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Application of TurboID-mediated proximity labeling for mapping a GSK3 kinase signaling network in Arabidopsis

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/pmic.201700002openalex-snapshot

Proximity Labeling of Interacting Proteins: Application of BioID as a Discovery Tool

inferredcites →https://doi.org/10.1016/j.cbpa.2018.10.017openalex-snapshot

Getting to know the neighborhood: using proximity-dependent biotinylation to characterize protein complexes and map organelles

inferredcites →https://doi.org/10.1016/j.cell.2017.03.022openalex-snapshot

An Approach to Spatiotemporally Resolve Protein Interaction Networks in Living Cells

inferredcites →https://doi.org/10.1016/j.chembiol.2017.02.002openalex-snapshot

Proximity Biotinylation as a Method for Mapping Proteins Associated with mtDNA in Living Cells

inferredcites →https://doi.org/10.1016/j.conb.2017.10.015openalex-snapshot

Proximity labeling: spatially resolved proteomic mapping for neurobiology

inferredcites →https://doi.org/10.1016/j.cub.2015.08.033openalex-snapshot

OCTOPUS Negatively Regulates BIN2 to Control Phloem Differentiation in Arabidopsis thaliana

inferredcites →https://doi.org/10.1016/j.jgg.2016.05.007openalex-snapshot

The Arabidopsis B-box protein BZS1/BBX20 interacts with HY5 and mediates strigolactone regulation of photomorphogenesis

inferredcites →https://doi.org/10.1016/j.molcel.2017.05.012openalex-snapshot

The F-box Protein KIB1 Mediates Brassinosteroid-Induced Inactivation and Degradation of GSK3-like Kinases in Arabidopsis

inferredcites →https://doi.org/10.1016/j.molp.2014.12.006openalex-snapshot

Functional Insights of Plant GSK3-like Kinases: Multi-Taskers in Diverse Cellular Signal Transduction Pathways

inferredcites →https://doi.org/10.1016/j.molp.2016.09.016openalex-snapshot

Immunopurification and Mass Spectrometry Identifies Protein Phosphatase 2A (PP2A) and BIN2/GSK3 as Regulators of AKS Transcription Factors in Arabidopsis

inferredcites →https://doi.org/10.1016/j.tibs.2017.05.003openalex-snapshot

Close Encounters – Probing Proximal Proteins in Live or Fixed Cells

inferredcites →https://doi.org/10.1038/nature10794openalex-snapshot

Brassinosteroid regulates stomatal development by GSK3-mediated inhibition of a MAPK pathway

inferredcites →https://doi.org/10.1038/nbt.1511openalex-snapshot

MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification

inferredcites →https://doi.org/10.1038/nbt.2839openalex-snapshot

ProteomeXchange provides globally coordinated proteomics data submission and dissemination

inferredcites →https://doi.org/10.1038/nbt.4201openalex-snapshot

Efficient proximity labeling in living cells and organisms with TurboID

inferredcites →https://doi.org/10.1038/ncb1970openalex-snapshot

Brassinosteroid signal transduction from cell-surface receptor kinases to nuclear transcription factors

inferredcites →https://doi.org/10.1038/ncb2151openalex-snapshot

PP2A activates brassinosteroid-responsive gene expression and plant growth by dephosphorylating BZR1

inferredcites →https://doi.org/10.1038/ncb2471openalex-snapshot

SPEECHLESS integrates brassinosteroid and stomata signalling pathways

inferredcites →https://doi.org/10.1038/ncb2893openalex-snapshot

A secreted peptide acts on BIN2-mediated phosphorylation of ARFs to potentiate auxin response during lateral root development

inferredcites →https://doi.org/10.1038/ncomms4504openalex-snapshot

Plant GSK3 proteins regulate xylem cell differentiation downstream of TDIF–TDR signalling

inferredcites →https://doi.org/10.1038/nmeth.3901openalex-snapshot

The Perseus computational platform for comprehensive analysis of (prote)omics data

inferredcites →https://doi.org/10.1038/nmeth.4343openalex-snapshot

CrY2H-seq: a massively multiplexed assay for deep-coverage interactome mapping

inferredcites →https://doi.org/10.1038/nprot.2007.261openalex-snapshot

Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips

inferredcites →https://doi.org/10.1038/s41586-018-0714-xopenalex-snapshot

POLAR-guided signalling complex assembly and localization drive asymmetric cell division

inferredcites →https://doi.org/10.1038/s41598-018-27500-3openalex-snapshot

In planta proximity dependent biotin identification (BioID)

inferredcites →https://doi.org/10.1073/pnas.0803996105openalex-snapshot

Integration of auxin and brassinosteroid pathways by Auxin Response Factor 2

inferredcites →https://doi.org/10.1073/pnas.0812346106openalex-snapshot

Three related receptor-like kinases are required for optimal cell elongation in Arabidopsis thaliana

inferredcites →https://doi.org/10.1073/pnas.1316717111openalex-snapshot

GSK3-like kinases positively modulate abscisic acid signaling through phosphorylating subgroup III SnRK2s in Arabidopsis

inferredcites →https://doi.org/10.1073/pnas.1406459111openalex-snapshot

Probing nuclear pore complex architecture with proximity-dependent biotinylation

inferredcites →https://doi.org/10.1073/pnas.152342599openalex-snapshot

The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a positive regulator of the brassinosteroid signaling pathway in Arabidopsis

inferredcites →https://doi.org/10.1074/jbc.m110.142547openalex-snapshot

A Direct Docking Mechanism for a Plant GSK3-like Kinase to Phosphorylate Its Substrates

inferredcites →https://doi.org/10.1074/mcp.tir118.000702openalex-snapshot

Universal Plant Phosphoproteomics Workflow and Its Application to Tomato Signaling in Response to Cold Stress*

inferredcites →https://doi.org/10.1083/jcb.201112098openalex-snapshot

A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells

inferredcites →https://doi.org/10.1104/pp.103.036897openalex-snapshot

Brassinosteroids Interact with Auxin to Promote Lateral Root Development in Arabidopsis

inferredcites →https://doi.org/10.1104/pp.105.064444openalex-snapshot

A Brassinosteroid-Hypersensitive Mutant of BAK1 Indicates That a Convergence of Photomorphogenic and Hormonal Signaling Modulates Phototropism

inferredcites →https://doi.org/10.1104/pp.123.3.997openalex-snapshot

Involvement of Brassinosteroids in the Gravitropic Response of Primary Root of Maize

inferredcites →https://doi.org/10.1111/tpj.12175openalex-snapshot

BSK s are partially redundant positive regulators of brassinosteroid signaling in A rabidopsis

inferredcites →https://doi.org/10.1126/science.1065769openalex-snapshot

Regulation of Brassinosteroid Signaling by a GSK3/SHAGGY-Like Kinase

inferredcites →https://doi.org/10.1126/science.1156973openalex-snapshot

BSKs Mediate Signal Transduction from the Receptor Kinase BRI1 in Arabidopsis

inferredcites →https://doi.org/10.1126/science.1203877openalex-snapshot

Evidence for Network Evolution in an Arabidopsis Interactome Map

inferredcites →https://doi.org/10.1126/science.1250778openalex-snapshot

A mutually assured destruction mechanism attenuates light signaling in Arabidopsis

inferredcites →https://doi.org/10.1126/science.1251358openalex-snapshot

Border Control—A Membrane-Linked Interactome of Arabidopsis

inferredcites →https://doi.org/10.1126/science.aag0821openalex-snapshot

Identification of an elaborate complex mediating postsynaptic inhibition

inferredcites →https://doi.org/10.1126/scisignal.260pe11openalex-snapshot

How Perfect Can Protein Interactomes Be?

inferredcites →https://doi.org/10.1146/annurev-arplant-050312-120140openalex-snapshot

Plant Protein Interactomes

inferredcites →https://doi.org/10.1146/annurev.arplant.043008.092057openalex-snapshot

Brassinosteroid Signal Transduction from Receptor Kinases to Transcription Factors

inferredcites →https://doi.org/10.12688/f1000research.16903.1openalex-snapshot

Recent advances in proximity-based labeling methods for interactome mapping

inferredcites →https://doi.org/10.3389/fpls.2017.00749openalex-snapshot

Screening of Proximal and Interacting Proteins in Rice Protoplasts by Proximity-Dependent Biotinylation

inferredcites →https://doi.org/10.3389/fpls.2018.00640openalex-snapshot

Recent Trends in Plant Protein Complex Analysis in a Developmental Context

inferredcites →https://doi.org/10.3389/fpls.2018.01882openalex-snapshot

Development of a Rapid in planta BioID System as a Probe for Plasma Membrane-Associated Immunity Proteins

inferredcites →https://doi.org/10.7554/elife.02525openalex-snapshot

Brassinosteroids control root epidermal cell fate via direct regulation of a MYB-bHLH-WD40 complex by GSK3-like kinases

inferredcites →https://doi.org/10.7554/elife.47864openalex-snapshot

Proximity labeling of protein complexes and cell-type-specific organellar proteomes in Arabidopsis enabled by TurboID

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1002/wdev.392openalex-snapshot

Proximity‐dependent labeling methods for proteomic profiling in living cells: An update

inferred← citeshttps://doi.org/10.1007/978-1-0716-0880-7_21openalex-snapshot

Biotin-Based Proximity Labeling of Protein Complexes in Planta

inferred← citeshttps://doi.org/10.1007/978-1-0716-3327-4_26openalex-snapshot

Cataloguing Protein Complexes In Planta Using TurboID-Catalyzed Proximity Labeling

inferred← citeshttps://doi.org/10.1007/s42977-025-00302-1openalex-snapshot

Protein–protein interaction detection in plants: from classical approaches to future perspectives

inferred← citeshttps://doi.org/10.1016/j.cell.2023.05.049openalex-snapshot

Pathogen protein modularity enables elaborate mimicry of a host phosphatase

inferred← citeshttps://doi.org/10.1016/j.tplants.2022.12.006openalex-snapshot

Mass spectrometric exploration of phytohormone profiles and signaling networks

inferred← citeshttps://doi.org/10.1016/j.xplc.2020.100137openalex-snapshot

Proximity labeling: an emerging tool for probing in planta molecular interactions

inferred← citeshttps://doi.org/10.1016/j.xplc.2021.100186openalex-snapshot

Endoplasmic reticulum-related E3 ubiquitin ligases: Key regulators of plant growth and stress responses

inferred← citeshttps://doi.org/10.1016/j.xpro.2023.102577openalex-snapshot

Protocol to identify protein-protein interaction networks in Solanum tuberosum using transient TurboID-based proximity labeling

inferred← citeshttps://doi.org/10.1038/s41467-021-20929-7openalex-snapshot

Arabidopsis ACINUS is O-glycosylated and regulates transcription and alternative splicing of regulators of reproductive transitions

inferred← citeshttps://doi.org/10.1038/s41467-024-48313-1openalex-snapshot

Receptor-like cytoplasmic kinases of different subfamilies differentially regulate SOBIR1/BAK1-mediated immune responses in Nicotiana benthamiana

inferred← citeshttps://doi.org/10.1042/etls20200270openalex-snapshot

Mapping the plant proteome: tools for surveying coordinating pathways

inferred← citeshttps://doi.org/10.1073/pnas.2118220119openalex-snapshot

Proteome-wide cellular thermal shift assay reveals unexpected cross-talk between brassinosteroid and auxin signaling

inferred← citeshttps://doi.org/10.1101/2021.03.01.433373openalex-snapshot

MoBiFC: development of a modular bimolecular fluorescence complementation toolkit for the analysis of chloroplast protein-protein interactions

inferred← citeshttps://doi.org/10.1101/2021.12.14.472597openalex-snapshot

Proteome-wide cellular thermal shift assay reveals novel crosstalk between brassinosteroid and auxin signaling

inferred← citeshttps://doi.org/10.1105/tpc.20.00235openalex-snapshot

Establishment of Proximity-Dependent Biotinylation Approaches in Different Plant Model Systems

inferred← citeshttps://doi.org/10.1111/pce.70194openalex-snapshot

Signalling Networks Underlying Cell Wall Responses to Salinity Stress

inferred← citeshttps://doi.org/10.1111/tpj.16157openalex-snapshot

Engineering the plant metabolic system by exploiting metabolic regulation

inferred← citeshttps://doi.org/10.1186/s13007-022-00902-1openalex-snapshot

MoBiFC: development of a modular bimolecular fluorescence complementation toolkit for the analysis of chloroplast protein–protein interactions

inferred← citeshttps://doi.org/10.18174/511017openalex-snapshot

Proteomics perspective on auxin biology

inferred← citeshttps://doi.org/10.18174/636038openalex-snapshot

Tubers and time : Exploring the intricate link between tuberization and senescence

inferred← citeshttps://doi.org/10.21203/rs.3.rs-1084155/v1openalex-snapshot

Profiling of associated proteins reveals dual functions of the phosphatase ABI1 in abscisic acid signaling

inferred← citeshttps://doi.org/10.3389/fpls.2022.832585openalex-snapshot

Application of Parallel Reaction Monitoring in 15N Labeled Samples for Quantification

inferred← citeshttps://doi.org/10.3389/fpls.2022.974598openalex-snapshot

Potential application of TurboID-based proximity labeling in studying the protein interaction network in plant response to abiotic stress

inferred← citeshttps://doi.org/10.3389/fpls.2023.1240973openalex-snapshot

RAB7 GTPases as coordinators of plant endomembrane traffic

inferred← citeshttps://doi.org/10.3390/ijms21218179openalex-snapshot

State-of-the-Art Technologies for Understanding Brassinosteroid Signaling Networks

inferred← citeshttps://doi.org/10.3390/ijms22063260openalex-snapshot

Maintenance of Cell Wall Integrity under High Salinity

inferred← citeshttps://doi.org/10.3390/ijms22137101openalex-snapshot

From Affinity to Proximity Techniques to Investigate Protein Complexes in Plants

inferred← citeshttps://doi.org/10.53846/goediss-10180openalex-snapshot

Regulation of plant stress responses by clade I TGA transcription factors and interacting CC-type glutaredoxins

inferred← citeshttps://doi.org/10.6084/m9.figshare.19898881openalex-snapshot

Additional file 1 of MoBiFC: development of a modular bimolecular fluorescence complementation toolkit for the analysis of chloroplast protein–protein interactions

inferred← citeshttps://doi.org/10.6084/m9.figshare.19898890openalex-snapshot

Additional file 3 of MoBiFC: development of a modular bimolecular fluorescence complementation toolkit for the analysis of chloroplast protein–protein interactions

inferred← citeshttps://doi.org/10.7554/elife.52770openalex-snapshot

Proximity proteomics in a marine diatom reveals a putative cell surface-to-chloroplast iron trafficking pathway

inferred← citeshttps://doi.org/10.7554/elife.66877openalex-snapshot

Vision, challenges and opportunities for a Plant Cell Atlas

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