Evidence map›Paper›PMID 21487094›Full record

ArticleThe Plant cell2011

Arabidopsis ABERRANT PEROXISOME MORPHOLOGY9 is a peroxin that recruits the PEX1-PEX6 complex to peroxisomes.

Shino Goto, Shoji Mano, Chihiro Nakamori, Mikio Nishimura

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

43 citing papers in PubMed, 88 citations in OpenAlex.

  1. Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026
    Review
  2. Article
  3. Article
  4. Growth and physiological response of YuluPlant signaling & behavior · 2024
    Article
  5. PEX1 is essential for glycosome biogenesis and trypanosomatid parasite survival.Frontiers in cellular and infection microbiology · 2024
    Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Anaerobic peroxisomes inProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Review
  13. APlant direct · 2019
    Article
  14. Review
  15. Article
  16. AProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Article
  18. Article
  19. Review
  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 2 institutions in 1 country.

Shino GotoDepartment of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan.
Shoji Mano
Chihiro Nakamori
Mikio Nishimura
The Graduate University for Advanced Studies, SOKENDAI · JPNational Institute for Basic Biology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxisomes have pivotal roles in several metabolic processes, such as the detoxification of H₂O₂ and β-oxidation of fatty acids, and their functions are tightly regulated by multiple factors involved in peroxisome biogenesis, including protein transport. This study describes the isolation of an embryonic lethal Arabidopsis thaliana mutant, aberrant peroxisome morphology9 (apem9), which is compromised in protein transport into peroxisomes. The APEM9 gene was found to encode an unknown protein. Compared with apem9 having the nucleotide substitution, the knockdown mutants showed severe defects in peroxisomal functions and plant growth. We showed that expression of APEM9 altered PEROXIN6 (PEX6) subcellular localization from the cytosol to peroxisomes. In addition, we showed that PEX1 and PEX6 comprise a heterooligomer and that this complex was recruited to peroxisomal membranes via protein-protein interactions of APEM9 with PEX6. These findings show that APEM9 functions as an anchoring protein, similar to Pex26 in mammals and Pex15p in yeast. Interestingly, however, the identities of amino acids among these anchoring proteins are quite low. These results indicate that although the association of the PEX1-PEX6 complex with peroxisomal membranes is essential for peroxisomal functions, the protein that anchors this complex evolved uniquely in plants.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceArabidopsisArabidopsis ProteinsATPases Associated with Diverse Cellular ActivitiesDNA, BacterialGene Expression Regulation, PlantGene Knockdown TechniquesGenes, PlantIntracellular MembranesMembrane ProteinsMolecular Sequence DataMutagenesis, InsertionalMutant ProteinsMutationOrgan SpecificityAdenosine TriphosphatasesAPEM9 protein, ArabidopsisArabidopsis ProteinsATPases Associated with Diverse Cellular ActivitiesDNA, BacterialMembrane ProteinsMutant ProteinsPEROXIN6 protein, ArabidopsisPEX1 protein, ArabidopsisT-DNA

Identifiers

PMID21487094
PMCPMC3101541
OpenAlexW2152677268

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.