Evidence map›Paper›PMID 23800962›Full record

ArticleThe Plant cell2013

The deubiquitinating enzyme AMSH1 and the ESCRT-III subunit VPS2.1 are required for autophagic degradation in Arabidopsis.

Anthi Katsiarimpa, Kamila Kalinowska, Franziska Anzenberger, Corina Weis, Maya Ostertag, Chie Tsutsumi, Claus Schwechheimer, Frédéric Brunner, Ralph Hückelhoven, Erika Isono

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed, 2 pooled it
7.9field-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

60 citing papers in PubMed, 2 syntheses or guidelines pooled it, 125 citations in OpenAlex.

  1. Guideline
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  9. Article
  10. Endosomal membrane budding patterns in plants.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Review
  13. Review
  14. Autophagy in plants.Autophagy reports · 2024
    Review
  15. Article
  16. Review
  17. Regulation of PIN-FORMED Protein Degradation.International journal of molecular sciences · 2023
    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

10 authors at 3 institutions in 2 countries.

Anthi KatsiarimpaDepartment of Plant Systems Biology, Technische Universität München, 85354 Freising, Germany.
Kamila Kalinowska
Franziska Anzenberger
Corina Weis
Maya Ostertag
Chie Tsutsumi
Claus Schwechheimer
Frédéric Brunner
Ralph Hückelhoven
Erika Isono
Technical University of Munich · DENational Museum of Nature and Science · JPUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, posttranslational modification by ubiquitin regulates the activity and stability of many proteins and thus influences a variety of developmental processes as well as environmental responses. Ubiquitination also plays a critical role in intracellular trafficking by serving as a signal for endocytosis. We have previously shown that the Arabidopsis thaliana associated molecule with the SH3 domain of STAM3 (AMSH3) is a deubiquitinating enzyme (DUB) that interacts with endosomal complex required for transport-III (ESCRT-III) and is essential for intracellular transport and vacuole biogenesis. However, physiological functions of AMSH3 in the context of its ESCRT-III interaction are not well understood due to the severe seedling lethal phenotype of its null mutant. In this article, we show that Arabidopsis AMSH1, an AMSH3-related DUB, interacts with the ESCRT-III subunit vacuolar protein sorting2.1 (VPS2.1) and that impairment of both AMSH1 and VPS2.1 causes early senescence and hypersensitivity to artificial carbon starvation in the dark similar to previously reported autophagy mutants. Consistent with this, both mutants accumulate autophagosome markers and accumulate less autophagic bodies in the vacuole. Taken together, our results demonstrate that AMSH1 and the ESCRT-III-subunit VPS2.1 are important for autophagic degradation and autophagy-mediated physiological processes.

Indexed as

ArabidopsisArabidopsis ProteinsAutophagyDarknessDisease ResistanceEndocytosisEndosomal Sorting Complexes Required for TransportFungiGene Expression Regulation, DevelopmentalGene Expression Regulation, PlantGreen Fluorescent ProteinsImmunoblottingMicroscopy, ConfocalMutationPlant DiseasesPlants, Genetically ModifiedAMSH1 protein, ArabidopsisAMSH3 protein, ArabidopsisArabidopsis ProteinsEndosomal Sorting Complexes Required for TransportGreen Fluorescent ProteinsProtein SubunitsUbiquitinated ProteinsUbiquitin-Specific ProteasesVPS2.1 protein, Arabidopsis

Identifiers

PMID23800962
PMCPMC3723623
OpenAlexW2141379701

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.