ArticleThe Journal of biological chemistry2012
Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by their CBL-interacting protein kinases (CIPKs) is required for full activity of CBL-CIPK complexes toward their target proteins.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 191 citations in OpenAlex.
- Calcium-ROS-NO signalling integration in plant immunity: mechanistic interactions and feedback regulation.Planta · 2026Review
- Article
- Genome-Wide Analysis of theInternational journal of molecular sciences · 2026Article
- PuCBL9-PuCIPK11 Modulates Stomatal Microfilament Reorganisation in a Phosphorylation-Dependent Manner to Enhance Drought Tolerance in Poplar.Plant, cell & environment · 2026Article
- Article
- OsCML17 a pollen-expressed calmodulin-like protein regulates pollen germination and tube growth in rice (Oryza sativa).Plant cell reports · 2026Article
- Genome-wide characterization of theFrontiers in plant science · 2026Article
- CBL1/CIPK23 phosphorylates tonoplast sugar transporter TST2 to enhance sugar accumulation in sweet orange (Citrus sinensis).Journal of integrative plant biology · 2025Article
- Structural and molecular dynamics simulation studies of CBL-interacting protein kinase CIPK and its complexes related to plant salinity stress.Journal of molecular modeling · 2024Article
- Integrative gene duplication and genome-wide analysis as an approach to facilitate wheat reverse genetics: An example in the TaCIPK family.Journal of advanced research · 2024Article
- High-throughput diagnostic markers for foliar fungal disease resistance and high oleic acid content in groundnut.BMC plant biology · 2024Article
- Overexpression and knockdown of cottoniScience · 2024Article
- Potato calcium sensor modules StCBL3-StCIPK7 and StCBL3-StCIPK24 negatively regulate plant immunity.BMC plant biology · 2024Article
- CIPK-B is essential for salt stress signalling in Marchantia polymorpha.The New phytologist · 2023Article
- Potassium nutrient status drives posttranslational regulation of a low-K response network in Arabidopsis.Nature communications · 2023Article
- Does Potassium (KInternational journal of molecular sciences · 2022Review
- Combined transcriptome and metabolome analysis revealed pathways involved in improved salt tolerance of Gossypium hirsutum L. seedlings in response to exogenous melatonin application.BMC plant biology · 2022Article
- Evolution of the CBL and CIPK gene families in Medicago: genome-wide characterization, pervasive duplication, and expression pattern under salt and drought stress.BMC plant biology · 2022Article
- Evolution of Volatile Aroma Compounds and Amino Acids in Cabernet Gernischt Grape Berries (Foods (Basel, Switzerland) · 2022Article
- Genome-Wide Identification, Characterization and Expression Analysis of theInternational journal of molecular sciences · 2021Article
8 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calcineurin B-like proteins (CBLs) represent a family of calcium sensor proteins that interact with a group of serine/threonine kinases designated as CBL-interacting protein kinases (CIPKs). CBL-CIPK complexes are crucially involved in relaying plant responses to many environmental signals and in regulating ion fluxes. However, the biochemical characterization of CBL-CIPK complexes has so far been hampered by low activities of recombinant CIPKs. Here, we report on an efficient wheat germ extract-based in vitro transcription/translation protocol that yields active full-length wild-type CIPK proteins. We identified a conserved serine residue within the C terminus of CBLs as being phosphorylated by their interacting CIPKs. Remarkably, our studies revealed that CIPK-dependent CBL phosphorylation is strictly dependent on CBL-CIPK interaction via the CIPK NAF domain. The phosphorylation status of CBLs does not appear to influence the stability, localization, or CIPK interaction of these calcium sensor proteins in general. However, proper phosphorylation of CBL1 is absolutely required for the in vivo activation of the AKT1 K(+) channel by CBL1-CIPK23 and CBL9-CIPK23 complexes in oocytes. Moreover, we show that by combining CBL1, CIPK23, and AKT1, we can faithfully reconstitute CBL-dependent enhancement of phosphorylation of target proteins by CIPKs in vitro. In addition, we report that phosphorylation of CBL1 by CIPK23 is also required for the CBL1-dependent enhancement of CIPK23 activity toward its substrate. Together, these data identify a novel general regulatory mechanism of CBL-CIPK complexes in that CBL phosphorylation at their flexible C terminus likely provokes conformational changes that enhance specificity and activity of CBL-CIPK complexes toward their target proteins.
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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.