Evidence map›Paper›PMID 26324913›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Arabidopsis ALIX is required for the endosomal localization of the deubiquitinating enzyme AMSH3.

Kamila Kalinowska, Marie-Kristin Nagel, Kaija Goodman, Laura Cuyas, Franziska Anzenberger, Angela Alkofer, Javier Paz-Ares, Pascal Braun, Vicente Rubio, Marisa S Otegui and 1 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
  2. Post-Golgi Trafficking in Plant Cells.Sub-cellular biochemistry · 2026
    Review
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  13. Bro1 family proteins harmonize cargo sorting with vesicle formation.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
  14. An unexpected function for an ESCRT protein.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Plant ESCRT protein ALIX coordinates with retromer complex in regulating receptor-mediated sorting of soluble vacuolar proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Review
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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

11 authors at 3 institutions in 3 countries.

Kamila KalinowskaPlant Systems Biology, Technische Universität München, 85354 Freising, Germany;
Marie-Kristin NagelPlant Systems Biology, Technische Universität München, 85354 Freising, Germany;
Kaija GoodmanDepartments of Botany and Genetics, Laboratory of Cell and Molecular Biology, University of Wisconsin-Madison, Madison, WI 53706;
Laura CuyasCentro Nacional de Biotecnología-CSIC, 28049 Madrid, Spain.
Franziska AnzenbergerPlant Systems Biology, Technische Universität München, 85354 Freising, Germany;
Angela AlkoferPlant Systems Biology, Technische Universität München, 85354 Freising, Germany;
Javier Paz-AresCentro Nacional de Biotecnología-CSIC, 28049 Madrid, Spain.
Pascal BraunPlant Systems Biology, Technische Universität München, 85354 Freising, Germany;
Vicente RubioCentro Nacional de Biotecnología-CSIC, 28049 Madrid, Spain.
Marisa S OteguiDepartments of Botany and Genetics, Laboratory of Cell and Molecular Biology, University of Wisconsin-Madison, Madison, WI 53706;
Erika IsonoPlant Systems Biology, Technische Universität München, 85354 Freising, Germany; erika.isono@wzw.tum.de.
Technical University of Munich · DECentro Nacional de Biotecnología · ESUniversity of Wisconsin–Madison · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination is a signal for various cellular processes, including for endocytic degradation of plasma membrane cargos. Ubiquitinating as well as deubiquitinating enzymes (DUBs) can regulate these processes by modifying the ubiquitination status of target protein. Although accumulating evidence points to the important regulatory role of DUBs, the molecular basis of their regulation is still not well understood. Associated molecule with the SH3 domain of signal transduction adaptor molecule (STAM) (AMSH) is a conserved metalloprotease DUB in eukaryotes. AMSH proteins interact with components of the endosomal sorting complex required for transport (ESCRT) and are implicated in intracellular trafficking. To investigate how the function of AMSH is regulated at the cellular level, we carried out an interaction screen for the Arabidopsis AMSH proteins and identified the Arabidopsis homolog of apoptosis-linked gene-2 interacting protein X (ALIX) as a protein interacting with AMSH3 in vitro and in vivo. Analysis of alix knockout mutants in Arabidopsis showed that ALIX is essential for plant growth and development and that ALIX is important for the biogenesis of the vacuole and multivesicular bodies (MVBs). Cell biological analysis revealed that ALIX and AMSH3 colocalize on late endosomes. Although ALIX did not stimulate AMSH3 activity in vitro, in the absence of ALIX, AMSH3 localization on endosomes was abolished. Taken together, our data indicate that ALIX could function as an important regulator for AMSH3 function at the late endosomes.

Indexed as

ArabidopsisArabidopsis ProteinsCarrier ProteinsEndosomal Sorting Complexes Required for TransportEndosomesImmunoblottingLuminescent ProteinsMicroscopy, ConfocalMicroscopy, Electron, TransmissionMutationPlant RootsPlants, Genetically ModifiedProtein BindingSeedlingsTwo-Hybrid System TechniquesUbiquitinALIX protein, ArabidopsisAMSH3 protein, ArabidopsisArabidopsis ProteinsCarrier ProteinsEndosomal Sorting Complexes Required for TransportLuminescent ProteinsUbiquitinUbiquitin-Specific ProteasesArabidopsisESCRT-IIIintracellular traffickingubiquitin

Identifiers

PMID26324913
PMCPMC4603487
OpenAlexW2116774289

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.