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J Biol Chem, Vol. 273, Issue 35, 22627-22634, August 28, 1998

A Heterotrimeric G Protein of the G_i Family Is Required for cAMP-triggered Trafficking of Aquaporin 2 in Kidney Epithelial Cells

Giovanna Valenti, Giuseppe Procino, Ursula Liebenhoff^§, Antonio Frigeri, Pio Alberto Benedetti^¶, Gudrun Ahnert-Hilger, Bernd Nürnberg^**, Maria Svelto, and Walter Rosenthal

From the  Dipartimento di Fisiologia Generale e Ambientale, Universitá degli Studi, 70126 Bari, Italy, ^§ Rudolf-Buchheim-Institut für Pharmakologie, Justus-Liebig-Universität Gießen, 35392 Gießen, Germany,  Forschungsinstitut für Molekulare Pharmakologie, 10315 Berlin, Germany, ^¶ Istituto di Biofisica-CNR, 56127 Pisa, Italy,  Institut for Anatomie, Humboldt-Universität zu Berlin, 10115 Berlin, Germany, and ^** Institut für Pharmakologie, Freie Universität Berlin, 14195 Berlin, Germany

Vasopressin is the key regulator of water homeostasis in vertebrates. Central to its antidiuretic action in mammals is the redistribution of the water channel aquaporin 2 (AQP2) from intracellular vesicles to the apical membrane of kidney epithelial cells, an event initiated by an increase in cAMP and activation of protein kinase A. The subsequent steps of the signaling cascade are not known. To identify proteins involved in the AQP2 shuttle we exploited a recently developed cell line (CD8) derived from the rabbit cortical collecting duct and stably transfected with rat AQP2 cDNA. Treatment of CD8 cells with pertussis toxin (PTX) inhibited both the vasopressin-induced increase in water permeability and the redistribution of AQP2 from an intracellular compartment to the apical membrane. ADP-ribosylation studies revealed the presence of at least two major PTX substrates. Correspondingly, two  subunits of PTX-sensitive G proteins, G_i2 and G_i3, were identified by Western blotting. Introduction of a synthetic peptide corresponding to the C terminus of the G_i3  subunit into permeabilized CD8 cells efficiently inhibited the cAMP-induced AQP2 translocation; a peptide corresponding to the  subunits of G_i1/2 was much less potent. Thus a member of the G_i family, most likely G_i3, is involved in the cAMP-triggered targeting of AQP2-bearing vesicles to the apical membrane of kidney epithelial cells.

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