Evidence map›Paper›PMID 23150599›Full record

ArticleGenetics2013

Genetic dissection of peroxisome-associated matrix protein degradation in Arabidopsis thaliana.

Sarah E Burkhart, Matthew J Lingard, Bonnie Bartel

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 54 citations in OpenAlex.

  1. Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026
    Review
  2. Article
  3. Profile of Bonnie Bartel.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. APlant direct · 2019
    Article
  11. Review
  12. Review
  13. AProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Review
  15. Article
  16. 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

3 authors at 1 institution in 1 country.

Sarah E BurkhartDepartment of Biochemistry and Cell Biology, Rice University, Houston, TX 77005, USA.
Matthew J Lingard
Bonnie Bartel
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 S10RR026399NIGMS NIH HHS R01 GM079177NIGMS NIH HHS R01GM079177
6 · The paper itself

Abstract

Peroxisomes are organelles that sequester certain metabolic pathways; many of these pathways generate H(2)O(2), which can damage proteins. However, little is known about how damaged or obsolete peroxisomal proteins are degraded. We exploit developmentally timed peroxisomal content remodeling in Arabidopsis thaliana to elucidate peroxisome-associated protein degradation. Isocitrate lyase (ICL) is a peroxisomal glyoxylate cycle enzyme necessary for early seedling development. A few days after germination, photosynthesis begins and ICL is degraded. We previously found that ICL is stabilized when a peroxisome-associated ubiquitin-conjugating enzyme and its membrane anchor are both mutated, suggesting that matrix proteins might exit the peroxisome for ubiquitin-dependent cytosolic degradation. To identify additional components needed for peroxisome-associated matrix protein degradation, we mutagenized a line expressing GFP-ICL, which is degraded similarly to endogenous ICL, and identified persistent GFP-ICL fluorescence (pfl) mutants. We found three pfl mutants that were defective in PEROXIN14 (PEX14/At5g62810), which encodes a peroxisomal membrane protein that assists in importing proteins into the peroxisome matrix, indicating that proteins must enter the peroxisome for efficient degradation. One pfl mutant was missing the peroxisomal 3-ketoacyl-CoA thiolase encoded by the PEROXISOME DEFECTIVE1 (PED1/At2g33150) gene, suggesting that peroxisomal metabolism influences the rate of matrix protein degradation. Finally, one pfl mutant that displayed normal matrix protein import carried a novel lesion in PEROXIN6 (PEX6/At1g03000), which encodes a peroxisome-tethered ATPase that is involved in recycling matrix protein receptors back to the cytosol. The isolation of pex6-2 as a pfl mutant supports the hypothesis that matrix proteins can exit the peroxisome for cytosolic degradation.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceArabidopsisArabidopsis ProteinsATPases Associated with Diverse Cellular ActivitiesMolecular Sequence DataMutationPeroxisomesProtein BindingProtein StabilityProtein TransportProteolysisSequence AlignmentAdenosine TriphosphatasesArabidopsis ProteinsATPases Associated with Diverse Cellular ActivitiesPEROXIN6 protein, Arabidopsis

Identifiers

PMID23150599
PMCPMC3527241
OpenAlexW2163134848

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.