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Originally published In Press as doi:10.1074/jbc.M011338200 on April 27, 2001

J. Biol. Chem., Vol. 276, Issue 29, 26906-26915, July 20, 2001
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Dopamine Acutely Stimulates Na+/H+ Exchanger (NHE3) Endocytosis via Clathrin-coated Vesicles
DEPENDENCE ON PROTEIN KINASE A-MEDIATED NHE3 PHOSPHORYLATION*

Ming Chang HuDagger , Lingzhi FanDagger , Ladonna A. CrowderDagger , Zoubida Karim-Jimenez§, Heini Murer§, and Orson W. MoeDagger ||

From the  Medical Service, Department of Veterans Affairs Medical Center, Dallas, Texas 75216, the Dagger  Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, Texas 75390-8856, and the § Institute of Physiology, University of Zürich, Zürich 8057, Switzerland

Dopamine (DA) is a key hormone in mammalian sodium homeostasis. DA induces natriuresis via acute inhibition of the renal proximal tubule apical membrane Na+/H+ exchanger NHE3. We examined the mechanism by which DA inhibits NHE3 in a renal cell line. DA acutely decreases surface NHE3 antigen in dose- and time-dependent fashion without altering total cellular NHE3. Although DA1 receptor agonist alone decreases surface NHE3, simultaneous DA2 agonist synergistically enhances the effect of DA1. Decreased surface NHE3 antigen, caused by stimulation of NHE3 endocytosis, is dependent on intact functioning of the GTPase dynamin and involves increased binding of NHE3 to the adaptor protein AP2. DA-stimulated NHE3 endocytosis can be blocked by pharmacologic or genetic protein kinase A inhibition or by mutation of two protein kinase A target serines (Ser-560 and Ser-613) on NHE3. We conclude that one mechanism by which DA induces natriuresis is via protein kinase A-mediated phosphorylation of proximal tubule NHE3 leading to endocytosis of NHE3 via clathrin-coated vesicles.

* This work was supported by National Institutes of Health Grants DK-48482 and DK-54396 (to O. W. M.), by the Department of Veterans Affairs Research Service (to O. W. M.), American Heart Association Texas Affiliate Grant 98G-052 (to O. W. M.), and Swiss National Science Foundation Grant 3100-46523.96 (to H. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The 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: Dept. of Internal Medicine, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-8856. Tel.: 214-648-3152; Fax: 214-648-2071; E-mail: orson.moe@utsouthwestern.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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