ArticleThe Plant cell1998
Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation.
Article in The Plant cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.
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Who cites it
134 citing papers in PubMed, 513 citations in OpenAlex.
- Genome-Wide Analysis of the Aquaporin Gene Family Reveals the Role ofPlants (Basel, Switzerland) · 2026Article
- Post-translational modification acts as a digital like switch influencing AtPIP2;1 water and cation permeability.Scientific reports · 2025Article
- Advances in the Structure, Function, and Regulatory Mechanism of Plant Plasma Membrane Intrinsic Proteins.Genes · 2024Review
- SPIKENET: An Evidence-Based Therapy for Long COVID.Viruses · 2024Review
- Functional regulation of aquaporin dynamics by lipid bilayer composition.Nature communications · 2024Article
- Functional Regulation of Aquaporin Dynamics by Lipid Bilayer Composition.bioRxiv : the preprint server for biology · 2023Article
- Exploring aquaporin functions during changes in leaf water potential.Frontiers in plant science · 2023Review
- Plasma membrane aquaporins of the PIP1 and PIP2 subfamilies facilitate hydrogen peroxide diffusion into plant roots.BMC plant biology · 2022Article
- Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.International journal of molecular sciences · 2022Review
- Is Endophytic Colonization of Host Plants a Method of Alleviating Drought Stress? Conceptualizing the Hidden World of Endophytes.International journal of molecular sciences · 2022Review
- Calcium-dependent protein kinase 16 phosphorylates and activates the aquaporin PIP2;2 to regulate reversible flower opening in Gentiana scabra.The Plant cell · 2022Article
- Masters of flower-bending: Aquaporins regulate flower re-opening.The Plant cell · 2022Article
- Aquaporin OsPIP2;2 links the H2O2 signal and a membrane-anchored transcription factor to promote plant defense.Plant physiology · 2022Article
- Plant Salinity Sensors: Current Understanding and Future Directions.Frontiers in plant science · 2022Review
- Mechanism of Multi-Organ Injury in Experimental COVID-19 and Its Inhibition by a Small Molecule Peptide.Frontiers in pharmacology · 2022Article
- Leaf Intracellular Water Transport Rate Based on Physiological Impedance: A Possible Role of Leaf Internal Retained Water in Photosynthesis and Growth of Tomatoes.Frontiers in plant science · 2022Article
- Investigation of ventriculoperitoneal shunt disconnection for hydrocephalus treatment.Journal of neurosurgery. Pediatrics · 2021Article
- Controversial Regulation of Gene Expression and Protein Transduction of Aquaporins under Drought and Salinity Stress.Plants (Basel, Switzerland) · 2020Review
- Salt Stress Signals on Demand: Cellular Events in the Right Context.International journal of molecular sciences · 2020Review
- Sweet Cherry (International journal of molecular sciences · 2020Article
74 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PM28A is a major intrinsic protein of the spinach leaf plasma membrane and the major phosphoprotein. Phosphorylation of PM28A is dependent in vivo on the apoplastic water potential and in vitro on submicromolar concentrations of Ca2+. Here, we demonstrate that PM28A is an aquaporin and that its water channel activity is regulated by phosphorylation. Wild-type and mutant forms of PM28A, in which putative phosphorylation sites had been knocked out, were expressed in Xenopus oocytes, and the resulting increase in osmotic water permeability was measured in the presence or absence of an inhibitor of protein kinases (K252a) or of an inhibitor of protein phosphatases (okadaic acid). The results indicate that the water channel activity of PM28A is regulated by phosphorylation of two serine residues, Ser-115 in the first cytoplasmic loop and Ser-274 in the C-terminal region. Labeling of spinach leaves with 32P-orthophosphate and subsequent sequencing of PM28A-derived peptides demonstrated that Ser-274 is phosphorylated in vivo, whereas phosphorylation of Ser-115, a residue conserved among all plant plasma membrane aquaporins, could not be demonstrated. This identifies Ser-274 of PM28A as the amino acid residue being phosphorylated in vivo in response to increasing apoplastic water potential and dephosphorylated in response to decreasing water potential. Taken together, our results suggest an active role for PM28A in maintaining cellular water balance.
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