The β2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange

Randy A. Hall, Richard T. Premont, Chung-Wai Chow, Jeremy T. Blitzer, Julie A. Pitcher, Audrey Claing, Robert H. Stoffel, Larry S. Barak, Shirish Shenolikar, Edward J. Weinman, Sergio Grinstein and Robert J. Lefkowitz ()
Additional contact information
Randy A. Hall: Howard Hughes Medical Institute, Biochemistry and Cell Biology, Duke University Medical Center
Richard T. Premont: Howard Hughes Medical Institute, Biochemistry and Cell Biology, Duke University Medical Center
Chung-Wai Chow: Research Institute, Hospital for Sick Children
Jeremy T. Blitzer: Howard Hughes Medical Institute, Biochemistry and Cell Biology, Duke University Medical Center
Julie A. Pitcher: Howard Hughes Medical Institute, Biochemistry and Cell Biology, Duke University Medical Center
Audrey Claing: Howard Hughes Medical Institute, Biochemistry and Cell Biology, Duke University Medical Center
Robert H. Stoffel: Howard Hughes Medical Institute, Biochemistry and Cell Biology, Duke University Medical Center
Larry S. Barak: Howard Hughes Medical Institute, Biochemistry and Cell Biology, Duke University Medical Center
Shirish Shenolikar: Duke University
Edward J. Weinman: Robert C. Byrd Health Science Center, West Virginia University
Sergio Grinstein: Research Institute, Hospital for Sick Children
Robert J. Lefkowitz: Howard Hughes Medical Institute, Biochemistry and Cell Biology, Duke University Medical Center

Nature, 1998, vol. 392, issue 6676, 626-630

Abstract: Abstract Stimulation of β2-adrenergic receptors on the cell surface by adrenaline or noradrenaline leads to alterations in the metabolism, excitability, differentiation and growth of many cell types. These effects have traditionally been thought to be mediated exclusively by receptor activation of intracellular G proteins1. However, certain physiological effects of β2-adrenergic receptor stimulation, notably the regulation of cellular pH by modulation of Na+/H+ exchanger (NHE) function, do not seem to be entirely dependent on G-protein activation2,3,4,5,6,7. We report here a direct agonist-promoted association of the β2-adrenergic receptor with the Na+/H+ exchanger regulatory factor (NHERF), a protein that regulates the activity of the Na+/H+ exchanger type 3 (NHE3)8. NHERF binds to the β2-adrenergic receptor by means of a PDZ-domain-mediated interaction with the last few residues of the carboxy-terminal cytoplasmic domain of the receptor. Mutation ofthe final residue of the β2-adrenergic receptor from leucine toalanine abolishes the receptor's interaction with NHERF andalso markedly alters β2-adrenergic receptor regulation of NHE3 in cells without altering receptor-mediated activation of adenylyl cyclase. Our findings indicate that agonist-dependent β2-adrenergic receptor binding of NHERF plays a role in β2-adrenergic receptor-mediated regulation of Na+/H+ exchange.

Date: 1998
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DOI: 10.1038/33458

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