Evidence map›Paper›PMID 21689253›Full record

ArticleTraffic (Copenhagen, Denmark)2011

Osh proteins regulate membrane sterol organization but are not required for sterol movement between the ER and PM.

Alexander G Georgiev, David P Sullivan, Michael C Kersting, Jeremy S Dittman, Christopher T Beh, Anant K Menon

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
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  7. The Fast and the Furious: Golgi Contact Sites.Contact (Thousand Oaks (Ventura County, Calif.)) · 2021
    Article
  8. Review
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  14. Review
  15. Review
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  17. Article
  18. Article
  19. Article
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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

6 authors at 2 institutions in 2 countries.

Alexander G GeorgievDepartment of Biochemistry, Weill Cornell Medical College, New York, NY, USA.
David P Sullivan
Michael C Kersting
Jeremy S Dittman
Christopher T Beh
Anant K Menon
Cornell University · USSimon Fraser University · CA

Funding

Analysis of synaptic protein dynamicsR01GM095674 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI DITTMAN, JEREMY SAMUEL · 2011 to 2019
$3.2M
BIOSYNTHESIS OF MEMBRANE PROTEIN GLYCOLIPID ANCHORSR01GM055427 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI MENON, ANANT K · 1997 to 2010
$3.0M
NIGMS NIH HHS GM09958674NIGMS NIH HHS GM55427NIGMS NIH HHS R01 GM055427NIGMS NIH HHS R01 GM095674
6 · The paper itself

Abstract

Sterol transport between the endoplasmic reticulum (ER) and plasma membrane (PM) occurs by an ATP-dependent, non-vesicular mechanism that is presumed to require sterol transport proteins (STPs). In Saccharomyces cerevisiae, homologs of the mammalian oxysterol-binding protein (Osh1-7) have been proposed to function as STPs. To evaluate this proposal we took two approaches. First we used dehydroergosterol (DHE) to visualize sterol movement in living cells by fluorescence microscopy. DHE was introduced into the PM under hypoxic conditions and observed to redistribute to lipid droplets on growing the cells aerobically. Redistribution required ATP and the sterol acyltransferase Are2, but did not require PM-derived transport vesicles. DHE redistribution occurred robustly in a conditional yeast mutant (oshΔ osh4-1(ts)) that lacks all functional Osh proteins at 37°C. In a second approach we used a pulse-chase protocol to analyze the movement of metabolically radiolabeled ergosterol from the ER to the PM. Arrival of radiolabeled ergosterol at the PM was assessed in isolated PM-enriched fractions as well as by extracting sterols from intact cells with methyl-β-cyclodextrin. These experiments revealed that whereas ergosterol is transported effectively from the ER to the PM in Osh-deficient cells, the rate at which it moves within the PM to equilibrate with the methyl-β-cyclodextrin extractable sterol pool is slowed. We conclude (i) that the role of Osh proteins in non-vesicular sterol transport between the PM, ER and lipid droplets is either minimal, or subsumed by other mechanisms and (ii) that Osh proteins regulate the organization of sterols at the PM.

Indexed as

Carrier ProteinsCell MembraneChromatography, High Pressure LiquidEndoplasmic ReticulumErgosterolMicroscopy, FluorescenceMolecular StructureOxygenOxysterol Binding ProteinsProtein TransportReceptors, SteroidSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSterolsCarrier ProteinsdehydroergosterolErgosterolOxygenOxysterol Binding ProteinsReceptors, SteroidSaccharomyces cerevisiae ProteinsSterols

Identifiers

PMID21689253
PMCPMC3171641
OpenAlexW2076554898

What OpenQuestion holds

Textmetadata
LicenceTDM
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.