ArticleThe Journal of biological chemistry2013
The variable domain of a plant calcium-dependent protein kinase (CDPK) confers subcellular localization and substrate recognition for NADPH oxidase.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 126 citations in OpenAlex.
- Aspects of plant intelligence (ii).Plant signaling & behavior · 2026Review
- Calcium-Dependent Protein Kinases in Plants: Structure, Signaling, and Multifaceted Regulatory Roles in Development and Stress Adaptation.International journal of molecular sciences · 2026Review
- Genomic survey and expression analysis of the CDPK genes in Liriodendron Chinense to explore their potential functions under multiple abiotic stresses.BMC genomics · 2026Article
- Visualization and Quantification of Apoplastic ROS by Plant Immune NADPH Oxidase Utilizing Chemiluminescence.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Interdependence of plasma membrane nanoscale dynamics of a kinase and its cognate substrate underlieseLife · 2025Article
- CDPK5 and CDPK13 play key roles in acclimation to low oxygen through the control of RBOH-mediated ROS production in rice.Plant physiology · 2024Article
- CDPK protein in cotton: genomic-wide identification, expression analysis, and conferring resistance to heat stress.BMC plant biology · 2024Article
- Micronutrient deficiency-induced oxidative stress in plants.Plant cell reports · 2024Review
- OsCPK12 phosphorylates OsCATA and OsCATC to regulate HPlant communications · 2024Article
- Types of Membrane Transporters and the Mechanisms of Interaction between Them and Reactive Oxygen Species in Plants.Antioxidants (Basel, Switzerland) · 2024Review
- Identification ofFrontiers in plant science · 2024Article
- Cytoplasmic Kinase Network Mediates Defense Response toPlants (Basel, Switzerland) · 2023Article
- Review of the Mechanisms by Which Transcription Factors and Exogenous Substances Regulate ROS Metabolism under Abiotic Stress.Antioxidants (Basel, Switzerland) · 2022Review
- Receptor for Activated C Kinase1B (OsRACK1B) Impairs Fertility in Rice through NADPH-Dependent HInternational journal of molecular sciences · 2022Article
- The Dually Localized EF-Hand Domain-Containing Protein TgEFP1 Regulates the Lytic Cycle ofCells · 2022Article
- Article
- The role of CDPKs in plant development, nutrient and stress signaling.Frontiers in genetics · 2022Review
- Molecular Characterization Reveals the Involvement of Calcium Dependent Protein Kinases in Abiotic Stress Signaling and Development in Chickpea (Frontiers in plant science · 2022Article
- Fungal genomes: suffering with functional annotation errors.IMA fungus · 2021Article
- Carbon/nitrogen metabolism and stress response networks - calcium-dependent protein kinases as the missing link?Journal of experimental botany · 2021Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calcium-dependent protein kinases (CDPKs) are Ca(2+) sensors that regulate diverse biological processes in plants and apicomplexans. However, how CDPKs discriminate specific substrates in vivo is still largely unknown. Previously, we found that a potato StCDPK5 is dominantly localized to the plasma membrane and activates the plasma membrane NADPH oxidase (RBOH; for respiratory burst oxidase homolog) StRBOHB by direct phosphorylation of the N-terminal region. Here, we report the contribution of the StCDPK5 N-terminal variable (V) domain to activation of StRBOHB in vivo using heterologous expression system in Nicotiana benthamiana. Mutations of N-terminal myristoylation and palmitoylation sites in the V domain eliminated the predominantly plasma membrane localization and the capacity of StCDPK5 to activate StRBOHB in vivo. A tomato SlCDPK2, which also contains myristoylation and palmitoylation sites in its N terminus, phosphorylated StRBOHB in vitro but not in vivo. Functional domains responsible for activation and phosphorylation of StRBOHB were identified by swapping regions for each domain between StCDPK5 and SlCDPK2. The substitution of the V domain of StCDPK5 with that of SlCDPK2 abolished the activation and phosphorylation abilities of StRBOHB in vivo and relocalized the chimeric CDPK to the trans-Golgi network, as observed for SlCDPK2. Conversely, SlCDPK2 substituted with the V domain of StCDPK5 localized to the plasma membrane and activated StRBOHB. These results suggest that the V domains confer substrate specificity in vivo by dictating proper subcellular localization of CDPKs.
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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.