Evidence map›Paper›PMID 25854684›Full record

ArticleOpen biology2015

The peroxisomal protein import machinery displays a preference for monomeric substrates.

Marta O Freitas, Tânia Francisco, Tony A Rodrigues, Celien Lismont, Pedro Domingues, Manuel P Pinto, Cláudia P Grou, Marc Fransen, Jorge E Azevedo

Abstract read
In one paragraph

Article in Open biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Peroxisome biogenesis disorders.Translational science of rare diseases · 2016
    Article
  15. Article
  16. Article
  17. Optical Control of Peroxisomal Trafficking.ACS synthetic biology · 2016
    Article
  18. Peroxisome protein import: a complex journey.Biochemical Society transactions · 2016
    Review
  19. 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

9 authors.

Marta O FreitasOrganelle Biogenesis and Function Group, Instituto de Biologia Celular e Molecular (IBMC), Universidade do Porto, Porto, Portugal.
Tânia FranciscoOrganelle Biogenesis and Function Group, Instituto de Biologia Celular e Molecular (IBMC), Universidade do Porto, Porto, Portugal.
Tony A RodriguesOrganelle Biogenesis and Function Group, Instituto de Biologia Celular e Molecular (IBMC), Universidade do Porto, Porto, Portugal Instituto de Ciências Biomédicas Abel Salazar (ICBAS), Universidade do Porto, Porto, Portugal.
Celien LismontDepartement Cellulaire en Moleculaire Geneeskunde, KU Leuven-Universiteit Leuven, Leuven, Belgium.
Pedro DominguesDepartamento de Química, Universidade de Aveiro, Aveiro, Portugal.
Manuel P PintoOrganelle Biogenesis and Function Group, Instituto de Biologia Celular e Molecular (IBMC), Universidade do Porto, Porto, Portugal.
Cláudia P GrouOrganelle Biogenesis and Function Group, Instituto de Biologia Celular e Molecular (IBMC), Universidade do Porto, Porto, Portugal.ORCID http://orcid.org/0000-0001-5197-2270
Marc FransenDepartement Cellulaire en Moleculaire Geneeskunde, KU Leuven-Universiteit Leuven, Leuven, Belgium.
Jorge E AzevedoOrganelle Biogenesis and Function Group, Instituto de Biologia Celular e Molecular (IBMC), Universidade do Porto, Porto, Portugal Instituto de Ciências Biomédicas Abel Salazar (ICBAS), Universidade do Porto, Porto, Portugal jazevedo@ibmc.up.pt.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxisomal matrix proteins are synthesized on cytosolic ribosomes and transported by the shuttling receptor PEX5 to the peroxisomal membrane docking/translocation machinery, where they are translocated into the organelle matrix. Under certain experimental conditions this protein import machinery has the remarkable capacity to accept already oligomerized proteins, a property that has heavily influenced current models on the mechanism of peroxisomal protein import. However, whether or not oligomeric proteins are really the best and most frequent clients of this machinery remain unclear. In this work, we present three lines of evidence suggesting that the peroxisomal import machinery displays a preference for monomeric proteins. First, in agreement with previous findings on catalase, we show that PEX5 binds newly synthesized (monomeric) acyl-CoA oxidase 1 (ACOX1) and urate oxidase (UOX), potently inhibiting their oligomerization. Second, in vitro import experiments suggest that monomeric ACOX1 and UOX are better peroxisomal import substrates than the corresponding oligomeric forms. Finally, we provide data strongly suggesting that although ACOX1 lacking a peroxisomal targeting signal can be imported into peroxisomes when co-expressed with ACOX1 containing its targeting signal, this import pathway is inefficient.

Indexed as

Models, BiologicalSignal TransductionAcyl-CoA OxidaseAnimalsBlotting, WesternChlorocebus aethiopsCOS CellsCytosolHumansMiceMicroscopy, FluorescenceMutationPeroxisomesPeroxisome-Targeting Signal 1 ReceptorProtein BindingProtein MultimerizationAcyl-CoA OxidasePeroxisome-Targeting Signal 1 ReceptorPEX5 protein, humanPex5 protein, mouseReceptors, Cytoplasmic and NuclearUrate Oxidaseacyl-CoA oxidasedocking/translocation machineryperoxisomesPEX5protein importurate oxidase

Identifiers

PMID25854684
PMCPMC4422123

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Registered trials

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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.