Evidence map›Paper›PMID 37953642›Full record

ArticleThe EMBO journal2023

Structure and mechanism of a eukaryotic ceramide synthase complex.

Tian Xie, Qi Fang, Zike Zhang, Yanfei Wang, Feitong Dong, Xin Gong

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
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  4. Review
  5. Review
  6. Review
  7. IGFBP2-Ceramide Pathway Mediates Divergent Myelin Breakdown in the PNS and CNS Following Injury.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Structure of the yeast ceramide synthase.Nature structural & molecular biology · 2025
    Article
  13. Article
  14. Article
  15. Magnolol Inhibits the Growth ofThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2025
    Article
  16. Article
  17. 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

6 authors at 1 institution in 1 country.

Tian Xie *Department of Chemical Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, China.ORCID 0000-0002-5445-664X
Qi Fang *Department of Chemical Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, China.ORCID 0009-0005-7581-0184
Zike ZhangDepartment of Chemical Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, China.ORCID 0000-0002-9799-1634
Yanfei WangDepartment of Chemical Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, China.
Feitong DongDepartment of Chemical Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, China.ORCID 0000-0001-8315-7086
Xin GongDepartment of Chemical Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, China.ORCID 0000-0003-3469-7718
Southern University of Science and Technology · CN

Funding

Guangdong Basic and Applied Basic Research Foundation 2019B151502047MOST | National Natural Science Foundation of China (NSFC) 32122043MOST | National Natural Science Foundation of China (NSFC) 92057101Shenzhen Science and Technology Program 20220815111002002Shenzhen Science and Technology Program RCYX20200714114522081
6 · The paper itself

Abstract

Ceramide synthases (CerS) catalyze ceramide formation via N-acylation of a sphingoid base with a fatty acyl-CoA and are attractive drug targets for treating numerous metabolic diseases and cancers. Here, we present the cryo-EM structure of a yeast CerS complex, consisting of a catalytic Lac1 subunit and a regulatory Lip1 subunit, in complex with C26-CoA substrate. The CerS holoenzyme exists as a dimer of Lac1-Lip1 heterodimers. Lac1 contains a hydrophilic reaction chamber and a hydrophobic tunnel for binding the CoA moiety and C26-acyl chain of C26-CoA, respectively. Lip1 interacts with both the transmembrane region and the last luminal loop of Lac1 to maintain the proper acyl chain binding tunnel. A lateral opening on Lac1 serves as a potential entrance for the sphingoid base substrate. Our findings provide a template for understanding the working mechanism of eukaryotic ceramide synthases and may facilitate the development of therapeutic CerS modulators.

Indexed as

CeramidesSaccharomyces cerevisiae ProteinsMembrane ProteinsOxidoreductasesSaccharomyces cerevisiaeCeramidesdihydroceramide desaturaseLip1 protein, S cerevisiaeMembrane ProteinsOxidoreductasesSaccharomyces cerevisiae Proteinsceramideceramide synthasecryo-EMLac1Lip1

Identifiers

PMID37953642
PMCPMC10711658
OpenAlexW4388635351

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.