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

Autor: Volker Henn, Friedrich W. Herberg, Michael Beyermann, Eduard Stefan, Walter Rosenthal, Burkhard Wiesner, Giovana Valenti, Sebastian Bachmann, Roland Schmitt, Dorothea Lorenz, Enno Klussmann, Eberhard Krause, Grazia Tamma, Franziska Theilig, Bayram Edemir, Lutz Vossebein
Rok vydání: 2004
Předmět:
A-kinase-anchoring protein
Vasopressin
Time Factors
Arginine
Protein Conformation
A Kinase Anchor Proteins
Kidney
urologic and male genital diseases
Biochemistry
Cyclic AMP
Fluorescence Resonance Energy Transfer
Protein Isoforms
Cloning
Molecular
Receptor
Cells
Cultured
Glutathione Transferase
Kidney Medulla
Immunohistochemistry
Cell biology
Protein Transport
medicine.anatomical_structure
Aquaporin 2
Intracellular
Protein Binding
Subcellular Fractions
DNA
Complementary
Vasopressins
Recombinant Fusion Proteins
Blotting
Western
Biology
Aquaporins
Cell Line
medicine
Animals
Humans
RNA
Messenger
Protein kinase A
Molecular Biology
Adaptor Proteins
Signal Transducing
Gene Library
urogenital system
Cell Membrane
Membrane Proteins
Cell Biology
Surface Plasmon Resonance
Blotting
Northern
Precipitin Tests
Rats
Arginine Vasopressin
Enzyme Activation
Kinetics
RNA
Carrier Proteins
Zdroj: Journal of Biological Chemistry. 279:26654-26665
ISSN: 0021-9258
Popis: 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.
Databáze: OpenAIRE
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