Evidence map›Paper›PMID 25016021›Full record

ArticleThe Journal of biological chemistry2014

AAA peroxins and their recruiter Pex26p modulate the interactions of peroxins involved in peroxisomal protein import.

Shigehiko Tamura, Naomi Matsumoto, Ryota Takeba, Yukio Fujiki

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Translational pediatrics · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Peroxisome: Metabolic Functions and Biogenesis.Advances in experimental medicine and biology · 2020
    Review
  11. Review
  12. A newly identified mutation in theCold Spring Harbor molecular case studies · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. AProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  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

4 authors at 1 institution in 1 country.

Shigehiko TamuraFaculty of Arts and Science, Kyushu University, Fukuoka 812-8581, Japan and Graduate School of Systems Life Sciences, Kyushu University Graduate School, Fukuoka 812-8581, Japan.
Naomi MatsumotoGraduate School of Systems Life Sciences, Kyushu University Graduate School, Fukuoka 812-8581, Japan.
Ryota TakebaGraduate School of Systems Life Sciences, Kyushu University Graduate School, Fukuoka 812-8581, Japan.
Yukio FujikiFrom the Department of Biology, Faculty of Sciences, and yfujiki@kyudai.jp.
Kyushu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pex1p and Pex6p are required for the relocation of the import receptor Pex5p from the peroxisomal membrane to the cytosol. We herein show that mammalian Pex26p directly binds to Pex14p, the initial docking receptor of Pex5p, and interacts with Pex5p via Pex14p. The binding affinity of Pex26p to Pex14p is altered by Pex5p. Further evidence suggests that the N-terminal region in Pex26p acts as a scaffold protein to recruit Pex14p·Pex5p complex together with Pex1p·Pex6p complexes on peroxisomes. Pex26p binding to Pex14p was suppressed by overexpression of Pex1p and Pex6p in an ATP-dependent manner, whereas Pex14p was not competed out by Pex1p and Pex6p from Pex26p mutant defective in peroxisomal matrix protein import. These results suggested that peroxisome biogenesis requires Pex1p- and Pex6p-regulated dissociation of Pex14p from Pex26p. Pex1p homo-oligomer directly binds to Pex5p as assessed by a surface plasmon resonance-based assay. Moreover, cytosolic Pex1p is likely to maintain the functional oligomer of Pex5p. Taken together, in the peroxisomal protein import, AAA peroxins modulate the interaction between Pex26p and Pex14p on peroxisome membrane as well as Pex5p oligomer in the cytosol.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAnimalsATPases Associated with Diverse Cellular ActivitiesBase SequenceCHO CellsCricetinaeCricetulusDNA PrimersHEK293 CellsHumansMembrane ProteinsNative Polyacrylamide Gel ElectrophoresisPolymerase Chain ReactionProtein BindingAdenosine TriphosphatasesAdenosine TriphosphateATPases Associated with Diverse Cellular ActivitiesDNA PrimersMembrane ProteinsPEX1 protein, humanPEX26 protein, humanPEX6 protein, humanAAA PeroxinsATPasePeroxisomePex14pPex26pProtein ComplexProtein ImportProtein TargetingScaffold Protein

Identifiers

PMID25016021
PMCPMC4148862
OpenAlexW2004262571

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.