ArticleThe Plant cell1997
The 14-3-3 protein interacts directly with the C-terminal region of the plant plasma membrane H(+)-ATPase.
Article in The Plant cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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Who cites it
80 citing papers in PubMed.
- Recent advances in understanding the regulatory mechanisms of P4-ATPase lipid flippases.Biochemical Society transactions · 2026Review
- Functional 14-3-3 Proteins: Master Regulators in Plant Responses to Salt Stress.Plants (Basel, Switzerland) · 2025Review
- Genetic Dissection of Rice Plant-Specific Non-ε Group 14-3-3 Proteins in Response to Phosphate Starvation.Rice (New York, N.Y.) · 2025Article
- Identification of a novel stomatal opening chemical, PP242, that inhibits early abscisic acid signal transduction in guard cells.Plant & cell physiology · 2025Article
- Poltergeist-Like 2 (PLL2)-dependent activation of herbivore defence distinguishes systemin from other immune signalling pathways.Nature plants · 2025Article
- Molecular tipping points in plant cell surface HQuantitative plant biology · 2025Review
- The 14-3-3 protein nt GF14e interacts with CIPK2 and increases low potassium stress in tobacco.Plant signaling & behavior · 2024Article
- Fungal Plasma Membrane HJournal of fungi (Basel, Switzerland) · 2024Review
- Phosphoregulation of the yeast Pma1 H+-ATPase autoinhibitory domain involves the Ptk1/2 kinases and the Glc7 PP1 phosphatase and is under TORC1 control.PLoS genetics · 2024Article
- 14-3-3 Proteins and the Plasma Membrane HPlants (Basel, Switzerland) · 2023Article
- Stomatal properties of Arabidopsis cauline and rice flag leaves and their contributions to seed production and grain yield.Journal of experimental botany · 2023Article
- Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps.International journal of molecular sciences · 2023Review
- The apple 14-3-3 geneFrontiers in plant science · 2023Article
- From sequence to function through structure: Deep learning for protein design.Computational and structural biotechnology journal · 2023Review
- The plasma membrane HMolecular plant pathology · 2022Article
- The role of 14-3-3 proteins in plant growth and response to abiotic stress.Plant cell reports · 2022Review
- Coat proteins of necroviruses target 14-3-3a to subvert MAPKKKα-mediated antiviral immunity in plants.Nature communications · 2022Article
- Proton and calcium pumping P-type ATPases and their regulation of plant responses to the environment.Plant physiology · 2021Review
- Article
- The Surprising Story of Fusicoccin: A Wilt-Inducing Phytotoxin, a Tool in Plant Physiology and a 14-3-3-Targeted Drug.Biomolecules · 2021Review
20 more citing papers are in PubMed but not listed here.
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Accumulating evidence suggests that 14-3-3 proteins are involved in the regulation of plant plasma membrane H(+)-ATPase activity. However, it is not known whether the 14-3-3 protein interacts directly or indirectly with the H(+)-ATPase. In this study, detergent-solubilized plasma membrane H(+)-ATPase isolated from fusicoccin-treated maize shoots was copurified with the 14-3-3 protein (as determined by protein gel blotting), and the H(+)-ATPase was recovered in an activated state. In the absence of fusicoccin treatment, H(+)-ATPase and the 14-3-3 protein were well separated, and the H(+)-ATPase was recovered in a nonactivated form. Trypsin treatment removed the 10-kD C-terminal region from the H(+)-ATPase as well as the 14-3-3 protein. Using the yeast two-hybrid system, we could show a direct interaction between Arabidopsis 14-3-3 GF14-phi and the last 98 C-terminal amino acids of the Arabidopsis AHA2 plasma membrane H(+)-ATPase. We propose that the 14-3-3 protein is a natural ligand of the plasma membrane H(+)-ATPase, regulating proton pumping by displacing the C-terminal autoinhibitory domain of the H(+)-ATPase.
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