Evidence map›Paper›PMID 36660928›Full record

ArticleThe Plant cell2023

Mapping the signaling network of BIN2 kinase using TurboID-mediated biotin labeling and phosphoproteomics.

Tae-Wuk Kim, Chan Ho Park, Chuan-Chih Hsu, Yeong-Woo Kim, Yeong-Woo Ko, Zhenzhen Zhang, Jia-Ying Zhu, Yu-Chun Hsiao, Tess Branon, Krista Kaasik and 8 more

Open access · hybridFull text read
In one paragraph

Article in The Plant cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
18.4field-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

55 citing papers in PubMed, 88 citations in OpenAlex.

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  8. CabioRxiv : the preprint server for biology · 2026
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  20. Split-YFP-coupled interaction-dependent TurboID identifies new functions of basal cell polarity inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

18 authors at 6 institutions in 4 countries.

Tae-Wuk KimDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California 94305, USA.ORCID 0000-0003-3941-1897
Chan Ho ParkDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California 94305, USA.ORCID 0000-0001-8104-2621
Chuan-Chih HsuDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California 94305, USA.ORCID 0000-0002-7100-1401
Yeong-Woo KimDepartment of Life Science, Hanyang University, Seoul 04763, South Korea.ORCID 0000-0002-4902-9416
Yeong-Woo KoDepartment of Life Science, Hanyang University, Seoul 04763, South Korea.ORCID 0000-0002-8264-746X
Zhenzhen ZhangDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California 94305, USA.ORCID 0000-0003-1617-8543
Jia-Ying ZhuDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California 94305, USA.ORCID 0000-0002-3773-584X
Yu-Chun HsiaoDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California 94305, USA.ORCID 0000-0002-6571-3584
Tess BranonDepartments of Genetics, Biology, and Chemistry, Stanford University, Stanford, California 94305, USA.ORCID 0000-0002-6520-6419
Krista KaasikDepartment of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, USA.ORCID 0000-0002-2295-1478
Evan SaldivarDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California 94305, USA.ORCID 0000-0002-4383-3550
Kevin LiDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California 94305, USA.ORCID 0000-0003-2038-7217
Asher PashaDepartment of Cell & Systems Biology/Centre for the Analysis of Genome Evolution and Function, University of Toronto, Toronto, Ontario M5S 3B2, Canada.ORCID 0000-0002-9315-0520
Nicholas J ProvartDepartment of Cell & Systems Biology/Centre for the Analysis of Genome Evolution and Function, University of Toronto, Toronto, Ontario M5S 3B2, Canada.ORCID 0000-0001-5551-7232
Alma L BurlingameDepartment of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, USA.ORCID 0000-0002-8403-7307
Shou-Ling XuDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California 94305, USA.ORCID 0000-0002-6741-9506
Alice Y TingDepartments of Genetics, Biology, and Chemistry, Stanford University, Stanford, California 94305, USA.ORCID 0000-0002-8277-5226
Zhi-Yong WangDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California 94305, USA.ORCID 0000-0003-4602-3390
Carnegie Institution for Science · USHanyang University · KRUniversity of California, San Francisco · USUniversity of Toronto · CAChan Zuckerberg Initiative (United States) · USMassachusetts Institute of Technology · US

Funding

Genetic Biochemical Studies of Signaling in Growth and AcclimationR01GM066258 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI ZHIYONG WANG · 2002 to 2026
$10.5M
Spatially-resolved proteomic mapping of living cellsR01CA186568 · NCI · STANFORD UNIVERSITY · PI TING, ALICE Y · 2013 to 2018
$3.3M
NCI NIH HHS R01 CA186568NIGMS NIH HHS R01 GM066258NIH HHS R01GM066258
6 · The paper itself

Abstract

Elucidating enzyme-substrate relationships in posttranslational modification (PTM) networks is crucial for understanding signal transduction pathways but is technically difficult because enzyme-substrate interactions tend to be transient. Here, we demonstrate that TurboID-based proximity labeling (TbPL) effectively and specifically captures the substrates of kinases and phosphatases. TbPL-mass spectrometry (TbPL-MS) identified over 400 proximal proteins of Arabidopsis thaliana BRASSINOSTEROID-INSENSITIVE2 (BIN2), a member of the GLYCOGEN SYNTHASE KINASE 3 (GSK3) family that integrates signaling pathways controlling diverse developmental and acclimation processes. A large portion of the BIN2-proximal proteins showed BIN2-dependent phosphorylation in vivo or in vitro, suggesting that these are BIN2 substrates. Protein-protein interaction network analysis showed that the BIN2-proximal proteins include interactors of BIN2 substrates, revealing a high level of interactions among the BIN2-proximal proteins. Our proteomic analysis establishes the BIN2 signaling network and uncovers BIN2 functions in regulating key cellular processes such as transcription, RNA processing, translation initiation, vesicle trafficking, and cytoskeleton organization. We further discovered significant overlap between the GSK3 phosphorylome and the O-GlcNAcylome, suggesting an evolutionarily ancient relationship between GSK3 and the nutrient-sensing O-glycosylation pathway. Our work presents a powerful method for mapping PTM networks, a large dataset of GSK3 kinase substrates, and important insights into the signaling network that controls key cellular functions underlying plant growth and acclimation.

Indexed as

Protein KinasesProteomicsSignal TransductionArabidopsisArabidopsis ProteinsBiotinBiotinylationBrassinosteroidsPhosphorylationArabidopsis ProteinsAt4g18710 protein, ArabidopsisBiotinBrassinosteroidsProtein Kinases

Identifiers

PMID36660928
PMCPMC10015162
OpenAlexW4317567837

What Socratic holds

Textfull text, public
LicenceCC BY
reference markers read1
measurements read99
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 Socratic graph.