| http://purl.uniprot.org/citations/9227644 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9227644 | http://www.w3.org/2000/01/rdf-schema#comment | "Vasopressin-dependent translocation of aquaporin-2 (AQP2) between intracellular vesicles and the plasma membrane has been demonstrated in vivo and in vitro. Furthermore, the vasopressin-induced increase in apical membrane water permeability of renal principal cells is dependent on a rise in intracellular adenosine 3',5'-cyclic monophosphate and activation of protein kinase A (PKA). To determine whether trafficking of AQP2 is dependent on PKA phosphorylation, we first examined the effect of the PKA-inhibitor N-(2[[3-(4-bromophenyl)-2-propenyl]-amino]-ethyl)-5-isoquinolinesulfonam ide (H-89) on AQP2 translocation in transfected LLC-PK1 cells. Vasopressin-induced membrane insertion of AQP2 was completely inhibited by pretreatment of the cells for 60 min with H-89. This reagent also caused a dense accumulation of AQP2 in the Golgi region. Next, LLC-PK1 cells were stably transfected with AQP2 cDNA in which the PKA phosphorylation site, Ser256, was replaced with alanine (S256A). S256A-AQP2 was not phosphorylated in vitro by PKA, and S256A-AQP2 was mainly localized to intracellular vesicles in the basal condition, similar to wild-type AQP2. However, after stimulation with vasopressin or forskolin, the cellular distribution of S256A-AQP2 remained unchanged. In addition, the usual vasopressin-induced increase in endocytosis seen in AQP2-transfected cells was not observed in S256A-AQP2-transfected cells. These results demonstrate that the Ser256 PKA phosphorylation site is possibly involved in the vasopressin-induced trafficking of AQP2 from intracellular vesicles to the plasma membrane and in the subsequent stimulation of endocytosis."xsd:string |
| http://purl.uniprot.org/citations/9227644 | http://purl.uniprot.org/core/author | "Brown D."xsd:string |
| http://purl.uniprot.org/citations/9227644 | http://purl.uniprot.org/core/author | "Katsura T."xsd:string |
| http://purl.uniprot.org/citations/9227644 | http://purl.uniprot.org/core/author | "Gustafson C.E."xsd:string |
| http://purl.uniprot.org/citations/9227644 | http://purl.uniprot.org/core/author | "Ausiello D.A."xsd:string |
| http://purl.uniprot.org/citations/9227644 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9227644 | http://purl.uniprot.org/core/name | "Am J Physiol"xsd:string |
| http://purl.uniprot.org/citations/9227644 | http://purl.uniprot.org/core/pages | "F817-22"xsd:string |
| http://purl.uniprot.org/citations/9227644 | http://purl.uniprot.org/core/title | "Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells."xsd:string |
| http://purl.uniprot.org/citations/9227644 | http://purl.uniprot.org/core/volume | "272"xsd:string |
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