Evidence map›Paper›PMID 37794019›Full record

ArticleNature communications2023

Structure of the ceramide-bound SPOTS complex.

Jan-Hannes Schäfer, Carolin Körner, Bianca M Esch, Sergej Limar, Kristian Parey, Stefan Walter, Dovile Januliene, Arne Moeller, Florian Fröhlich

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. ORMDL Proteins Turnover via Proteasome and Autophagy Is Cell-Type Dependent and Tied to Ceramide Homeostasis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Structure of the yeast ceramide synthase.Nature structural & molecular biology · 2025
    Article
  15. Review
  16. The Dsc complex and its role in Golgi quality control.Biochemical Society transactions · 2024
    Review
  17. Regulation of cellular and systemic sphingolipid homeostasis.Nature reviews. Molecular cell biology · 2024
    Review
  18. Article
  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

9 authors at 1 institution in 1 country.

Jan-Hannes Schäfer *Osnabrück University Department of Biology/Chemistry Structural Biology section, 49076, Osnabrück, Germany.ORCID 0000-0001-8163-1629
Carolin Körner *Osnabrück University Department of Biology/Chemistry Bioanalytical Chemistry section, 49076, Osnabrück, Germany.
Bianca M EschOsnabrück University Department of Biology/Chemistry Bioanalytical Chemistry section, 49076, Osnabrück, Germany.
Sergej LimarOsnabrück University Department of Biology/Chemistry Bioanalytical Chemistry section, 49076, Osnabrück, Germany.
Kristian PareyOsnabrück University Department of Biology/Chemistry Structural Biology section, 49076, Osnabrück, Germany.ORCID 0000-0002-4842-6479
Stefan WalterOsnabrück University Center of Cellular Nanoanalytic Osnabrück (CellNanOs), 49076, Osnabrück, Germany.ORCID 0000-0002-8797-3184
Dovile JanulieneOsnabrück University Department of Biology/Chemistry Structural Biology section, 49076, Osnabrück, Germany. dovile.januliene@uos.de.ORCID 0000-0002-3279-7590
Arne MoellerOsnabrück University Department of Biology/Chemistry Structural Biology section, 49076, Osnabrück, Germany. arne.moeller@uos.de.ORCID 0000-0003-1101-5366
Florian FröhlichOsnabrück University Department of Biology/Chemistry Bioanalytical Chemistry section, 49076, Osnabrück, Germany. florian.froehlich@uos.de.ORCID 0000-0001-8307-2189
Osnabrück University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sphingolipids are structural membrane components that also function in cellular stress responses. The serine palmitoyltransferase (SPT) catalyzes the rate-limiting step in sphingolipid biogenesis. Its activity is tightly regulated through multiple binding partners, including Tsc3, Orm proteins, ceramides, and the phosphatidylinositol-4-phosphate (PI4P) phosphatase Sac1. The structural organization and regulatory mechanisms of this complex are not yet understood. Here, we report the high-resolution cryo-EM structures of the yeast SPT in complex with Tsc3 and Orm1 (SPOT) as dimers and monomers and a monomeric complex further carrying Sac1 (SPOTS). In all complexes, the tight interaction of the downstream metabolite ceramide and Orm1 reveals the ceramide-dependent inhibition. Additionally, observation of ceramide and ergosterol binding suggests a co-regulation of sphingolipid biogenesis and sterol metabolism within the SPOTS complex.

Indexed as

CeramidesSaccharomyces cerevisiae ProteinsProteinsSaccharomyces cerevisiaeSerine C-PalmitoyltransferaseSphingolipidsCeramidesOrm1 protein, S cerevisiaeProteinsSaccharomyces cerevisiae ProteinsSerine C-PalmitoyltransferaseSphingolipids

Identifiers

PMID37794019
PMCPMC10550967
OpenAlexW4387330425

What OpenQuestion holds

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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.