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Targeting of Cyclic AMP Degradation to β2-Adrenergic Receptors by β-Arrestins

Science  25 Oct 2002:
Vol. 298, Issue 5594, pp. 834-836
DOI: 10.1126/science.1074683

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Abstract

Catecholamines signal through the β2-adrenergic receptor by promoting production of the second messenger adenosine 3′,5′-monophosphate (cAMP). The magnitude of this signal is restricted by desensitization of the receptors through their binding to β-arrestins and by cAMP degradation by phosphodiesterase (PDE) enzymes. We show that β-arrestins coordinate both processes by recruiting PDEs to activated β2-adrenergic receptors in the plasma membrane of mammalian cells. In doing so, the β-arrestins limit activation of membrane-associated cAMP-activated protein kinase by simultaneously slowing the rate of cAMP production through receptor desensitization and increasing the rate of its degradation at the membrane.

  • * These authors contributed equally to this work.

  • Present address: Scottish Biomedical, Todd Campus West of Scotland Science Park, Glasgow, Scotland, UK.

  • To whom correspondence should be addressed. E-mail: lefko001{at}receptor-biol.duke.edu.

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