Evidence map›Paper›PMID 20972263›Full record

ArticleThe Journal of biological chemistry2010

Interruption of inositol sphingolipid synthesis triggers Stt4p-dependent protein kinase C signaling.

Stephen A Jesch, Maria L Gaspar, Christopher J Stefan, Manuel A Aregullin, Susan A Henry

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Applied and environmental microbiology · 2019
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Plant-derived antifungal agent poacic acid targets β-1,3-glucan.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. The yeast sphingolipid signaling landscape.Chemistry and physics of lipids · 2014
    Review
  20. The capacity ofFungal biology and biotechnology · 2014
    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

5 authors at 1 institution in 1 country.

Stephen A JeschDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA.
Maria L Gaspar
Christopher J Stefan
Manuel A Aregullin
Susan A Henry
Cornell University · US

Funding

GENETICS AND DEVELOPMENT OF YEAST MEMBRANE MUTANTSR01GM019629 · NIGMS · YESHIVA UNIVERSITY · PI HENRY, SUSAN ARMSTRONG · 1985 to 2015
$6.0M
GENETIC REGULATION OF PHOSPHOLIPID SYNTHESIS IN YEASTR37GM019629 · NIGMS · CORNELL UNIVERSITY ITHACA · PI HENRY, SUSAN A. · 1991 to 2000
$426k
STRUCTURE/FUNCTION ANALYSIS OF PHA4 IN C ELEGANSF32GM019629 · NIGMS · UNIVERSITY OF UTAH · PI KALTENBACH, LINDA S · 1999 to 2001
$59k
NIGMS NIH HHS F32 GM019629NIGMS NIH HHS GM-19629NIGMS NIH HHS R01 GM019629NIGMS NIH HHS R37 GM019629
6 · The paper itself

Abstract

The protein kinase C (PKC)-MAPK signaling cascade is activated and is essential for viability when cells are starved for the phospholipid precursor inositol. In this study, we report that inhibiting inositol-containing sphingolipid metabolism, either by inositol starvation or treatment with agents that block sphingolipid synthesis, triggers PKC signaling independent of sphingoid base accumulation. Under these same growth conditions, a fluorescent biosensor that detects the necessary PKC signaling intermediate, phosphatidylinositol (PI)-4-phosphate (PI4P), is enriched on the plasma membrane. The appearance of the PI4P biosensor on the plasma membrane correlates with PKC activation and requires the PI 4-kinase Stt4p. Like other mutations in the PKC-MAPK pathway, mutants defective in Stt4p and the PI4P 5-kinase Mss4p, which generates phosphatidylinositol 4,5-bisphosphate, exhibit inositol auxotrophy, yet fully derepress INO1, encoding inositol-3-phosphate synthase. These observations suggest that inositol-containing sphingolipid metabolism controls PKC signaling by regulating access of the signaling lipids PI4P and phosphatidylinositol 4,5-bisphosphate to effector proteins on the plasma membrane.

Indexed as

1-Phosphatidylinositol 4-KinaseBiosensing TechniquesCell MembraneEnzyme ActivationGene Expression Regulation, FungalInositolMAP Kinase Signaling SystemPhenotypeProtein Kinase CSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionSphingolipidsTemperatureTime Factors1-Phosphatidylinositol 4-KinaseInositolProtein Kinase CSaccharomyces cerevisiae ProteinsSphingolipidsSTT4 protein, S cerevisiae

Identifiers

PMID20972263
PMCPMC3009921
OpenAlexW2057109887

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.