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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

Item Type:Article
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
Creators Name:Henn, V. and Edemir, B. and Stefan, E. and Wiesner, B. and Lorenz, D. and Theilig, F. and Schmitt, R. and Vossebein, L. and Tamma, G. and Beyermann, M. and Krause, E. and Herberg, F.W. and Valenti, G. and Bachmann, S. and Rosenthal, W. and Klussmann, E.
Abstract: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 shuttle. During the search for AKAP(s) involved in the shuttle, a new splice variant of AKAP18, AKAP18delta, was identified. AKAP18delta functions as an AKAP in vitro and in vivo. In the kidney, it is mainly expressed in principal cells of the inner medullary collecting duct, closely resembling the distribution of AQP2. It is present in both the soluble and particulate fractions derived from renal inner medullary tissue. Within the particulate fraction, AKAP18delta was identified on the same intracellular vesicles as AQP2 and PKA. AVP not only recruited AQP2, but also AKAP18delta to the plasma membrane. The elevation of cAMP caused the dissociation of AKAP18delta and PKA. The data suggest that AKAP18delta is involved in the AQP2 shuttle.
Keywords:A Kinase Anchor Proteins, Signal Transducing Adaptor Proteins, Aquaporins, Arginine Vasopressin, Northern Blotting, Western Blotting, Carrier Proteins, Cell Line, Cell Membrane, Cultured Cells, Molecular Cloning, Cyclic AMP, Complementary DNA, Enzyme Activation, Fluorescence Resonance Energy Transfer, Gene Library, Glutathione Transferase, Immunohistochemistry, Kidney Medulla, Kinetics, Membrane Proteins, Precipitin Tests, Protein Binding, Protein Conformation, Protein Isoforms, Protein Transport, Messenger RNA, Recombinant Fusion Proteins, Subcellular Fractions, Surface Plasmon Resonance, Time Factors, Vasopressins, Animals, Rats
Source:Journal of Biological Chemistry
ISSN:0021-9258
Publisher:American Society for Biochemistry and Molecular Biology (U.S.A.)
Volume:279
Number:25
Page Range:26654-26665
Date:18 June 2004
Official Publication:https://doi.org/10.1074/jbc.M312835200
PubMed:View item in PubMed

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