Phosphorylation of Serine 256 Is Required for cAMP-dependent Regulatory Exocytosis of the Aquaporin-2 Water Channel

• Published in: The Journal of biological chemistry Vol. 272; no. 23; pp. 14800 - 14804
• Main Authors: Fushimi, K, Sasaki, S, Marumo, F
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 06.06.1997
• Subjects: Alanine; Animals; Aquaporin 2; Aquaporin 6; Aquaporins; Cell Line; Cyclic AMP - analogs & derivatives; Cyclic AMP - metabolism; Cyclic AMP - pharmacology; Exocytosis; Ion Channels - biosynthesis; Ion Channels - metabolism; Light; Mutagenesis, Site-Directed; Phosphorylation; Point Mutation; Rats; Recombinant Proteins - biosynthesis; Recombinant Proteins - metabolism; Scattering, Radiation; Serine; Thionucleotides - pharmacology; Transfection

The aquaporin-2 (AQP2) vasopressin water channel is translocated to the apical membrane upon vasopressin stimulation. Phosphorylation of serine 256 of AQP2 by cAMP-dependent protein kinase has been shown, but its relation to vasopressin-regulated translocation has not been elucidated. To address thi...