Evidence map›Paper›PMID 23667124›Full record

ArticleThe Plant cell2013

Advanced proteomic analyses yield a deep catalog of ubiquitylation targets in Arabidopsis.

Do-Young Kim, Mark Scalf, Lloyd M Smith, Richard D Vierstra

Open access · greenAbstract 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 133 papers.

0numbers the graph read from it
0cells of the map it votes in
133citing papers in PubMed
11.7field-weighted citation impact, top 1% 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

133 citing papers in PubMed, 240 citations in OpenAlex.

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73 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Do-Young KimDepartment of Genetics, University of Wisconsin, Madison, Wisconsin 53706, USA.
Mark Scalf
Lloyd M Smith
Richard D Vierstra
University of Wisconsin–Madison · USUniversity of Wisconsin System · US

Funding

Wisconsin Center of Excellence in Genomics ScienceP50HG004952 · NHGRI · TEXAS BIOMEDICAL RESEARCH INSTITUTE · PI OLIVIER, MICHAEL · 2009 to 2013
$13.0M
The Epigenotype of Human ES CellsP01GM081629 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI THOMSON, JAMES ALEXANDER · 2008 to 2012
$8.9M
NHGRI NIH HHS 1P50HG004952NHGRI NIH HHS P50 HG004952NIGMS NIH HHS P01 GM081629NIGMS NIH HHS P01GM081629
6 · The paper itself

Abstract

The posttranslational addition of ubiquitin (Ub) profoundly controls the half-life, interactions, and/or trafficking of numerous intracellular proteins. Using stringent two-step affinity methods to purify Ub-protein conjugates followed by high-sensitivity mass spectrometry, we identified almost 950 ubiquitylation substrates in whole Arabidopsis thaliana seedlings. The list includes key factors regulating a wide range of biological processes, including metabolism, cellular transport, signal transduction, transcription, RNA biology, translation, and proteolysis. The ubiquitylation state of more than half of the targets increased after treating seedlings with the proteasome inhibitor MG132 (carbobenzoxy-Leu-Leu-Leu-al), strongly suggesting that Ub addition commits many to degradation by the 26S proteasome. Ub-attachment sites were resolved for a number of targets, including six of the seven Lys residues on Ub itself with a Lys-48>Lys-63>Lys-11>>>Lys-33/Lys-29/Lys-6 preference. However, little sequence consensus was detected among conjugation sites, indicating that the local environment has little influence on global ubiquitylation. Intriguingly, the level of Lys-11-linked Ub polymers increased substantially upon MG132 treatment, revealing that they might be important signals for proteasomal breakdown. Taken together, this proteomic analysis illustrates the breadth of plant processes affected by ubiquitylation and provides a deep data set of individual targets from which to explore the roles of Ub in various physiological and developmental pathways.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsCysteine Proteinase InhibitorsImmunoblottingLeupeptinsLysineMass SpectrometryPlants, Genetically ModifiedProteasome Endopeptidase ComplexProteomeProteomicsUbiquitinUbiquitinated ProteinsUbiquitinationArabidopsis Proteinsbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCysteine Proteinase InhibitorsLeupeptinsLysineProteasome Endopeptidase ComplexProteomeUbiquitinUbiquitinated Proteins

Identifiers

PMID23667124
PMCPMC3694690
OpenAlexW2101066284

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.