Associated Papers
Focal adhesion kinase inhibition induces membrane accumulation of aquaporin-2 in renal epithelial cells by actin depolymerization and endocytosis inhibition.
Tchakal-Mesbahi A et al.
American Journal of Physiology. Renal Physiology, 2025
Ribosomal s6 kinase is a mediator of aquaporin-2 S256 phosphorylation and membrane accumulation after EGFR inhibition with erlotinib.
Babicz RSE et al.
American Journal of Physiology. Renal Physiology, 2025
Focal Adhesion Kinase (FAK) inhibition induces membrane accumulation of aquaporin2 (AQP2) through endocytosis inhibition and actin depolymerization in renal epithelial cells.
Tchakal-Mesbahi A et al.
Biorxiv : the Preprint Server for Biology, 2024
Novel signalling pathways in nephrogenic syndrome of inappropriate antidiuresis: functional implication of site-specific AQP2 phosphorylation.
Venneri M et al.
The Journal of Physiology, 2024
Many kinases for controlling the water channel aquaporin-2.
Kharin A et al.
The Journal of Physiology, 2024
Intracellular sites of AQP2 S256 phosphorylation identified using inhibitors of the AQP2 recycling itinerary.
Cheung PW et al.
American Journal of Physiology. Renal Physiology, 2023
AQP2 trafficking in health and diseases: an updated overview.
Centrone M et al.
The International Journal of Biochemistry & Cell Biology, 2022
Acute pyelonephritis: Increased plasma membrane targeting of renal aquaporin-2.
Ernstsen CV et al.
Acta Physiologica (oxford, England), 2022
Updates and Perspectives on Aquaporin-2 and Water Balance Disorders.
Noda Y et al.
International Journal of Molecular Sciences, 2021
Activation of AQP2 water channels by protein kinase A: therapeutic strategies for congenital nephrogenic diabetes insipidus.
Ando F
Clinical and Experimental Nephrology, 2021
AQP2: Mutations Associated with Congenital Nephrogenic Diabetes Insipidus and Regulation by Post-Translational Modifications and Protein-Protein Interactions.
Gao C et al.
Cells, 2020
Direct effect of protein kinase A on four putative phosphorylation sites of aquaporin 2 in vitro.
Chen Z et al.
Biochemical and Biophysical Research Communications, 2020
Involvement of PDZ-SAP97 interactions in regulating AQP2 translocation in response to vasopressin in LLC-PK1 cells.
Nooh MM et al.
American Journal of Physiology. Renal Physiology, 2019
A versatile aquaporin-2 cell system for quantitative temporal expression and live cell imaging.
Holst MR et al.
American Journal of Physiology. Renal Physiology, 2019
Inhibition of non-receptor tyrosine kinase Src induces phosphoserine 256-independent aquaporin-2 membrane accumulation.
Cheung PW et al.
The Journal of Physiology, 2019
Vasopressin-Independent Regulation of Aquaporin-2 by Tamoxifen in Kidney Collecting Ducts.
Tingskov SJ et al.
Frontiers in Physiology, 2019
The vertebrate Aqp14 water channel is a neuropeptide-regulated polytransporter.
Chauvigné F et al.
Communications Biology, 2019
Structural Basis for Mutations of Human Aquaporins Associated to Genetic Diseases.
Calvanese L et al.
International Journal of Molecular Sciences, 2018
Protein phosphatase 2C is responsible for VP-induced dephosphorylation of AQP2 serine 261.
Cheung PW et al.
American Journal of Physiology. Renal Physiology, 2017
Aquaporin-2 Ser-261 phosphorylation is regulated in combination with Ser-256 and Ser-269 phosphorylation.
Yui N et al.
Biochemical and Biophysical Research Communications, 2017
Molecular mechanisms regulating aquaporin-2 in kidney collecting duct.
Jung HJ et al.
American Journal of Physiology. Renal Physiology, 2016
AQP2 Plasma Membrane Diffusion Is Altered by the Degree of AQP2-S256 Phosphorylation.
Arnspang EC et al.
International Journal of Molecular Sciences, 2016
Regulation of the Water Channel Aquaporin-2 via 14-3-3θ and -ζ.
Moeller HB et al.
The Journal of Biological Chemistry, 2016
The Trafficking of the Water Channel Aquaporin-2 in Renal Principal Cells-a Potential Target for Pharmacological Intervention in Cardiovascular Diseases.
Vukićević T et al.
Frontiers in Pharmacology, 2016
Partial nephrogenic diabetes insipidus caused by a novel AQP2 variation impairing trafficking of the aquaporin-2 water channel.
Dollerup P et al.
Bmc Nephrology, 2015
Characterization of the putative phosphorylation sites of the AQP2 C terminus and their role in AQP2 trafficking in LLC-PK1 cells.
Arthur J et al.
American Journal of Physiology. Renal Physiology, 2015
Expression of a dominant negative PKA mutation in the kidney elicits a diabetes insipidus phenotype.
Gilbert ML et al.
American Journal of Physiology. Renal Physiology, 2015
Phosphorylation and ubiquitylation are opposing processes that regulate endocytosis of the water channel aquaporin-2.
Moeller HB et al.
Journal of Cell Science, 2014
Cell biology of vasopressin-regulated aquaporin-2 trafficking.
Moeller HB et al.
Pflugers Archiv : European Journal of Physiology, 2012
Differential, phosphorylation dependent trafficking of AQP2 in LLC-PK1 cells.
Rice WL et al.
Plos One, 2012
Bilateral ureteral obstruction induces early downregulation and redistribution of AQP2 and phosphorylated AQP2.
Stødkilde L et al.
American Journal of Physiology. Renal Physiology, 2011
Regulation of the water channel aquaporin-2 by posttranslational modification.
Moeller HB et al.
American Journal of Physiology. Renal Physiology, 2011
Regulation of AQP2 localization by S256 and S261 phosphorylation and ubiquitination.
Tamma G et al.
American Journal of Physiology. Cell Physiology, 2011
Calcitonin has a vasopressin-like effect on aquaporin-2 trafficking and urinary concentration.
Bouley R et al.
Journal of the American Society of Nephrology : Jasn, 2011
Phosphorylation of aquaporin-2 regulates its water permeability.
Eto K et al.
The Journal of Biological Chemistry, 2010
Aquaporins in kidney pathophysiology.
Noda Y et al.
Nature Reviews. Nephrology, 2010
Aquaporin-2 regulates cell volume recovery via tropomyosin.
Li YH et al.
The International Journal of Biochemistry & Cell Biology, 2009
p.R254Q mutation in the aquaporin-2 water channel causing dominant nephrogenic diabetes insipidus is due to a lack of arginine vasopressin-induced phosphorylation.
Savelkoul PJ et al.
Human Mutation, 2009
Repulsion between Lys258 and upstream arginines explains the missorting of the AQP2 mutant p.Glu258Lys in nephrogenic diabetes insipidus.
Kamsteeg EJ et al.
Human Mutation, 2009
Syntaxin specificity of aquaporins in the inner medullary collecting duct.
Mistry AC et al.
American Journal of Physiology. Renal Physiology, 2009
LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation.
van Balkom BW et al.
Journal of the American Society of Nephrology : Jasn, 2009
Role of multiple phosphorylation sites in the COOH-terminal tail of aquaporin-2 for water transport: evidence against channel gating.
Moeller HB et al.
American Journal of Physiology. Renal Physiology, 2009
Sensing, signaling and sorting events in kidney epithelial cell physiology.
Brown D et al.
Traffic (copenhagen, Denmark), 2009
Identification of phosphorylation-dependent binding partners of aquaporin-2 using protein mass spectrometry.
Zwang NA et al.
Journal of Proteome Research, 2009
Regulation of aquaporin-2 trafficking.
Nedvetsky PI et al.
Handbook of Experimental Pharmacology, 2009
A fluorimetry-based ssYFP secretion assay to monitor vasopressin-induced exocytosis in LLC-PK1 cells expressing aquaporin-2.
Nunes P et al.
American Journal of Physiology. Cell Physiology, 2008
AKAP220 colocalizes with AQP2 in the inner medullary collecting ducts.
Okutsu R et al.
Kidney International, 2008
Vasopressin-stimulated increase in phosphorylation at Ser269 potentiates plasma membrane retention of aquaporin-2.
Hoffert JD et al.
The Journal of Biological Chemistry, 2008
Phosphorylation events and the modulation of aquaporin 2 cell surface expression.
Brown D et al.
Current Opinion in Nephrology and Hypertension, 2008