ArticleMolecular plant2013
Salt stress triggers phosphorylation of the Arabidopsis vacuolar K+ channel TPK1 by calcium-dependent protein kinases (CDPKs).
Article in Molecular plant, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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91 citing papers in PubMed, 188 citations in OpenAlex.
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- Calcium-Dependent Protein Kinases in Plants: Structure, Signaling, and Multifaceted Regulatory Roles in Development and Stress Adaptation.International journal of molecular sciences · 2026Review
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- Omics-Driven Strategies for Developing Saline-Smart Lentils: A Comprehensive Review.International journal of molecular sciences · 2024Review
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- OsCPK12 phosphorylates OsCATA and OsCATC to regulate HPlant communications · 2024Article
- Identification and expression analysis of calcium-dependent protein kinase family in oat (Frontiers in plant science · 2024Article
- Resveratrol enhances the tolerance ofFrontiers in plant science · 2024Article
- Ion Changes and Signaling under Salt Stress in Wheat and Other Important Crops.Plants (Basel, Switzerland) · 2023Review
- Co-Expression Network Analysis of the Transcriptome Identified Hub Genes and Pathways Responding to Saline-Alkaline Stress inInternational journal of molecular sciences · 2023Article
- How Plants Tolerate Salt Stress.Current issues in molecular biology · 2023Review
31 more citing papers are in PubMed but not listed here.
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10 authors at 2 institutions in 3 countries.
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Abstract
14-3-3 proteins play an important role in the regulation of many cellular processes. The Arabidopsis vacuolar two-pore K(+) channel 1 (TPK1) interacts with the 14-3-3 protein GRF6 (GF14-λ). Upon phosphorylation of the putative binding motif in the N-terminus of TPK1, GRF6 binds to TPK1 and activates the potassium channel. In order to gain a deeper understanding of this 14-3-3-mediated signal transduction, we set out to identify the respective kinases, which regulate the phosphorylation status of the 14-3-3 binding motif in TPK1. Here, we report that the calcium-dependent protein kinases (CDPKs) can phosphorylate and thereby activate the 14-3-3 binding motif in TPK1. Focusing on the stress-activated kinase CPK3, we visualized direct and specific interaction of TPK1 with the kinase at the tonoplast in vivo. In line with its proposed role in K(+) homeostasis, TPK1 phosphorylation was found to be induced by salt stress in planta, and both cpk3 and tpk1 mutants displayed salt-sensitive phenotypes. Molecular modeling of the TPK1-CPK3 interaction domain provided mechanistic insights into TPK1 stress-regulated phosphorylation responses and pinpointed two arginine residues in the N-terminal 14-3-3 binding motif in TPK1 critical for kinase interaction. Taken together, our studies provide evidence for an essential role of the vacuolar potassium channel TPK1 in salt-stress adaptation as a target of calcium-regulated stress signaling pathways involving Ca(2+), Ca(2+)-dependent kinases, and 14-3-3 proteins.
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