Evidence map›Paper›PMID 28461270›Full record

ArticleMolecular plant2017

Mass Spectrometric Analyses Reveal a Central Role for Ubiquitylation in Remodeling the Arabidopsis Proteome during Photomorphogenesis.

Victor Aguilar-Hernández, Do-Young Kim, Robert J Stankey, Mark Scalf, Lloyd M Smith, Richard D Vierstra

Open access · bronzeAbstract read
In one paragraph

Article in Molecular plant, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

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  12. Differing biophysical properties underpin the unique signaling potentials within the plant phytochrome photoreceptor families.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

6 authors at 2 institutions in 1 country.

Victor Aguilar-HernándezDepartment of Biology, Washington University in St. Louis, Campus Box 1137, One Brookings Drive, St. Louis, MO 63130, USA; Department of Genetics, 425-G Henry Mall, University of Wisconsin-Madison, Madison, WI 53706, USA.
Do-Young KimDepartment of Genetics, 425-G Henry Mall, University of Wisconsin-Madison, Madison, WI 53706, USA.
Robert J StankeyDepartment of Genetics, 425-G Henry Mall, University of Wisconsin-Madison, Madison, WI 53706, USA.
Mark ScalfDepartment of Chemistry, 1101 University Avenue, University of Wisconsin-Madison, Madison, WI 53706, USA.
Lloyd M SmithDepartment of Chemistry, 1101 University Avenue, University of Wisconsin-Madison, Madison, WI 53706, USA.
Richard D VierstraDepartment of Biology, Washington University in St. Louis, Campus Box 1137, One Brookings Drive, St. Louis, MO 63130, USA; Department of Genetics, 425-G Henry Mall, University of Wisconsin-Madison, Madison, WI 53706, USA. Electronic address: rdvierstra@wustl.edu.
University of Wisconsin–Madison · USWashington University in St. Louis · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007133 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI PERNA, NICOLE T · 1985 to 2023
$16.5M
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 P50 HG004952NIGMS NIH HHS P01 GM081629NIGMS NIH HHS T32 GM007133
6 · The paper itself

Abstract

The switch from skotomorphogenesis to photomorphogenesis is a key developmental transition in the life of seed plants. While much of the underpinning proteome remodeling is driven by light-induced changes in gene expression, the proteolytic removal of specific proteins by the ubiquitin-26S proteasome system is also likely paramount. Through mass spectrometric analysis of ubiquitylated proteins affinity-purified from etiolated Arabidopsis seedlings before and after red-light irradiation, we identified a number of influential proteins whose ubiquitylation status is modified during this switch. We observed a substantial enrichment for proteins involved in auxin, abscisic acid, ethylene, and brassinosteroid signaling, peroxisome function, disease resistance, protein phosphorylation and light perception, including the phytochrome (Phy) A and phototropin photoreceptors. Soon after red-light treatment, PhyA becomes the dominant ubiquitylated species, with ubiquitin attachment sites mapped to six lysines. A PhyA mutant protected from ubiquitin addition at these sites is substantially more stable in planta upon photoconversion to Pfr and is hyperactive in driving photomorphogenesis. However, light still stimulates ubiquitylation and degradation of this mutant, implying that other attachment sites and/or proteolytic pathways exist. Collectively, we expand the catalog of ubiquitylation targets in Arabidopsis and show that this post-translational modification is central to the rewiring of plants for photoautotrophic growth.

Indexed as

ArabidopsisArabidopsis ProteinsGene Expression Regulation, PlantMass SpectrometryPhytochromePlants, Genetically ModifiedProteasome Endopeptidase ComplexProteomeSignal TransductionUbiquitinationArabidopsis ProteinsATP dependent 26S proteasePhytochromeProteasome Endopeptidase ComplexProteomeArabidopsismass spectrometryphotomorphogenesisphytochrome degradationubiquitin

Identifiers

PMID28461270
PMCPMC5695678
OpenAlexW2608509813

What OpenQuestion holds

Textmetadata
LicenceTDM
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.