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Volume 271, Number 37, Issue of September 13, 1996 pp. 22546-22551
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Expression of Phosducin in a Phosducin-negative Cell Line Reveals Functions of a Gbeta gamma -binding Protein

(Received for publication, February 6, 1996, and in revised form, June 26, 1996)

Karin Schulz , Stefan Danner , Petra Bauer , Stefan Schröder and Martin J. Lohse

From the Institute for Pharmacology, University of Würzburg, Versbacher Strabeta e 9, D-97078 Würzburg, Federal Republic of Germany

Phosducin is a member of the large group of proteins that bind to G-protein beta gamma -subunits (Gbeta gamma ) and whose biological functions are often unknown. Human A431 cells do not contain detectable amounts of phosducin. We generated A431 cells expressing phosducin at a level of approx 1 pmol/mg of cytosolic protein, which is approx 10% of the phosducin level in brain. cAMP accumulation in response to beta 2-adrenergic receptor agonists was enhanced at early times in phosducin-expressing cells, but reached a lower plateau than in control cells. Permeabilization of the cells with digitonin did not change this pattern, but allowed the introduction of specific inhibitors: antibodies to phosducin abolished all differences between the two cell lines. Inhibitors of the beta -adrenergic receptor kinase abolished the differences at early time points. An almost complete loss of beta 2-adrenergic receptor desensitization in the phosducin-expressing cells was also observed when intact cells were desensitized and receptor function was then determined in membrane preparations. Inhibition of protein kinase A accentuated the effects of phosducin, suggesting that also in vivo phosducin is regulated by this kinase. These data indicate that phosducin affects G-protein-mediated signaling in at least two ways: it dampens the overall responsiveness, and it impairs the rapid desensitization mediated by the beta -adrenergic receptor kinase.


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