Evidence map›Paper›PMID 22493507›Full record

ArticleThe Journal of biological chemistry2012

Peroxisomal fatty acid uptake mechanism in Saccharomyces cerevisiae.

Carlo W T van Roermund, Lodewijk Ijlst, Wiktor Majczak, Hans R Waterham, Hendrik Folkerts, Ronald J A Wanders, Klaas J Hellingwerf

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Engineering yeast for tailored fatty acid profiles.Applied microbiology and biotechnology · 2025
    Review
  5. Article
  6. In focus in HCB.Histochemistry and cell biology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Fatty acid uptake inFrontiers in cellular and infection microbiology · 2022
    Review
  13. Review
  14. Article
  15. Peroxisomal ABC Transporters: An Update.International journal of molecular sciences · 2021
    Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Frontiers in cell and developmental biology · 2020
    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

7 authors.

Carlo W T van RoermundDepartments of Pediatrics and Clinical Chemistry, Laboratory Genetic Metabolic Diseases, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands. c.vanroermund@amc.uva.nl
Lodewijk Ijlst
Wiktor Majczak
Hans R Waterham
Hendrik Folkerts
Ronald J A Wanders
Klaas J Hellingwerf

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxisomes play a major role in human cellular lipid metabolism, including fatty acid β-oxidation. The most frequent peroxisomal disorder is X-linked adrenoleukodystrophy, which is caused by mutations in ABCD1. The biochemical hallmark of X-linked adrenoleukodystrophy is the accumulation of very long chain fatty acids (VLCFAs) due to impaired peroxisomal β-oxidation. Although this suggests a role of ABCD1 in VLCFA import into peroxisomes, no direct experimental evidence is available to substantiate this. To unravel the mechanism of peroxisomal VLCFA transport, we use Saccharomyces cerevisiae as a model organism. Here we provide evidence that in this organism very long chain acyl-CoA esters are hydrolyzed by the Pxa1p-Pxa2p complex prior to the actual transport of their fatty acid moiety into the peroxisomes with the CoA presumably being released into the cytoplasm. The Pxa1p-Pxa2p complex functionally interacts with the acyl-CoA synthetases Faa2p and/or Fat1p on the inner surface of the peroxisomal membrane for subsequent re-esterification of the VLCFAs. Importantly, the Pxa1p-Pxa2p complex shares this molecular mechanism with HsABCD1 and HsABCD2.

Indexed as

AdrenoleukodystrophyATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily DATP Binding Cassette Transporter, Subfamily D, Member 1Biological Transport, ActiveCoenzyme A LigasesFatty AcidsFatty Acid Transport ProteinsHumansMultiprotein ComplexesOxidation-ReductionPeroxisomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsABCD1 protein, humanABCD2 protein, humanATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily DATP Binding Cassette Transporter, Subfamily D, Member 1Coenzyme A LigasesFAA2 protein, S cerevisiaeFAT1 protein, S cerevisiaeFatty AcidsFatty Acid Transport ProteinsMultiprotein ComplexesPXA1 protein, S cerevisiaePXA2 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID22493507
PMCPMC3370197

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.