ArticleJournal of the American Society of Nephrology : JASN2010
Phosphoproteomic profiling reveals vasopressin-regulated phosphorylation sites in collecting duct.
Article in Journal of the American Society of Nephrology : JASN, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 69 citations in OpenAlex.
- The Physiological Roles and Pathological Implications of Urea Transporters in the Cardiovascular System.Biomedicines · 2025Review
- Utilizing Omic Data to Understand Integrative Physiology.Physiology (Bethesda, Md.) · 2025Review
- Critical factors for flow cytometry analysis of the brain.The FEBS journal · 2025Article
- Multifaceted roles of Epac signaling in renal functions.The Biochemical journal · 2025Review
- Protein Structures of Urea Transporters.Sub-cellular biochemistry · 2025Review
- Tissue Distribution, Expression and Regulation of Urea Transporters.Sub-cellular biochemistry · 2025Review
- Phosphoproteomic response to epidermal growth factor in native rat inner medullary collecting duct.American journal of physiology. Renal physiology · 2025Article
- Bayesian mapping of protein kinases to vasopressin-regulated phosphorylation sites in renal collecting duct.American journal of physiology. Renal physiology · 2024Article
- Vasopressin V2 receptor, tolvaptan, and ERK1/2 phosphorylation in the renal collecting duct.American journal of physiology. Renal physiology · 2024Article
- Poly(ADP-ribose) polymerase-1 affects vasopressin-mediated AQP2 expression in collecting duct cells of the kidney.American journal of physiology. Renal physiology · 2024Article
- Data resource: vasopressin-regulated protein phosphorylation sites in the collecting duct.American journal of physiology. Renal physiology · 2023Article
- Bayesian analysis of dynamic phosphoproteomic data identifies protein kinases mediating GPCR responses.Cell communication and signaling : CCS · 2022Article
- Phosphoproteomic Identification of Vasopressin/cAMP/Protein Kinase A-Dependent Signaling in Kidney.Molecular pharmacology · 2021Review
- Phosphoproteomic identification of vasopressin-regulated protein kinases in collecting duct cells.British journal of pharmacology · 2021Article
- Phosphoproteomic identification of vasopressin V2 receptor-dependent signaling in the renal collecting duct.American journal of physiology. Renal physiology · 2019Article
- New insights into the transcriptional regulation of aquaporin-2 and the treatment of X-linked hereditary nephrogenic diabetes insipidus.Kidney research and clinical practice · 2019Article
- From Molecules to Mechanisms: Functional Proteomics and Its Application to Renal Tubule Physiology.Physiological reviews · 2018Review
- Proteomic determination of the lysine acetylome and phosphoproteome in the rat native inner medullary collecting duct.Physiological genomics · 2018Article
- Sequence-based searching of custom proteome and transcriptome databases.Physiological reports · 2018Article
- Intracellular cAMP Sensor EPAC: Physiology, Pathophysiology, and Therapeutics Development.Physiological reviews · 2018Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein phosphorylation is an important component of vasopressin signaling in the renal collecting duct, but the database of known phosphoproteins is incomplete. We used tandem mass spectrometry to identify vasopressin-regulated phosphorylation events in isolated rat inner medullary collecting duct (IMCD) suspensions. Using multiple search algorithms to identify the phosphopeptides from spectral data, we expanded the size of the existing collecting duct phosphoproteome database from 367 to 1187 entries. Label-free quantification in vasopressin- and vehicle-treated samples detected a significant change in the phosphorylation of 29 of 530 quantified phosphopeptides. The targets include important structural, regulatory, and transporter proteins. The vasopressin-regulated sites included two known sites (Ser-486 and Ser-499) present in the urea channel UT-A1 and one previously unknown site (Ser-84) on vasopressin-sensitive urea channels UT-A1 and UT-A3. In vitro assays using synthetic peptides showed that purified protein kinase A (PKA) could phosphorylate all three sites, and immunoblotting confirmed the PKA dependence of Ser-84 and Ser-486 phosphorylation. These results expand the known list of collecting duct phosphoproteins and highlight the utility of targeted phosphoproteomic approaches.
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Registered trials
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