Identification of a novel A-kinase anchoring protein 18 isoform and evidence for its role in the vasopressin-induced aquaporin-2 shuttle in renal principal cells.

@article{Henn2004IdentificationOA,
  title={Identification of a novel A-kinase anchoring protein 18 isoform and evidence for its role in the vasopressin-induced aquaporin-2 shuttle in renal principal cells.},
  author={Volker Henn and Bayram Edemir and Eduard Stefan and Burkhard Wiesner and Dorothea Lorenz and Franziska Theilig and Roland Schmitt and Lutz Vossebein and Grazia Tamma and Michael Beyermann and Eberhard Krause and Friedrich W Herberg and Giovana Valenti and Sebastian Bachmann and Walter Rosenthal and Enno Klussmann},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 25},
  pages={26654-65}
}
Arginine vasopressin (AVP) increases the water permeability of renal collecting duct principal cells by inducing the fusion of vesicles containing the water channel aquaporin-2 (AQP2) with the plasma membrane (AQP2 shuttle). This event is initiated by activation of vasopressin V2 receptors, followed by an elevation of cAMP and the activation of protein kinase A (PKA). The tethering of PKA to subcellular compartments by protein kinase A anchoring proteins (AKAPs) is a prerequisite for the AQP2… CONTINUE READING

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