Evidence map›Paper›PMID 21951626›Full record

ArticleTraffic (Copenhagen, Denmark)2012

A subtle interplay between three Pex11 proteins shapes de novo formation and fission of peroxisomes.

Anja Huber, Johannes Koch, Friedrich Kragler, Cécile Brocard, Andreas Hartig

Open access · greenAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

41 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  8. EngineeringSynthetic and systems biotechnology · 2023
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Cells · 2022
    Article
  14. Article
  15. Article
  16. Determinants of Peroxisome Membrane Dynamics.Frontiers in physiology · 2022
    Review
  17. Article
  18. Review
  19. Article
  20. 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 2 countries.

Anja HuberUniversity of Vienna, Max F. Perutz Laboratories, Center for Molecular Biology, Department of Biochemistry and Cell Biology, Dr. Bohr-Gasse 9, Vienna, Austria.
Johannes Koch
Friedrich Kragler
Cécile Brocard
Andreas Hartig
University of Vienna · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The organization of eukaryotic cells into membrane-bound compartments must be faithfully sustained for survival of the cell. A subtle equilibrium exists between the degradation and the proliferation of organelles. Commonly, proliferation is initiated by a membrane remodeling process. Here, we dissect the function of proteins driving organelle proliferation in the particular case of peroxisomes. These organelles are formed either through a growth and division process from existing peroxisomes or de novo from the endoplasmic reticulum (ER). Among the proteins involved in the biogenesis of peroxisomes, peroxins, members of the Pex11 protein family participate in peroxisomal membrane alterations. In the yeast Saccharomyces cerevisiae, the Pex11 family consists of three proteins, Pex11p, Pex25p and Pex27p. Here we demonstrate that yeast mutants lacking peroxisomes require the presence of Pex25p to regenerate this organelle de novo. We also provide evidence showing that Pex27p inhibits peroxisomal function and illustrate that Pex25p initiates elongation of the peroxisomal membrane. Our data establish that although structurally conserved each of the three Pex11 protein family members plays a distinct role. While ScPex11p promotes the proliferation of peroxisomes already present in the cell, ScPex25p initiates remodeling at the peroxisomal membrane and ScPex27p acts to counter this activity. In addition, we reveal that ScPex25p acts in concert with Pex3p in the initiation of de novo peroxisome biogenesis from the ER.

Indexed as

Blotting, WesternEndoplasmic ReticulumEscherichia coliGene ExpressionGreen Fluorescent ProteinsIntracellular MembranesMembrane ProteinsMutationOleic AcidOrganelle SizePeroxinsPeroxisomesPlasmidsProtein TransportReal-Time Polymerase Chain ReactionSaccharomyces cerevisiaeenhanced green fluorescent proteinGreen Fluorescent ProteinsMembrane ProteinsOleic AcidPeroxinsPEX11 protein, S cerevisiaePEX25 protein, S cerevisiaePex27 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID21951626
PMCPMC3245845
OpenAlexW2015905425

What OpenQuestion holds

Textmetadata
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.