Evidence map›Paper›PMID 23308220›Full record

ArticlePloS one2013

Self-interaction of human Pex11pβ during peroxisomal growth and division.

Nina A Bonekamp, Sandra Grille, Maria Joao Cardoso, Monica Almeida, Miguel Aroso, Silvia Gomes, Ana Cristina Magalhaes, Daniela Ribeiro, Markus Islinger, Michael Schrader

Open access · goldAbstract 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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Determinants of Peroxisome Membrane Dynamics.Frontiers in physiology · 2022
    Review
  10. Review
  11. Article
  12. The cell biology of the retinal pigment epithelium.Progress in retinal and eye research · 2020
    Review
  13. Article
  14. Article
  15. Article
  16. Crosstalk between mitochondria and peroxisomes.World journal of biological chemistry · 2015
    Review
  17. Peroxisome-mitochondria interplay and disease.Journal of inherited metabolic disease · 2015
    Review
  18. The membrane remodeling protein Pex11p activates the GTPase Dnm1p during peroxisomal fission.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  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

10 authors at 2 institutions in 2 countries.

Nina A BonekampCentre for Cell Biology and Department of Biology, University of Aveiro, Campus Universitário de Santiago, Aveiro, Portugal.
Sandra Grille
Maria Joao Cardoso
Monica Almeida
Miguel Aroso
Silvia Gomes
Ana Cristina Magalhaes
Daniela Ribeiro
Markus Islinger
Michael Schrader
University of Aveiro · PTUniversity of Exeter · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pex11 proteins are involved in membrane elongation and division processes associated with the multiplication of peroxisomes. Human Pex11pβ has recently been linked to a new disorder affecting peroxisome morphology and dynamics. Here, we have analyzed the exact membrane topology of Pex11pβ. Studies with an epitope-specific antibody and protease protection assays show that Pex11pβ is an integral membrane protein with two transmembrane domains flanking an internal region exposed to the peroxisomal matrix and N- and C-termini facing the cytosol. A glycine-rich internal region within Pex11pβ is dispensable for peroxisome membrane elongation and division. However, we demonstrate that an amphipathic helix (Helix 2) within the first N-terminal 40 amino acids is crucial for membrane elongation and self-interaction of Pex11pβ. Interestingly, we find that Pex11pβ self-interaction strongly depends on the detergent used for solubilization. We also show that N-terminal cysteines are not essential for membrane elongation, and that putative N-terminal phosphorylation sites are dispensable for Pex11pβ function. We propose that self-interaction of Pex11pβ regulates its membrane deforming activity in conjunction with membrane lipids.

Indexed as

AnimalsChlorocebus aethiopsCOS CellsHumansIntracellular MembranesMembrane ProteinsPeroxisomesPhosphorylationProtein Interaction Domains and MotifsProtein Structure, SecondaryRecombinant Fusion ProteinsTransfectionMembrane ProteinsPEX11B protein, humanRecombinant Fusion Proteins

Identifiers

PMID23308220
PMCPMC3538539
OpenAlexW1967200055

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.