Evidence map›Paper›PMID 22396764›Full record

ArticlePloS one2012

Post-translational regulation and trafficking of the granulin-containing protease RD21 of Arabidopsis thaliana.

Christian Gu, Mohammed Shabab, Richard Strasser, Pieter J Wolters, Takayuki Shindo, Melanie Niemer, Farnusch Kaschani, Lukas Mach, Renier A L van der Hoorn

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

48 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Pathogen-inspired engineering of plant protease enhances late blight resistance.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Transient proteolysis reduction ofFrontiers in plant science · 2022
    Article
  13. Article
  14. Review
  15. The Papain-like Cysteine ProteaseInternational journal of molecular sciences · 2021
    Article
  16. Article
  17. Horticulture research · 2020
    Article
  18. Article
  19. Article
  20. Do proteolytic cascades exist in plants?Journal of experimental botany · 2019
    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

9 authors at 4 institutions in 2 countries.

Christian GuThe Plant Chemetics Lab, Chemical Genomics Centre of the Max Planck Society, Max Planck Institute for Plant Breeding Research, Cologne, Germany.
Mohammed Shabab
Richard Strasser
Pieter J Wolters
Takayuki Shindo
Melanie Niemer
Farnusch Kaschani
Lukas Mach
Renier A L van der Hoorn
BOKU University · ATMax Planck Institute for Plant Breeding Research · DEMax Planck Society · DEChemical Genomics Centre · DE

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

RD21-like proteases are ubiquitous, plant-specific papain-like proteases typified by carrying a C-terminal granulin domain. RD21-like proteases are involved in immunity and associated with senescence and various types of biotic and abiotic stresses. Here, we interrogated Arabidopsis RD21 regulation and trafficking by site-directed mutagenesis, agroinfiltration, western blotting, protease activity profiling and protein degradation. Using an introduced N-glycan sensor, deglycosylation experiments and glyco-engineered N. benthamiana plants, we show that RD21 passes through the Golgi where it becomes fucosylated. Our studies demonstrate that RD21 is regulated at three post-translational levels. Prodomain removal is not blocked in the catalytic Cys mutant, indicating that RD21 is activated by a proteolytic cascade. However, RD21 activation in Arabidopsis does not require vacuolar processing enzymes (VPEs) or aleurain-like protease AALP. In contrast, granulin domain removal requires the catalytic Cys and His residues and is therefore autocatalytic. Furthermore, SDS can (re-)activate latent RD21 in Arabidopsis leaf extracts, indicating the existence of a third layer of post-translational regulation, possibly mediated by endogenous inhibitors. RD21 causes a dominant protease activity in Arabidopsis leaf extracts, responsible for SDS-induced proteome degradation.

Indexed as

Protein Processing, Post-TranslationalArabidopsisArabidopsis ProteinsBiotinylationCatalysisCysteineCysteine EndopeptidasesCysteine ProteasesGene DeletionGene Expression Regulation, PlantGlycosylationGolgi ApparatusIntercellular Signaling Peptides and ProteinsMass SpectrometryMutationPlant ExtractsaleurainArabidopsis ProteinsCysteineCysteine EndopeptidasesCysteine ProteasesIntercellular Signaling Peptides and ProteinsPlant ExtractsPolysaccharidesProgranulinsRD21 protein, Arabidopsisvacuolar processing enzyme

Identifiers

PMID22396764
PMCPMC3292552
OpenAlexW1985694955

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.