Targeting of Cyclic AMP Degradation to β2-Adrenergic Receptors by β-Arrestins
SJ Perry, GS Baillie, TA Kohout, I McPhee, MM Magiera… - Science, 2002 - science.org
SJ Perry, GS Baillie, TA Kohout, I McPhee, MM Magiera, KL Ang, WE Miller, AJ McLean…
Science, 2002•science.orgCatecholamines 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 …
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 …
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.
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