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Science 308 (5721): 512-517

Copyright © 2005 by the American Association for the Advancement of Science

Transduction of Receptor Signals by ß-Arrestins

Robert J. Lefkowitz1,2*, and Sudha K. Shenoy2

Abstract: The transmission of extracellular signals to the interior of the cell is a function of plasma membrane receptors, of which the seven transmembrane receptor family is by far the largest and most versatile. Classically, these receptors stimulate heterotrimeric G proteins, which control rates of generation of diffusible second messengers and entry of ions at the plasma membrane. Recent evidence, however, indicates another previously unappreciated strategy used by the receptors to regulate intracellular signaling pathways. They direct the recruitment, activation, and scaffolding of cytoplasmic signaling complexes via two multifunctional adaptor and transducer molecules, ß-arrestins 1 and 2. This mechanism regulates aspects of cell motility, chemotaxis, apoptosis, and likely other cellular functions through a rapidly expanding list of signaling pathways.

1 Howard Hughes Medical Institute, Durham, NC 27710, USA.
2 Duke University Medical Center, Durham, NC 27710, USA.

* To whom correspondence should be addressed. E-mail: lefko001{at}

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{beta}-Arrestin-dependent activation of Ca2+/calmodulin kinase II after {beta}1-adrenergic receptor stimulation.
S. Mangmool, A. K. Shukla, and H. A. Rockman (2010)
J. Cell Biol. 189, 573-587
   Abstract »    Full Text »    PDF »
Antidepressants Increase {beta}-Arrestin2 Ubiquitinylation and Degradation by the Proteasomal Pathway in C6 Rat Glioma Cells.
M. Golan, G. Schreiber, and S. Avissar (2010)
J. Pharmacol. Exp. Ther. 332, 970-976
   Abstract »    Full Text »    PDF »
Genetic Deletion of p90 Ribosomal S6 Kinase 2 Alters Patterns of 5-Hydroxytryptamine2A Serotonin Receptor Functional Selectivity.
R. T. Strachan, N. Sciaky, M. R. Cronan, W. K. Kroeze, and B. L. Roth (2010)
Mol. Pharmacol. 77, 327-338
   Abstract »    Full Text »    PDF »
Recruitment of the ESCRT Machinery to a Putative Seven-Transmembrane-Domain Receptor Is Mediated by an Arrestin-Related Protein.
A. Herrador, S. Herranz, D. Lara, and O. Vincent (2010)
Mol. Cell. Biol. 30, 897-907
   Abstract »    Full Text »    PDF »
Ligand Detection in the Allosteric World.
T. P. Kenakin (2010)
J Biomol Screen 15, 119-130
   Abstract »    Full Text »    PDF »
GLP-1 Mediates Antiapoptotic Effect by Phosphorylating Bad through a {beta}-Arrestin 1-mediated ERK1/2 Activation in Pancreatic {beta}-Cells.
J. Quoyer, C. Longuet, C. Broca, N. Linck, S. Costes, E. Varin, J. Bockaert, G. Bertrand, and S. Dalle (2010)
J. Biol. Chem. 285, 1989-2002
   Abstract »    Full Text »    PDF »
{beta}-arrestin- but not G protein-mediated signaling by the "decoy" receptor CXCR7.
S. Rajagopal, J. Kim, S. Ahn, S. Craig, C. M. Lam, N. P. Gerard, C. Gerard, and R. J. Lefkowitz (2010)
PNAS 107, 628-632
   Abstract »    Full Text »    PDF »
Arrestin Orchestrates Crosstalk Between G Protein-Coupled Receptors to Modulate the Spatiotemporal Activation of ERK MAPK.
D. Cervantes, C. Crosby, and Y. Xiang (2010)
Circ. Res. 106, 79-88
   Abstract »    Full Text »    PDF »
Wnt5a regulates distinct signalling pathways by binding to Frizzled2.
A. Sato, H. Yamamoto, H. Sakane, H. Koyama, and A. Kikuchi (2010)
EMBO J. 29, 41-54
   Abstract »    Full Text »    PDF »
Requirements for Recruitment of a G Protein-coupled Receptor to Clathrin-coated Pits in Budding Yeast.
J. Y. Toshima, J.-i. Nakanishi, K. Mizuno, J. Toshima, and D. G. Drubin (2009)
Mol. Biol. Cell 20, 5039-5050
   Abstract »    Full Text »    PDF »
{beta}-Arrestin-2 Interaction and Internalization of the Human P2Y1 Receptor Are Dependent on C-Terminal Phosphorylation Sites.
S. Reiner, N. Ziegler, C. Leon, K. Lorenz, K. von Hayn, C. Gachet, M. J. Lohse, and C. Hoffmann (2009)
Mol. Pharmacol. 76, 1162-1171
   Abstract »    Full Text »    PDF »
Participation of Tom1L1 in EGF-stimulated endocytosis of EGF receptor.
N. S. Liu, L. S. Loo, E. Loh, L.-F. Seet, and W. Hong (2009)
EMBO J. 28, 3485-3499
   Abstract »    Full Text »    PDF »
Tyrosine Phosphorylation of Kir3 following {kappa}-Opioid Receptor Activation of p38 MAPK Causes Heterologous Desensitization.
C. C. Clayton, M. Xu, and C. Chavkin (2009)
J. Biol. Chem. 284, 31872-31881
   Abstract »    Full Text »    PDF »
Evolution of vertebrate rod and cone phototransduction genes.
D. Larhammar, K. Nordstrom, and T. A. Larsson (2009)
Phil Trans R Soc B 364, 2867-2880
   Abstract »    Full Text »    PDF »

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