ArticlePlant physiology1998
Guard cells possess a calcium-dependent protein kinase that phosphorylates the KAT1 potassium channel.
Article in Plant physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
56 citing papers in PubMed, 184 citations in OpenAlex.
- CDPK gene family in Camellia nitidissima: genome-wide identification and expression analysis during petal development and hormone treatments.BMC plant biology · 2026Article
- OnGuard3e: A predictive, ecophysiology-ready tool for gas exchange and photosynthesis research.Plant, cell & environment · 2023Article
- CaInternational journal of molecular sciences · 2021Article
- Predicting the unexpected in stomatal gas exchange: not just an open-and-shut case.Biochemical Society transactions · 2020Review
- Proteins with calmodulin-like domains: structures and functional roles.Cellular and molecular life sciences : CMLS · 2019Review
- The Complex Fine-Tuning of K⁺ Fluxes in Plants in Relation to Osmotic and Ionic Abiotic Stresses.International journal of molecular sciences · 2019Review
- Impaired Function of the Calcium-Dependent Protein Kinase,Frontiers in plant science · 2019Article
- The Calcium-Dependent Protein Kinase CPK33 Mediates Strigolactone-Induced Stomatal Closure inFrontiers in plant science · 2019Article
- TheInternational journal of molecular sciences · 2018Review
- A novel mechanism of "metal gel-shift" by histidine-rich Ni2+-binding Hpn protein from Helicobacter pylori strain SS1.PloS one · 2017Article
- Hydrogen sulfide regulates inward-rectifying K+ channels in conjunction with stomatal closure.Plant physiology · 2015Article
- Arabidopsis CALCIUM-DEPENDENT PROTEIN KINASE8 and CATALASE3 Function in Abscisic Acid-Mediated Signaling and H2O2 Homeostasis in Stomatal Guard Cells under Drought Stress.The Plant cell · 2015Article
- CPK13, a noncanonical Ca2+-dependent protein kinase, specifically inhibits KAT2 and KAT1 shaker K+ channels and reduces stomatal opening.Plant physiology · 2014Article
- Two calcium-dependent protein kinases from Chlamydomonas reinhardtii are transcriptionally regulated by nutrient starvation.Plant signaling & behavior · 2014Article
- Protein phosphorylation in stomatal movement.Plant signaling & behavior · 2014Review
- Calcium: The Missing Link in Auxin Action.Plants (Basel, Switzerland) · 2013Review
- Can prolonged exposure to low VPD disturb the ABA signalling in stomatal guard cells?Journal of experimental botany · 2013Review
- Cross-talk between abscisic acid-dependent and abscisic acid-independent pathways during abiotic stress.Plant cell reports · 2013Review
- The myristoylated amino-terminus of an Arabidopsis calcium-dependent protein kinase mediates plasma membrane localization.Plant molecular biology · 2013Article
- Ca2+-dependent protein kinase11 and 24 modulate the activity of the inward rectifying K+ channels in Arabidopsis pollen tubes.The Plant cell · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Increasing evidence suggests that changes in cytosolic Ca2+ levels and phosphorylation play important roles in the regulation of stomatal aperture and as ion transporters of guard cells. However, protein kinases responsible for Ca2+ signaling in guard cells remain to be identified. Using biochemical approaches, we have identified a Ca(2+)-dependent protein kinase with a calmodulin-like domain (CDPK) in guard cell protoplasts of Vicia faba. Both autophosphorylation and catalytic activity of CDPK are Ca2+ dependent. CDPK exhibits a Ca(2+)-induced electrophoretic mobility shift and its Ca(2+)-dependent catalytic activity can be inhibited by the calmodulin antagonists trifluoperazine and N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide. Antibodies to soybean CDPK alpha cross-react with CDPK. Micromolar Ca2+ concentrations stimulate phosphorylation of several proteins from guard cells; cyclosporin A, a specific inhibitor of the Ca(2+)-dependent protein phosphatase calcineurin enhances the Ca(2+)-dependent phosphorylation of several soluble proteins. CDPK from guard cells phosphorylates the K+ channel KAT1 protein in a Ca(2+)-dependent manner. These results suggest that CDPK may be an important component of Ca2+ signaling in guard cells.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.