Evidence map›Paper›PMID 25214533›Full record

ArticlePlant physiology2014

Peroxisomal ubiquitin-protein ligases peroxin2 and peroxin10 have distinct but synergistic roles in matrix protein import and peroxin5 retrotranslocation in Arabidopsis.

Sarah E Burkhart, Yun-Ting Kao, Bonnie Bartel

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 41 citations in OpenAlex.

  1. Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. The Structure of theFrontiers in cell and developmental biology · 2022
    Article
  10. Review
  11. Review
  12. Article
  13. APlant direct · 2019
    Article
  14. Review
  15. AProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Sarah E BurkhartDepartment of BioSciences, Rice University, Houston, Texas 77005.
Yun-Ting KaoDepartment of BioSciences, Rice University, Houston, Texas 77005.
Bonnie BartelDepartment of BioSciences, Rice University, Houston, Texas 77005 bartel@rice.edu.
Rice University · US

Funding

Using Arabidopsis to uncover new roles for peroxinsR01GM079177 · NIGMS · RICE UNIVERSITY · PI BARTEL, BONNIE · 2009 to 2017
$2.4M
Laser scanning confocal microscopeS10RR026399 · NCRR · RICE UNIVERSITY · PI BARTEL, BONNIE · 2010 to 2010
$500k
NCRR NIH HHS S10 RR026399NCRR NIH HHS S10RR026399-01NIGMS NIH HHS R01 GM079177NIGMS NIH HHS R01GM079177
6 · The paper itself

Abstract

Peroxisomal matrix proteins carry peroxisomal targeting signals (PTSs), PTS1 or PTS2, and are imported into the organelle with the assistance of peroxin (PEX) proteins. From a microscopy-based screen to identify Arabidopsis (Arabidopsis thaliana) mutants defective in matrix protein degradation, we isolated unique mutations in PEX2 and PEX10, which encode ubiquitin-protein ligases anchored in the peroxisomal membrane. In yeast (Saccharomyces cerevisiae), PEX2, PEX10, and a third ligase, PEX12, ubiquitinate a peroxisome matrix protein receptor, PEX5, allowing the PEX1 and PEX6 ATP-hydrolyzing enzymes to retrotranslocate PEX5 out of the membrane after cargo delivery. We found that the pex2-1 and pex10-2 Arabidopsis mutants exhibited defects in peroxisomal physiology and matrix protein import. Moreover, the pex2-1 pex10-2 double mutant exhibited severely impaired growth and synergistic physiological defects, suggesting that PEX2 and PEX10 function cooperatively in the wild type. The pex2-1 lesion restored the unusually low PEX5 levels in the pex6-1 mutant, implicating PEX2 in PEX5 degradation when retrotranslocation is impaired. PEX5 overexpression altered pex10-2 but not pex2-1 defects, suggesting that PEX10 facilitates PEX5 retrotranslocation from the peroxisomal membrane. Although the pex2-1 pex10-2 double mutant displayed severe import defects of both PTS1 and PTS2 proteins into peroxisomes, both pex2-1 and pex10-2 single mutants exhibited clear import defects of PTS1 proteins but apparently normal PTS2 import. A similar PTS1-specific pattern was observed in the pex4-1 ubiquitin-conjugating enzyme mutant. Our results indicate that Arabidopsis PEX2 and PEX10 cooperate to support import of matrix proteins into plant peroxisomes and suggest that some PTS2 import can still occur when PEX5 retrotranslocation is slowed.

Indexed as

Adenosine TriphosphatasesArabidopsisArabidopsis ProteinsATPases Associated with Diverse Cellular ActivitiesGene Expression Regulation, PlantGenetic Complementation TestMalate DehydrogenaseMembrane ProteinsMembrane Transport ProteinsMutationPeroxinsPeroxisomesPeroxisome-Targeting Signal 1 ReceptorPlants, Genetically ModifiedProtein StabilityProtein TransportAdenosine TriphosphatasesArabidopsis ProteinsATPases Associated with Diverse Cellular ActivitiesMalate DehydrogenaseMembrane ProteinsMembrane Transport ProteinsPEROXIN6 protein, ArabidopsisPeroxinsPeroxisome-Targeting Signal 1 ReceptorPEX10 protein, ArabidopsisPEX5 protein, ArabidopsisPMDH1 protein, ArabidopsisReceptors, Cytoplasmic and NuclearTED3 protein, Arabidopsis

Identifiers

PMID25214533
PMCPMC4226347
OpenAlexW2006085907

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.