Evidence map›Paper›PMID 18370930›Full record

ArticleThe Biochemical journal2008

Sphingomyelin synthases regulate production of diacylglycerol at the Golgi.

Maristella Villani, Marimuthu Subathra, Yeong-Bin Im, Young Choi, Paola Signorelli, Maurizio Del Poeta, Chiara Luberto

Open access · greenAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

50 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. PI3K Signaling at the Crossroads of Lipid Metabolism and Cancer.Advances in experimental medicine and biology · 2025
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. SiScience · 2023
    Article
  8. Sphingolipids in mitochondria-from function to disease.Frontiers in cell and developmental biology · 2023
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

7 authors at 2 institutions in 2 countries.

Maristella VillaniDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA.
Marimuthu Subathra
Yeong-Bin Im
Young Choi
Paola Signorelli
Maurizio Del Poeta
Chiara Luberto
Medical University of South Carolina · USUniversity of Milan · IT

Funding

THE ROLE OF LACTOSYLCERAMIDE IN RENAL AGING AND DISEASEP20RR017677 · NCRR · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI MAO, CUNGUI · 2002 to 2011
$23.4M
Sphingolipid-mediated fungal pathogenesisR01AI056168 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI DEL POETA, MAURIZIO · 2004 to 2013
$2.7M
Role of phagocytosis in pathogenesis of Cryptococcus neorformansR01AI071142 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI DEL POETA, MAURIZIO · 2008 to 2012
$1.7M
New methods for the early diagnosis of invasive fungal infectionsR21AI078493 · NIAID · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI DEL POETA, MAURIZIO · 2008 to 2009
$406k
Host sphingolipids and fungal infectionR56AI087541 · NIAID · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI HAMA, HIROKO · 2011 to 2011
$383k
NCRR NIH HHS P20 RR-017677NCRR NIH HHS P20 RR017677NIAID NIH HHS R01 AI056168NIAID NIH HHS R01 AI071142NIAID NIH HHS R21 AI078493NIAID NIH HHS R56 AI087541
6 · The paper itself

Abstract

SMS [SM (sphingomyelin) synthase] is a class of enzymes that produces SM by transferring a phosphocholine moiety on to ceramide. PC (phosphatidylcholine) is believed to be the phosphocholine donor of the reaction with consequent production of DAG (diacylglycerol), an important bioactive lipid. In the present study, by modulating SMS1 and SMS2 expression, the role of these enzymes on the elusive regulation of DAG was investigated. Because we found that modulation of SMS1 or SMS2 did not affect total levels of endogenous DAG in resting cells, whereas they produce DAG in vitro, the possibility that SMSs could modulate subcellular pools of DAG, once acute activation of the enzymes is triggered, was investigated. Stimulation of SM synthesis was induced by either treatment with short-chain ceramide analogues or by increasing endogenous ceramide at the plasma membrane, and a fluorescently labelled conventional C1 domain [from PKC (protein kinase C)] enhanced in its DAG binding activity was used to probe subcellular pools of DAG in the cell. With this approach, we found, using confocal microscopy and subcellular fractionation, that modulation of SMS1 and, to a lesser extent, SMS2 affected the formation of DAG at the Golgi apparatus. Similarly, down-regulation of SMS1 and SMS2 reduced the localization of the DAG-binding protein PKD (protein kinase D) to the Golgi. These results provide direct evidence that both enzymes are capable of regulating the formation of DAG in cells, that this pool of DAG is biologically active, and for the first time directly implicate SMS1 and SMS2 as regulators of DAG-binding proteins in the Golgi apparatus.

Indexed as

Cells, CulturedDiglyceridesEnzyme ActivationGolgi ApparatusHeLa CellsHumansMembrane ProteinsNerve Tissue ProteinsProtein BindingTransferases (Other Substituted Phosphate Groups)DiglyceridesMembrane ProteinsNerve Tissue Proteinsphosphatidylcholine-ceramide phosphocholine transferaseSGMS1 protein, humanTransferases (Other Substituted Phosphate Groups)

Identifiers

PMID18370930
PMCPMC5125090
OpenAlexW2027632911

What OpenQuestion holds

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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.