Editors' ChoiceSignal Compartmentalization

β-Arrestin Regulation of Cyclic AMP Signaling

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Science's STKE  29 Oct 2002:
Vol. 2002, Issue 156, pp. tw399-TW399
DOI: 10.1126/stke.2002.156.tw399

A molecular understanding of the spatiotemporal regulation of various intracellular signals has revealed how tightly controlled this process can be. For example, the intracellular second messenger adenosine 3′,5′-monophosphate (cAMP) is generated in response to the activation of some G protein-coupled receptors, and cAMP microdomains are thought to be generated by the rate and location of cAMP degradation by phosphodiesterases (PDEs). The cAMP signals generated by activated β2-adrenergic receptors are quenched when the cytosolic molecule β-arrestin associates with and desensitizes the receptors from further agonist stimulation. Perry et al. now report that β-arrestins not only blunt the rate of cAMP generation but also promote cAMP degradation by recruiting PDEs to activated receptors at the plasma membrane. This coordinated activity may allow β-arrestins to restrict the extent of cAMP-dependent activities at the cell surface.

S. J. Perry, G. S. Baillie, T. A. Kohout, I. McPhee, M. M. Magiera, K. L. Ang, W. E. Miller, A. J. McLean, M. Conti, M. D. Houslay, R. J. Lefkowitz, Targeting of cyclic AMP degradation to β2-adrenergic receptors by β-arrestins. Science 298, 834-836 (2002). [Abstract] [Full Text]

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