Evidence map›Paper›PMID 38388831›Full record

ArticleNature structural & molecular biology2024

Cryo-EM structure of human sphingomyelin synthase and its mechanistic implications for sphingomyelin synthesis.

Kexin Hu, Qing Zhang, Yang Chen, Jintong Yang, Ying Xia, Bing Rao, Shaobai Li, Yafeng Shen, Mi Cao, Hongliang Lu and 6 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Sphingolipids and Atherosclerosis.Current atherosclerosis reports · 2026
    Review
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  5. Review
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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

16 authors at 4 institutions in 2 countries.

Kexin Hu *Institute of Precision Medicine, the Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Qing Zhang *Department of Orthopaedics, Shanghai Key Laboratory of Orthopaedic Implant, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Yang Chen *Institute of Precision Medicine, the Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Jintong Yang *Department of Medicinal Chemistry, School of Pharmacy, Fudan University, Shanghai, China.
Ying XiaInstitute of Precision Medicine, the Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Bing RaoInstitute of Precision Medicine, the Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Shaobai LiInstitute of Precision Medicine, the Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Yafeng ShenInstitute of Precision Medicine, the Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Mi CaoInstitute of Precision Medicine, the Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Hongliang LuCollege of Basic Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
An QinDepartment of Orthopaedics, Shanghai Key Laboratory of Orthopaedic Implant, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.ORCID http://orcid.org/0000-0002-8785-8848
Xian-Cheng JiangDepartment of Cell Biology, State University of New York Downstate Health Sciences University, Brooklyn, NY, USA.
Deqiang YaoInstitute of Precision Medicine, the Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China. yaodeqiang@renji.com.ORCID http://orcid.org/0000-0003-4881-265X
Jie ZhaoDepartment of Orthopaedics, Shanghai Key Laboratory of Orthopaedic Implant, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China. profzhaojie@126.com.ORCID http://orcid.org/0000-0003-1000-5641
Lu ZhouDepartment of Medicinal Chemistry, School of Pharmacy, Fudan University, Shanghai, China. zhoulu@fudan.edu.cn.ORCID http://orcid.org/0000-0002-6807-2647
Yu CaoInstitute of Precision Medicine, the Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China. yu.cao@shsmu.edu.cn.ORCID http://orcid.org/0000-0003-1409-2068
Shanghai Jiao Tong University · CNFudan University · CNMemorial Sloan Kettering Cancer Center · USState University of New York · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sphingomyelin (SM) has key roles in modulating mammalian membrane properties and serves as an important pool for bioactive molecules. SM biosynthesis is mediated by the sphingomyelin synthase (SMS) family, comprising SMS1, SMS2 and SMS-related (SMSr) members. Although SMS1 and SMS2 exhibit SMS activity, SMSr possesses ceramide phosphoethanolamine synthase activity. Here we determined the cryo-electron microscopic structures of human SMSr in complexes with ceramide, diacylglycerol/phosphoethanolamine and ceramide/phosphoethanolamine (CPE). The structures revealed a hexameric arrangement with a reaction chamber located between the transmembrane helices. Within this structure, a catalytic pentad E-H/D-H-D was identified, situated at the interface between the lipophilic and hydrophilic segments of the reaction chamber. Additionally, the study unveiled the two-step synthesis process catalyzed by SMSr, involving PE-PLC (phosphatidylethanolamine-phospholipase C) hydrolysis and the subsequent transfer of the phosphoethanolamine moiety to ceramide. This research provides insights into the catalytic mechanism of SMSr and expands our understanding of sphingolipid metabolism.

Indexed as

Cryoelectron MicroscopyModels, MolecularSphingomyelinsTransferases (Other Substituted Phosphate Groups)CeramidesDiglyceridesEthanolaminesHumansMembrane ProteinsNerve Tissue ProteinsPhosphatidylethanolaminesceramide phosphoethanolamineCeramidesDiglyceridesEthanolaminesMembrane ProteinsNerve Tissue Proteinsphosphatidylcholine-ceramide phosphocholine transferasePhosphatidylethanolaminesphosphorylethanolamineSGMS1 protein, humanSphingomyelinsTransferases (Other Substituted Phosphate Groups)

Identifiers

PMID38388831
OpenAlexW4392058194

What OpenQuestion holds

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Registered trials

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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.