ArticleThe Journal of biological chemistry2016
The Arabidopsis AtPP2CA Protein Phosphatase Inhibits the GORK K+ Efflux Channel and Exerts a Dominant Suppressive Effect on Phosphomimetic-activating Mutations.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.
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
17 citing papers in PubMed, 1 synthesis or guideline pooled it, 48 citations in OpenAlex.
- Primary nitrate responses mediated by calcium signalling and diverse protein phosphorylation.Journal of experimental botany · 2020Pooled it
- Structural and mechanistic insights into symmetry conversion in plant GORK K+ channel regulation.Protein & cell · 2025Article
- The multifaceted roles of PP2C phosphatases in plant growth, signaling, and responses to abiotic and biotic stresses.Plant communications · 2025Review
- ALA induces stomatal opening through regulation among PTPA, PP2AC, and SnRK2.6.Frontiers in plant science · 2023Article
- Morphophysiological and transcriptome analysis reveal that reprogramming of metabolism, phytohormones and root development pathways governs the potassium (KFrontiers in plant science · 2022Article
- Structural and Functional Insights into the Role of Guard Cell Ion Channels in Abiotic Stress-Induced Stomatal Closure.Plants (Basel, Switzerland) · 2021Review
- Integrative transcriptomic and metabolomic analysis of D-leaf of seven pineapple varieties differing in N-P-K% contents.BMC plant biology · 2021Article
- Adjustment of KInternational journal of molecular sciences · 2021Review
- Recognition and Activation of the Plant AKT1 Potassium Channel by the Kinase CIPK23.Plant physiology · 2020Article
- Molecular Snapshots of the AKT1-CIPK23 Complex Involved in KPlant physiology · 2020Article
- The Shaker Type Potassium Channel, GORK, Regulates Abscisic Acid Signaling in Arabidopsis.The plant pathology journal · 2019Article
- Review
- The Complex Fine-Tuning of K⁺ Fluxes in Plants in Relation to Osmotic and Ionic Abiotic Stresses.International journal of molecular sciences · 2019Review
- Regulation of KFrontiers in plant science · 2019Review
- Surviving a Dry Future: Abscisic Acid (ABA)-Mediated Plant Mechanisms for Conserving Water under Low Humidity.Plants (Basel, Switzerland) · 2017Review
- The Membrane Transport System of the Guard Cell and Its Integration for Stomatal Dynamics.Plant physiology · 2017Review
- Physiological Responses and Gene Co-Expression Network of Mycorrhizal Roots under KPlant physiology · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The regulation of the GORK (Guard Cell Outward Rectifying) Shaker channel mediating a massive K(+) efflux in Arabidopsis guard cells by the phosphatase AtPP2CA was investigated. Unlike the gork mutant, the atpp2ca mutants displayed a phenotype of reduced transpiration. We found that AtPP2CA interacts physically with GORK and inhibits GORK activity in Xenopus oocytes. Several amino acid substitutions in the AtPP2CA active site, including the dominant interfering G145D mutation, disrupted the GORK-AtPP2CA interaction, meaning that the native conformation of the AtPP2CA active site is required for the GORK-AtPP2CA interaction. Furthermore, two serines in the GORK ankyrin domain that mimic phosphorylation (Ser to Glu) or dephosphorylation (Ser to Ala) were mutated. Mutations mimicking phosphorylation led to a significant increase in GORK activity, whereas mutations mimicking dephosphorylation had no effect on GORK. In Xenopus oocytes, the interaction of AtPP2CA with "phosphorylated" or "dephosphorylated" GORK systematically led to inhibition of the channel to the same baseline level. Single-channel recordings indicated that the GORK S722E mutation increases the open probability of the channel in the absence, but not in the presence, of AtPP2CA. The dephosphorylation-independent inactivation mechanism of GORK by AtPP2CA is discussed in relation with well known conformational changes in animal Shaker-like channels that lead to channel opening and closing. In plants, PP2C activity would control the stomatal aperture by regulating both GORK and SLAC1, the two main channels required for stomatal closure.
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.