associated nuclease Cas9 to create a sphingosine-1-phosphate lyase (SGPL1) HeLa knockout cell line to disrupt the sphingolipid-to-glycerolipid metabolic pathway. We found that the lipid and protein compositions as well as sphingolipid metabolism of SGPL1 knock-out HeLa cells only show little adaptations, which validates these cells as model systems to study transient protein-sphingolipid interactions.

Indexed as

Lipid MetabolismAldehyde-LyasesAnimalsCells, CulturedChromatography, Thin LayerClustered Regularly Interspaced Short Palindromic RepeatsGene Knockdown TechniquesHeLa CellsHumansMiceProtein BindingProteinsAldehyde-LyasesProteinssphingosine 1-phosphate lyase (aldolase)

Identifiers

PMID27100999
PMCPMC4839656
OpenAlexW2342228129

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.