Evidence map›Paper›PMID 25538232›Full record

ArticleThe Journal of biological chemistry2015

Mechanistic insights into PTS2-mediated peroxisomal protein import: the co-receptor PEX5L drastically increases the interaction strength between the cargo protein and the receptor PEX7.

Markus Kunze, Naila Malkani, Sebastian Maurer-Stroh, Christoph Wiesinger, Johannes A Schmid, Johannes Berger

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026
    Review
  2. Article
  3. Pieces of the peroxisomal import puzzle.Nature cell biology · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Ophthalmology science · 2021
    Article
  12. Glycosome heterogeneity in kinetoplastids.Biochemical Society transactions · 2021
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Peroxisomes in brain development and function.Biochimica et biophysica acta · 2016
    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

6 authors at 2 institutions in 2 countries.

Markus KunzeCenter for Brain Research, Medical University of Vienna, Spitalgasse 4, 1090 Vienna, Austria,. Electronic address: markus.kunze@meduniwien.ac.at.
Naila MalkaniDepartment of Vascular Biology and Thrombosis Research, Medical University of Vienna, Schwarzspanierstrasse 17, 1090 Vienna, Austria.
Sebastian Maurer-StrohBioinformatics Institute (BII), Agency for Science, Technology and Research (A*STAR), 30 Biopolis Street, Singapore 138671; School of Biological Sciences (SBS), Nanyang Technological University (NTU), 8 Medical Drive, Singapore 117597.
Christoph WiesingerCenter for Brain Research, Medical University of Vienna, Spitalgasse 4, 1090 Vienna, Austria.
Johannes A SchmidDepartment of Vascular Biology and Thrombosis Research, Medical University of Vienna, Schwarzspanierstrasse 17, 1090 Vienna, Austria.
Johannes BergerCenter for Brain Research, Medical University of Vienna, Spitalgasse 4, 1090 Vienna, Austria.
Medical University of Vienna · ATBioinformatics Institute · SG

Funding

Austrian Science Fund FWF P 21950
6 · The paper itself

Abstract

The destination of peroxisomal matrix proteins is encoded by short peptide sequences, which have been characterized as peroxisomal targeting signals (PTS) residing either at the C terminus (PTS1) or close to the N terminus (PTS2). PTS2-carrying proteins interact with their cognate receptor protein PEX7 that mediates their transport to peroxisomes by a concerted action with a co-receptor protein, which in mammals is the PTS1 receptor PEX5L. Using a modified version of the mammalian two-hybrid assay, we demonstrate that the interaction strength between cargo and PEX7 is drastically increased in the presence of the co-receptor PEX5L. In addition, cargo binding is a prerequisite for the interaction between PEX7 and PEX5L and ectopic overexpression of PTS2-carrying cargo protein drastically increases the formation of PEX7-PEX5L complexes in this assay. Consistently, we find that the peroxisomal transfer of PEX7 depends on cargo binding and that ectopic overexpression of cargo protein stimulates this process. Thus, the sequential formation of a highly stable trimeric complex involving cargo protein, PEX7 and PEX5L stabilizes cargo binding and is a prerequisite for PTS2-mediated peroxisomal import.

Indexed as

AnimalsChlorocebus aethiopsCOS CellsHumansMultiprotein ComplexesPeroxisomal Targeting Signal 2 ReceptorPeroxisomesProtein TransportReceptors, Cytoplasmic and NuclearTwo-Hybrid System TechniquesMultiprotein ComplexesPeroxisomal Targeting Signal 2 ReceptorPEX5L protein, humanPEX7 protein, humanReceptors, Cytoplasmic and NuclearConformational ChangeMammalian Two-hybrid AssayPeroxisomePEX5PEX7Protein SortingProtein TargetingPTS2ReceptorTrimeric Complex

Identifiers

PMID25538232
PMCPMC4335231
OpenAlexW2115992493

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.