Evidence map›Paper›PMID 23593226›Full record

ArticlePloS one2013

The yeast oxysterol binding protein Kes1 maintains sphingolipid levels.

Marissa A LeBlanc, Gregory D Fairn, Sarah B Russo, Ola Czyz, Vanina Zaremberg, L Ashley Cowart, Christopher R McMaster

Abstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. 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.

Marissa A LeBlancDepartment of Pathology, Dalhousie University, Halifax, Nova Scotia, Canada.
Gregory D Fairn
Sarah B Russo
Ola Czyz
Vanina Zaremberg
L Ashley Cowart
Christopher R McMaster

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

The oxysterol binding protein family are amphitropic proteins that bind oxysterols, sterols, and possibly phosphoinositides, in a conserved binding pocket. The Saccharomyces cerevisiae oxysterol binding protein family member Kes1 (also known as Osh4) also binds phosphoinositides on a distinct surface of the protein from the conserved binding pocket. In this study, we determine that the oxysterol binding protein family member Kes1 is required to maintain the ratio of complex sphingolipids and levels of ceramide, sphingosine-phosphate and sphingosine. This inability to maintain normal sphingolipid homeostasis resulted in misdistribution of Pma1, a protein that requires normal sphingolipid synthesis to occur to partition into membrane rafts at the Golgi for its trafficking to the plasma membrane.

Indexed as

Cell MembraneCeramidesGolgi ApparatusMembrane ProteinsOxysterol Binding ProteinsProtein TransportProton-Translocating ATPasesReceptors, SteroidSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSphingolipidsCeramidesKES1 protein, S cerevisiaeMembrane ProteinsOxysterol Binding ProteinsPMA1 protein, S cerevisiaeProton-Translocating ATPasesReceptors, SteroidSaccharomyces cerevisiae ProteinsSphingolipids

Identifiers

PMID23593226
PMCPMC3617146

What OpenQuestion holds

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LicenceCC BY
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.