Evidence map›Paper›PMID 15798189›Full record

ArticleMolecular and cellular biology2005

Identification of a novel, intraperoxisomal pex14-binding site in pex13: association of pex13 with the docking complex is essential for peroxisomal matrix protein import.

Annette Schell-Steven, Katharina Stein, Mara Amoros, Christiane Landgraf, Rudolf Volkmer-Engert, Hanspeter Rottensteiner, Ralf Erdmann

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Glycosome heterogeneity in kinetoplastids.Biochemical Society transactions · 2021
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. 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.

Annette Schell-StevenInstitut für Physiologische Chemie, Ruhr-Universität Bochum, D-44780 Bochum, Germany.
Katharina Stein
Mara Amoros
Christiane Landgraf
Rudolf Volkmer-Engert
Hanspeter Rottensteiner
Ralf Erdmann

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The peroxisomal docking complex is a key component of the import machinery for matrix proteins. The core protein of this complex, Pex14, is thought to represent the initial docking site for the import receptors Pex5 and Pex7. Associated with this complex is a fraction of Pex13, another essential component of the import machinery. Here we demonstrate that Pex13 directly binds Pex14 not only via its SH3 domain but also via a novel intraperoxisomal site. Furthermore, we demonstrate that Pex5 also contributes to the association of Pex13 with Pex14. Peroxisome function was affected only mildly by mutations within the novel Pex14 interaction site of Pex13 or by the non-Pex13-interacting mutant Pex5(W204A). However, when these constructs were tested in combination, PTS1-dependent import and growth on oleic acid were severely compromised. When the SH3 domain-mediated interaction of Pex13 with Pex14 was blocked on top of that, PTS2-dependent matrix protein import was completely compromised and Pex13 was no longer copurified with the docking complex. We conclude that the association of Pex13 with Pex14 is an essential step in peroxisomal protein import that is enabled by two direct interactions and by one that is mediated by Pex5, a result which indicates a novel, receptor-independent function of Pex5.

Indexed as

Amino Acid SequenceBinding SitesFungal ProteinsGenetic Complementation TestMembrane ProteinsMembrane Transport ProteinsMolecular Sequence DataMutationOleic AcidPeroxisomal Targeting Signal 2 ReceptorPeroxisomesPeroxisome-Targeting Signal 1 ReceptorProtein Interaction MappingProtein TransportReceptors, Cytoplasmic and NuclearRepressor ProteinsFungal ProteinsMembrane ProteinsMembrane Transport ProteinsOleic AcidPeroxisomal Targeting Signal 2 ReceptorPeroxisome-Targeting Signal 1 ReceptorPEX13 protein, S cerevisiaePEX5 protein, S cerevisiaeReceptors, Cytoplasmic and NuclearRepressor ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID15798189
PMCPMC1069607

What OpenQuestion holds

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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.