Evidence map›Paper›PMID 15560753›Full record

ArticleThe Biochemical journal2005

Inositol phosphoceramide synthase is a regulator of intracellular levels of diacylglycerol and ceramide during the G1 to S transition in Saccharomyces cerevisiae.

Jorge Cerbón, Alejandro Falcon, Carlos Hernández-Luna, David Segura-Cobos

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2005. 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
0.5field-weighted citation impact, top 36% 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, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Lipids and Trehalose Actively Cooperate in Heat Stress Management ofInternational journal of molecular sciences · 2021
    Article
  5. Regulation of sphingolipid synthesis by the G1/S transcription factor Swi4.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021
    Article
  6. Article
  7. Lipids in the cell: organisation regulates function.Cellular and molecular life sciences : CMLS · 2018
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Sphingolipid homeostasis in the endoplasmic reticulum and beyond.Cold Spring Harbor perspectives in biology · 2013
    Review
  13. Article
  14. Article
  15. 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

4 authors at 2 institutions in 1 country.

Jorge CerbónDepartment of Biochemistry, Centro de Investigación y de Estudios Avanzados del IPN, 07000 México, D.F., Mexico. jcerbon@mail.cinvestav.mx
Alejandro Falcon
Carlos Hernández-Luna
David Segura-Cobos
Instituto Politécnico Nacional · MXCenter for Research and Advanced Studies of the National Polytechnic Institute · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We recently reported that DAG (diacylglycerol) generated during sphingomyelin synthesis plays an important role in protein kinase C activation and cell proliferation in Madin-Darby canine kidney cells [Cerbon and Lopez-Sanchez (2003) Biochem. J. 373, 917-924]. In yeast cells, IPC (inositol phosphoceramide) synthase catalyses the transfer of phosphoinositol from phosphatidylinositol to ceramide to form IPC and generates DAG. In the present study, we found that, during the G1 to S transition after N2-starvation, there was a significant increase in the synthesis of IPC accompanied by a progressive increase (up to 6-fold) in the level of DAG. The increased DAG levels coincided with decrements in ceramide and sphingoid base levels, conditions that are adequate for the activation of putative protein kinase C required for the G1 to S transition and proliferation of yeast cells. To separate the role of DAG generated during IPC synthesis from that originating from other sources, we utilized beta-chloroalanine and myriocin, inhibitors of serine:palmitoyl-CoA transferase, the first committed step in sphingolipid synthesis, to avoid accumulation of sphingolipid intermediates. When the synthesis of sphingolipids was inhibited, DAG accumulation was significantly decreased and the G1 to S transition was blocked; such blockage was avoided by metabolic complementation with phytosphingosine. The DAG/ceramide ratio was 0.27 and it changed to 2.0 during growth re-initiation, suggesting that the synthesis of phosphosphingolipids could act to switch growth arrest (increased ceramide) to a mitogenic signal (increased DAG), and that this signalling process is preserved in yeast and mammalian cells.

Indexed as

G1 PhaseS Phasebeta-AlanineCell ProliferationCeramidesDepsipeptidesDiglyceridesFatty Acids, MonounsaturatedHexosyltransferasesPhospholipidsProtein Kinase CSaccharomyces cerevisiaeSignal TransductionSphingolipids3-chloroalanineaureobasidin Abeta-AlanineCeramidesDepsipeptidesDiglyceridesFatty Acids, MonounsaturatedHexosyltransferasesphosphatidylinositol-ceramide phosphoinositol transferasePhospholipidsProtein Kinase CSphingolipidsthermozymocidin

Identifiers

PMID15560753
PMCPMC1186705
OpenAlexW2101435004

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.