Evidence map›Paper›PMID 24379391›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Differential processing of Arabidopsis ubiquitin-like Atg8 autophagy proteins by Atg4 cysteine proteases.

Jongchan Woo, Eunsook Park, S P Dinesh-Kumar

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

57 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Functional Analysis of the Autophagy-Related GenePlants (Basel, Switzerland) · 2025
    Article
  5. Article
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  7. Evolutionary conservation and metabolic significance of autophagy in algae.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  8. Article
  9. Article
  10. Autophagy in plants.Autophagy reports · 2024
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Detection of Autophagy in Plants by Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  18. Review
  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 2 institutions in 1 country.

Jongchan WooDepartment of Plant Biology and the Genome Center, College of Biological Sciences, and Department of Plant Sciences, College of Agricultural and Environmental Sciences, University of California, Davis, CA 95616.
Eunsook Park
S P Dinesh-Kumar
University of California, Davis · USUniversity of Minnesota · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is a highly conserved biological process during which double membrane bound autophagosomes carry intracellular cargo material to the vacuole or lysosome for degradation and/or recycling. Autophagosome biogenesis requires Autophagy 4 (Atg4) cysteine protease-mediated processing of ubiquitin-like Atg8 proteins. Unlike single Atg4 and Atg8 genes in yeast, the Arabidopsis genome contains two Atg4 (AtAtg4a and AtAtg4b) and nine Atg8 (AtAtg8a-AtAtg8i) genes. However, we know very little about specificity of different AtAtg4s for processing of different AtAtg8s. Here, we describe a unique bioluminescence resonance energy transfer-based AtAtg8 synthetic substrate to assess AtAtg4 activity in vitro and in vivo. In addition, we developed a unique native gel assay of superhRLUC catalytic activity assay to monitor cleavage of AtAtg8s in vitro. Our results indicate that AtAtg4a is the predominant protease and that it processes AtAtg8a, AtAtg8c, AtAtg8d, and AtAtg8i better than AtAtg4b in vitro. In addition, kinetic analyses indicate that although both AtAtg4s have similar substrate affinity, AtAtg4a is more active than AtAtg4b in vitro. Activity of AtAtg4s is reversibly inhibited in vitro by reactive oxygen species such as H2O2. Our in vivo bioluminescence resonance energy transfer analyses in Arabidopsis transgenic plants indicate that the AtAtg8 synthetic substrate is efficiently processed and this is AtAtg4 dependent. These results indicate that the synthetic AtAtg8 substrate is used efficiently in the biogenesis of autophagosomes in vivo. Transgenic Arabidopsis plants expressing the AtAtg8 synthetic substrate will be a valuable tool to dissect autophagy processes and the role of autophagy during different biological processes in plants.

Indexed as

ArabidopsisArabidopsis ProteinsAutophagyAutophagy-Related ProteinsCysteine ProteasesImmunoblottingLuminescent MeasurementsMicroscopy, ConfocalMicrotubule-Associated ProteinsPhagosomesPlants, Genetically ModifiedSubstrate SpecificityUbiquitinsAPG8a protein, ArabidopsisArabidopsis ProteinsAtg4 protein, ArabidopsisAutophagy-Related ProteinsCysteine ProteasesMicrotubule-Associated ProteinsUbiquitinsatg4a4bautophagic bodymonodansylcadaverinenitrogen starvation

Identifiers

PMID24379391
PMCPMC3896200
OpenAlexW2039063541

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.