Evidence map›Paper›PMID 15270698›Full record

ArticleThe Biochemical journal2004

Identification and biophysical characterization of a very-long-chain-fatty-acid-substituted phosphatidylinositol in yeast subcellular membranes.

Roger Schneiter, Britta Brügger, Clare M Amann, Glenn D Prestwich, Raquel F Epand, Günther Zellnig, Felix T Wieland, Richard M Epand

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

44 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
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  3. The MoLfa1 Protein Regulates Fungal Development and Septin Ring Formation inInternational journal of molecular sciences · 2024
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  8. Synthesis of Dolichols inInternational journal of molecular sciences · 2021
    Article
  9. Lipids and Trehalose Actively Cooperate in Heat Stress Management ofInternational journal of molecular sciences · 2021
    Article
  10. Article
  11. Article
  12. Phospholipid turnover and acyl chain remodeling in the yeast ER.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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

8 authors at 4 institutions in 4 countries.

Roger SchneiterDivision of Biochemistry, Department of Medicine, University of Fribourg, Chemin du Musee 5, CH-1700 Fribourg, Switzerland. roger.schneiter@unifr.ch
Britta Brügger
Clare M Amann
Glenn D Prestwich
Raquel F Epand
Günther Zellnig
Felix T Wieland
Richard M Epand
Heidelberg University · DEMcMaster University · CAUniversity of Fribourg · CHUniversity of Graz · AT

Funding

Phosphoinositide and Inositol Polyphosphate ProbesR01NS029632 · NINDS · UNIVERSITY OF UTAH · PI PRESTWICH, GLENN DOWNES · 1992 to 2007
$2.5M
NINDS NIH HHS R01 NS029632
6 · The paper itself

Abstract

Morphological analysis of a conditional yeast mutant in acetyl-CoA carboxylase acc1ts/mtr7, the rate-limiting enzyme of fatty acid synthesis, suggested that the synthesis of C26 VLCFAs (very-long-chain fatty acids) is important for maintaining the structure and function of the nuclear membrane. To characterize this C26-dependent pathway in more detail, we have now examined cells that are blocked in pathways that require C26. In yeast, ceramide synthesis and remodelling of GPI (glycosylphosphatidylinositol)-anchors are two pathways that incorporate C26 into lipids. Conditional mutants blocked in either ceramide synthesis or the synthesis of GPI anchors do not display the characteristic alterations of the nuclear envelope observed in acc1ts, indicating that the synthesis of another C26-containing lipid may be affected in acc1ts mutant cells. Lipid analysis of isolated nuclear membranes revealed the presence of a novel C26-substituted PI (phosphatidylinositol). This C26-PI accounts for approx. 1% of all the PI species, and is present in both the nuclear and the plasma membrane. Remarkably, this C26-PI is the only C26-containing glycerophospholipid that is detectable in wild-type yeast, and the C26-substitution is highly specific for the sn-1 position of the glycerol backbone. To characterize the biophysical properties of this lipid, it was chemically synthesized. In contrast to PIs with normal long-chain fatty acids (C16 or C18), the C26-PI greatly reduced the bilayer to hexagonal phase transition of liposomes composed of 1,2-dielaidoyl-sn-glycero-3-phosphoethanolamine (DEPE). The biophysical properties of this lipid are thus consistent with a possible role in stabilizing highly curved membrane domains.

Indexed as

AcyltransferasesCeramidesFatty AcidsGlycosylphosphatidylinositolsIntracellular MembranesLipidsMass SpectrometryModels, MolecularNuclear EnvelopePhosphatidylinositolsSaccharomyces cerevisiaeSerine C-Palmitoyltransferase1-O-hexacosanoyl-2-O-palmitoylphosphatidylinositolAcyltransferasesCeramidesFatty AcidsGlycosylphosphatidylinositolsLipidsPhosphatidylinositolsSerine C-Palmitoyltransferase

Identifiers

PMID15270698
PMCPMC1133906
OpenAlexW2100088060

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.