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J. Biol. Chem., Vol. 279, Issue 25, 26654-26665, June 18, 2004

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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^*

Volker Henn, Bayram Edemir, Eduard Stefan, Burkhard Wiesner, Dorothea Lorenz, Franziska Theilig, Roland Schmitt, Lutz Vossebein¶, Grazia Tamma||, Michael Beyermann, Eberhard Krause, Friedrich W. Herberg¶, Giovana Valenti||, Sebastian Bachmann, Walter Rosenthal**, and Enno Klussmann**

From the Forschungsinstitut für Molekulare Pharmakologie, Campus Berlin-Buch, Robert-Rössle-Strasse 10, 13125 Berlin, Germany, the Institut für Anatomie, Charité, Universitätsmedizin Berlin, Campus Mitte, Humboldt-Universität zu Berlin, Philippstrasse 12, 10117 Berlin, Germany, the ^¶Abteilung Biochemie, Universität Kassel, Heinrich-Plett-Strasse 40, 34132 Kassel, Germany, the ^||Dipartimento di Fisiologia Generale e Ambientale, Universita de Bari, Via Amendola 165/A, 70126 Bari, Italy, and the ^**Institut für Pharmakologie, Charité, Universitätsmedizin Berlin, Campus Benjamin Franklin, Freie Universität Berlin, Thielallee 67-73, 14195 Berlin, Germany

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, AKAP18, was identified. AKAP18 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, AKAP18 was identified on the same intracellular vesicles as AQP2 and PKA. AVP not only recruited AQP2, but also AKAP18 to the plasma membrane. The elevation of cAMP caused the dissociation of AKAP18 and PKA. The data suggest that AKAP18 is involved in the AQP2 shuttle.

Received for publication, November 24, 2003 , and in revised form, March 11, 2004.

^* This work was supported by Deutsche Forschungsgemeinschaft Grants Ro597/6, Ro597/9, and He1818/3, the Fonds der Chemischen Industrie, and European Union Grants QLK3-CT-2002-02149 and QLRT-2000-00987. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Forschungsinstitut für Molekulare Pharmakologie, Campus Berlin-Buch, Robert-Rössle-Str. 10, D-13125 Berlin, Germany. Tel.: 49-30-94793-260; Fax: 49-30-94793-109; E-mail: klussmann{at}fmp-berlin.de.

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