Evidence map›Paper›PMID 27208306›Full record

ArticlePlant physiology2016

Unraveling K63 Polyubiquitination Networks by Sensor-Based Proteomics.

Alexander Johnson, Grégory Vert

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.1field-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

27 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Decoding Ubiquitin Modifications by Mass Spectrometry.Advances in experimental medicine and biology · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Root Membrane Ubiquitinome under Short-Term Osmotic Stress.International journal of molecular sciences · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

2 authors at 1 institution in 1 country.

Alexander JohnsonInstitute for Integrative Biology of the Cell (I2BC), CNRS/CEA/Univ. Paris Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette, France.
Grégory VertInstitute for Integrative Biology of the Cell (I2BC), CNRS/CEA/Univ. Paris Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette, France gregory.vert@i2bc.paris-saclay.fr.
CEA Paris-Saclay · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The polybiquitination of proteins can take on different topologies depending on the residue from ubiquitin involved in the chain formation. Although the role of lysine-48 (K48) polyubiquitination in proteasome-mediated degradation is fairly well characterized, much less is understood about the other types of ubiquitin chains and proteasome-independent functions. To overcome this, we developed a K63 polyubiquitin-specific sensor-based approach to track and isolate K63 polyubiquitinated proteins in plants. Proteins carrying K63 polyubiquitin chains were found to be enriched in diverse membrane compartments as well as in nuclear foci. Using liquid chromatography-tandem mass spectrometry, we identified over 100 proteins from Arabidopsis (Arabidopsis thaliana) that are modified with K63 polyubiquitin chains. The K63 ubiquitinome contains critical factors involved in a wide variety of biological processes, including transport, metabolism, protein trafficking, and protein translation. Comparison of the proteins found in this study with previously published nonresolutive ubiquitinomes identified about 70 proteins as ubiquitinated and specifically modified with K63-linked chains. To extend our knowledge about K63 polyubiquitination, we compared the K63 ubiquitinome with K63 ubiquitination networks based on the Arabidopsis interactome. Altogether, this work increases our resolution of the cellular and biological roles associated with this poorly characterized posttranslational modification and provides a unique insight into the networks of K63 polyubiquitination in plants.

Indexed as

ArabidopsisArabidopsis ProteinsBiosensing TechniquesEndosomal Sorting Complexes Required for TransportLysinePlants, Genetically ModifiedProtein TransportProteomicsSaccharomyces cerevisiae ProteinsTandem Mass SpectrometryUbiquitinationArabidopsis ProteinsEndosomal Sorting Complexes Required for TransportLysineSaccharomyces cerevisiae ProteinsVPS27 protein, S cerevisiae

Identifiers

PMID27208306
PMCPMC4936586
OpenAlexW2353658081

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.