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J. Biol. Chem., Vol. 283, Issue 25, 17561-17567, June 20, 2008

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G-protein-coupled Receptor-mediated Traffic of Na,K-ATPase to the Plasma Membrane Requires the Binding of Adaptor Protein 1 to a Tyr-255-based Sequence in the -Subunit^*

Riad Efendiev¹, Claudia E. Budu, Alejandro M. Bertorello, and Carlos H. Pedemonte

From the College of Pharmacy, University of Houston, Houston, Texas 77204 and Membrane Signaling Networks, Atherosclerosis Research Unit, Department of Medicine, Karolinska Institutet, Karolinska University Hospital-Solna, S-171 76 Stockholm, Sweden

Motion of integral membrane proteins to the plasma membrane in response to G-protein-coupled receptor signals requires selective cargo recognition motifs that bind adaptor protein 1 and clathrin. Angiotensin II, through the activation of AT1 receptors, promotes the recruitment to the plasma membrane of Na,K-ATPase molecules from intracellular compartments. We present evidence to demonstrate that a tyrosine-based sequence (IVVY-255) present within the Na,K-ATPase 1-subunit is involved in the binding of adaptor protein 1. Mutation of Tyr-255 to a phenylalanine residue in the Na,K-ATPase 1-subunit greatly reduces the angiotensin II-dependent activation of Na,K-ATPase, recruitment of Na,K-ATPase molecules to the plasma membrane, and association of adaptor protein 1 with Na,K-ATPase 1-subunit molecules. To determine protein-protein interaction, we used fluorescence resonance energy transfer between fluorophores attached to the Na,K-ATPase 1-subunit and adaptor protein 1. Although angiotensin II activation of AT1 receptors induces a significant increase in the level of fluorescence resonance energy transfer between the two molecules, this effect was blunted in cells expressing the Tyr-255 mutant. Thus, results from different methods and techniques suggest that the Tyr-255-based sequence within the NKA 1-subunit is the site of adaptor protein 1 binding in response to the G-protein-coupled receptor signals produced by angiotensin II binding to AT1 receptors.

Received for publication, November 12, 2007 , and in revised form, April 15, 2008.

^* This work was supported, in whole or in part, by National Institutes of Health Grant DK62195 (to C. H. P.). This work was also supported by American Heart Association, Texas Affiliate, Grant 0455110Y (to C. H. P.) and Grants 32X-10860 and 32P-14879 from the Swedish Research Council and a grant from the Swedish Heart and Lung Foundation and the Swedish Foundation for Kidney Research (to A. M. B.). 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.

¹ To whom correspondence should be addressed: Dept. of Integrative Biology & Pharmacology, University of Texas Health Science Center at Houston, 6431 Fannin, MSB-4.218, Houston, TX 77030. Tel.: 713-500-6854; Fax: 713-500-7444; E-mail: riad.efendi{at}uth.tmc.edu.

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