Evidence map›Paper›PMID 39570863›Full record

ArticleThe Plant cell2024

Quantitative proteomics reveals extensive lysine ubiquitination and transcription factor stability states in Arabidopsis.

Gaoyuan Song, Christian Montes, Damilola Olatunji, Shikha Malik, Chonghui Ji, Natalie M Clark, Yunting Pu, Dior R Kelley, Justin W Walley

Abstract read
In one paragraph

Article in The Plant cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. 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

9 authors.

Gaoyuan SongDepartment of Plant Pathology, Entomology, and Microbiology, Iowa State University, Ames, IA 50014, USA.ORCID 0000-0003-1633-9159
Christian MontesDepartment of Plant Pathology, Entomology, and Microbiology, Iowa State University, Ames, IA 50014, USA.ORCID 0000-0003-1249-2308
Damilola OlatunjiDepartment of Genetics, Development and Cell Biology, Iowa State University, Ames, IA 50014, USA.ORCID 0000-0002-0829-7254
Shikha MalikDepartment of Plant Pathology, Entomology, and Microbiology, Iowa State University, Ames, IA 50014, USA.ORCID 0009-0005-9676-8341
Chonghui JiFujian Provincial Key Laboratory of Haixia Applied Plant Systems Biology, Haixia Institute of Science and Technology, Fujian Agriculture and Forestry University, Fuzhou 350002, China.ORCID 0000-0003-2724-0859
Natalie M ClarkDepartment of Plant Pathology, Entomology, and Microbiology, Iowa State University, Ames, IA 50014, USA.ORCID 0000-0003-0988-321X
Yunting PuDepartment of Genetics, Development and Cell Biology, Iowa State University, Ames, IA 50014, USA.ORCID 0000-0001-8744-6141
Dior R KelleyDepartment of Genetics, Development and Cell Biology, Iowa State University, Ames, IA 50014, USA.ORCID 0000-0001-9186-4186
Justin W WalleyDepartment of Plant Pathology, Entomology, and Microbiology, Iowa State University, Ames, IA 50014, USA.ORCID 0000-0001-7553-2237

Funding

Crosstalk between Brassinosteroid and autophagy pathways in the regulation of plant growth and stress responses: Equipment SupplementR01GM120316 · NIGMS · IOWA STATE UNIVERSITY · PI DIANE C BASSHAM, Justin William Walley · 2017 to 2026
$2.0M
Hatch IOW3808Iowa State UniversityISU R01GM120316ISU Crop Bioengineering Center 2019-67012-29712NIGMS NIH HHS R01 GM120316USDA NIFA
6 · The paper itself

Abstract

Protein activity, abundance, and stability can be regulated by post-translational modification including ubiquitination. Ubiquitination is conserved among eukaryotes and plays a central role in modulating cellular function; yet, we lack comprehensive catalogs of proteins that are modified by ubiquitin in plants. In this study, we describe an antibody-based approach to enrich ubiquitinated peptides coupled with isobaric labeling to enable quantification of up to 18-multiplexed samples. This approach identified 17,940 ubiquitinated lysine sites arising from 6,453 proteins from Arabidopsis (Arabidopsis thaliana) primary roots, seedlings, and rosette leaves. Gene ontology analysis indicated that ubiquitinated proteins are associated with numerous biological processes including hormone signaling, plant defense, protein homeostasis, and metabolism. We determined ubiquitinated lysine residues that directly regulate the stability of three transcription factors, CRYPTOCHROME-INTERACTING BASIC-HELIX-LOOP-HELIX 1 (CIB1), CIB1 LIKE PROTEIN 2 (CIL2), and SENSITIVE TO PROTON RHIZOTOXICITY1 (STOP1) using in vivo degradation assays. Furthermore, codon mutation of CIB1 to create a K166R conversion to prevent ubiquitination, via CRISPR/Cas9-derived adenosine base editing, led to an early flowering phenotype and increased expression of FLOWERING LOCUS T (FT). These comprehensive site-level ubiquitinome profiles provide a wealth of data for future functional studies related to modulation of biological processes mediated by this post-translational modification in plants.

Indexed as

ArabidopsisArabidopsis ProteinsLysineProteomicsTranscription FactorsUbiquitinationGene Expression Regulation, PlantProtein StabilityArabidopsis ProteinsLysineTranscription Factors

Identifiers

PMID39570863
PMCPMC11663597

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Registered trials

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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.