ArticleJournal of proteome research2013
A versatile mass spectrometry-based method to both identify kinase client-relationships and characterize signaling network topology.
Article in Journal of proteome research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Direct coupling of nod factor signaling to vesicular trafficking initiates legume nodulation.Nature communications · 2026Article
- Multimodal knowledge expansion widget powered by plant protein phosphorylation database and ChatGPT.Frontiers in bioinformatics · 2025Article
- Identification of mitogen-activated protein kinases substrates inPlant signaling & behavior · 2024Article
- DecodingPlants (Basel, Switzerland) · 2024Article
- Unveiling orphan receptor-like kinases in plants: novel client discovery using high-confidence library predictions in the Kinase-Client (KiC) assay.Frontiers in plant science · 2024Article
- The Raf-like MAPKKK INTEGRIN-LINKED KINASE 5 regulates purinergic receptor-mediated innate immunity in Arabidopsis.The Plant cell · 2023Article
- Back From the Dead: The Atypical Kinase Activity of a Pseudokinase Regulator of Cation Fluxes During Inducible Immunity.Frontiers in plant science · 2022Article
- S-acylation of P2K1 mediates extracellular ATP-induced immune signaling in Arabidopsis.Nature communications · 2021Article
- Extracellular ATP elicits DORN1-mediated RBOHD phosphorylation to regulate stomatal aperture.Nature communications · 2017Article
- Identification of the phosphorylation targets of symbiotic receptor-like kinases using a high-throughput multiplexed assay for kinase specificity.The Plant journal : for cell and molecular biology · 2017Article
- Activation of the LRR Receptor-Like Kinase PSY1R Requires Transphosphorylation of Residues in the Activation Loop.Frontiers in plant science · 2017Article
- Two SERK Receptor-Like Kinases Interact with EMS1 to Control Anther Cell Fate Determination.Plant physiology · 2017Article
- Quantitative Phosphoproteomic Analysis of T-Cell Receptor Signaling.Methods in molecular biology (Clifton, N.J.) · 2017Article
- The Raf-like Kinase ILK1 and the High Affinity K+ Transporter HAK5 Are Required for Innate Immunity and Abiotic Stress Response.Plant physiology · 2016Article
- Substrate thiophosphorylation by Arabidopsis mitogen-activated protein kinases.BMC plant biology · 2016Article
- The Emerging Role of Protein Phosphorylation as a Critical Regulatory Mechanism Controlling Cellulose Biosynthesis.Frontiers in plant science · 2016Review
- Advantages and limitations of shot-gun proteomic analyses on Arabidopsis plants with altered MAPK signaling.Frontiers in plant science · 2015Article
- P³DB 3.0: From plant phosphorylation sites to protein networks.Nucleic acids research · 2014Article
- Circles within circles: crosstalk between protein Ser/Thr/Tyr-phosphorylation and Met oxidation.BMC bioinformatics · 2013Article
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Authors and funding
8 authors.
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Abstract
While more than a thousand protein kinases (PK) have been identified in the Arabidopsis thaliana genome, relatively little progress has been made toward identifying their individual client proteins. Herein we describe the use of a mass spectrometry-based in vitro phosphorylation strategy, termed Kinase Client assay (KiC assay), to study a targeted-aspect of signaling. A synthetic peptide library comprising 377 in vivo phosphorylation sequences from developing seed was screened using 71 recombinant A. thaliana PK. Among the initial results, we identified 23 proteins as putative clients of 17 PK. In one instance protein phosphatase inhibitor-2 (AtPPI-2) was phosphorylated at multiple-sites by three distinct PK, casein kinase1-like 10, AME3, and a Ser PK-like protein. To confirm this result, full-length recombinant AtPPI-2 was reconstituted with each of these PK. The results confirmed multiple distinct phosphorylation sites within this protein. Biochemical analyses indicate that AtPPI-2 inhibits type 1 protein phosphatase (TOPP) activity, and that the phosphorylated forms of AtPPI-2 are more potent inhibitors. Structural modeling revealed that phosphorylation of AtPPI-2 induces conformational changes that modulate TOPP binding.
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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.