ArticleKidney international2009
Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells.
Article in Kidney international, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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Who cites it
83 citing papers in PubMed, 131 citations in OpenAlex.
- Transcriptional regulatory factors of the Aqp2 gene.Kidney research and clinical practice · 2026Article
- Molecular mechanism of p-Coumaric acid in the regulation of AQP2 function through the activation of calcium-sensing receptor signaling.Scientific reports · 2026Article
- Focal adhesion kinase inhibition induces membrane accumulation of aquaporin-2 in renal epithelial cells by actin depolymerization and endocytosis inhibition.American journal of physiology. Renal physiology · 2025Article
- Goreisan promotes diuresis by regulating the abundance of aquaporin 2 phosphorylated at serine 269 through calcium-sensing receptor activation.Scientific reports · 2024Article
- Collecting duct water permeability inhibition by EGF is associated with decreased cAMP, PKA activity, and AQP2 phosphorylation at SerAmerican journal of physiology. Renal physiology · 2024Article
- Using CRISPR-Cas9/phosphoproteomics to identify substrates of calcium/calmodulin-dependent kinase 2δ.The Journal of biological chemistry · 2023Article
- Structural and functional analysis of aquaporin-2 mutants involved in nephrogenic diabetes insipidus.Scientific reports · 2023Article
- Phosphatases Decrease Water and Urea Permeability in Rat Inner Medullary Collecting Ducts.International journal of molecular sciences · 2023Article
- Intracellular sites of AQP2 S256 phosphorylation identified using inhibitors of the AQP2 recycling itinerary.American journal of physiology. Renal physiology · 2023Article
- Data resource: vasopressin-regulated protein phosphorylation sites in the collecting duct.American journal of physiology. Renal physiology · 2023Article
- Protein Structure and Modification of Aquaporins.Advances in experimental medicine and biology · 2023Article
- Expression Regulation and Trafficking of Aquaporins.Advances in experimental medicine and biology · 2023Review
- LRBA is essential for urinary concentration and body water homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A multiscale model of the regulation of aquaporin 2 recycling.NPJ systems biology and applications · 2022Article
- Molecular mechanisms governing aquaporin relocalisation.Biochimica et biophysica acta. Biomembranes · 2022Review
- Role of protein phosphatase 2A in kidney disease (Review).Experimental and therapeutic medicine · 2021Review
- Aquaporin 2 regulation: implications for water balance and polycystic kidney diseases.Nature reviews. Nephrology · 2021Review
- A five amino acids deletion in NKCC2 of C57BL/6 mice affects analysis of NKCC2 phosphorylation but does not impact kidney function.Acta physiologica (Oxford, England) · 2021Article
- Rapid development of vasopressin resistance in dietary KAmerican journal of physiology. Renal physiology · 2021Article
- Epigenetic regulation of arginine vasopressin receptor 2 expression by PAX2 and Pax transcription interacting protein.American journal of physiology. Renal physiology · 2021Article
23 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Trafficking of the water channel aquaporin-2 to the apical plasma membrane of the collecting duct is mediated by arginine vasopressin, rendering the cell permeable to water. We recently identified a novel form of aquaporin-2 that is phosphorylated at serine-269 (pS269-AQP2). Using antibodies specific for this form of the water channel, we detected rat and mouse pS269-AQP2 in the connecting tubule and throughout the collecting duct system. Using confocal immunofluorescence microscopy with organelle-specific markers and immunogold electron microscopy, we found that pS269-AQP2 was found only on the apical plasma membrane of principal cells. In vasopressin-deficient Brattleboro rats, pS269-AQP2 was undetectable but dramatically increased in abundance after these rats were treated with [deamino-Cys-1, d-Arg-8]vasopressin (dDAVP). This increase occurred only at the apical plasma membrane, even after long-term dDAVP treatment. Following dDAVP there was a time-dependent redistribution of total aquaporin-2 from predominantly intracellular vesicles to the apical plasma membrane, clathrin-coated vesicles, early endosomal compartments, and lysosomes. However, pS269-AQP2 was found only on the apical plasma membrane at any time. Our results show that S269 phosphorylated aquaporin-2 is exclusively associated with the apical plasma membrane, where it escapes endocytosis to remain at the cell surface.
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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.