Seven-transmembrane receptors

Lefkowitz, R. J. The superfamily of heptahelical receptors. Nature Cell Biol. 2, E133–E136 (2000).A historical perspective describing the origins of the field of 7TM receptor signalling in the 1970s and 1980s.

Dixon, R. A. et al. Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin. Nature 321, 75–79 (1986).This paper reports the cloning of the β2-adrenergic receptor, its analogy and 7TM homology with rhodopsin, and speculates on the existence of a large family of such receptors.

Dohlman, H. G., Thorner, J., Caron, M. G. & Lefkowitz, R. J. Model systems for the study of seven-transmembrane-segment receptors. Annu. Rev. Biochem. 60, 653–688 (1991).

Lee, D. K., George, S. R. & O'Dowd, B. F. Novel G-protein-coupled receptor genes expressed in the brain: continued discovery of important therapeutic targets. Expert Opin. Ther. Targets 6, 1–18 (2002).

Palczewski, K. et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289, 739–745 (2000).Describes the crystal structure of the only 7TM receptor so far solved.

Rodbell, M., Birnbaumer, L., Pohl, S. L. & Krans, H. M. The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. V. An obligatory role of guanylnucleotides in glucagon action. J. Biol. Chem. 246, 1877–1882 (1971).

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Ballesteros, J. A. et al. Activation of the β2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6. J. Biol. Chem. 276, 29171–29177 (2001).

Farahbakhsh, Z. T., Ridge, K. D., Khorana, H. G. & Hubbell, W. L. Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: a site-directed spin labeling study. Biochemistry 34, 8812–8819 (1995).

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Ross, E. M. & Wilkie, T. M. GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins. Annu. Rev. Biochem. 69, 795–827 (2000).

Klein, S., Reuveni, H. & Levitzki, A. Signal transduction by a nondissociable heterotrimeric yeast G protein. Proc. Natl Acad. Sci. USA 97, 3219–3123 (2000).

Ferguson, S. S. Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling. Pharmacol. Rev. 53, 1–24 (2001).

Pitcher, J. A., Freedman, N. J. & Lefkowitz, R. J. G protein-coupled receptor kinases. Annu. Rev. Biochem. 67, 653–692 (1998).An extensive review of the biochemistry and regulation of the G-protein-coupled-receptor kinases.

Daaka, Y., Luttrell, L. M. & Lefkowitz, R. J. Switching of the coupling of the β2-adrenergic receptor to different G proteins by protein kinase A. Nature 390, 88–91 (1997).Describes a novel mechanism by which the G-protein coupling specificity of 7TM receptors might be regulated by protein-kinase-A-mediated receptor phosphorylation.

Zamah, A. M., Delahunty, M., Luttrell, L. M. & Lefkowitz, R. J. PKA-mediated phosphorylation of the β2-adrenergic receptor regulates its coupling to Gs and Gi: Demonstration in a reconstituted system. J. Biol. Chem. (in the press).

Lawler, O. A., Miggin, S. M. & Kinsella, B. T. Protein kinase A-mediated phosphorylation of serine 357 of the mouse prostacyclin receptor regulates its coupling to Gs-, to Gi-, and to Gq-coupled effector signaling. J. Biol. Chem. 276, 33596–33607 (2001).

Krupnick, J. G. & Benovic, J. L. The role of receptor kinases and arrestins in G protein-coupled receptor regulation. Annu. Rev. Pharmacol. Toxicol. 38, 289–319 (1998).An extensive review of this universal receptor regulatory system.

Zhang, J. et al. Molecular mechanisms of G protein-coupled receptor signaling: role of G protein-coupled receptor kinases and arrestins in receptor desensitization and resensitization. Receptors Channels 5, 193–199 (1997).

Winstel, R. et al. Protein kinase cross-talk: membrane targeting of the β-adrenergic receptor kinase by protein kinase C. Proc. Natl Acad. Sci. USA 93, 2105–2109 (1996).

Cong, M. et al. Regulation of membrane targeting of the G protein-coupled receptor kinase 2 by protein kinase A and its anchoring protein AKAP79. J. Biol. Chem. 276, 15192–15199 (2001).

Krueger, K. M., Daaka, Y., Pitcher, J. A. & Lefkowitz, R. J. The role of sequestration in G protein-coupled receptor resensitization. Regulation of β2-adrenergic receptor dephosphorylation by vesicular acidification. J. Biol. Chem. 272, 5–8 (1997).

Pitcher, J. A. et al. The G-protein-coupled receptor phosphatase: a protein phosphatase type 2A with a distinct subcellular distribution and substrate specificity. Proc. Natl Acad. Sci. USA 92, 8343–8347 (1995).

Tsao, P. & von Zastrow, M. Downregulation of G protein-coupled receptors. Curr. Opin. Neurobiol. 10, 365–369 (2000).

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Howard, A. D. et al. Orphan G-protein-coupled receptors and natural ligand discovery. Trends Pharmacol. Sci. 22, 132–140 (2001).

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Daaka, Y. et al. Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase. J. Biol. Chem. 273, 685–688 (1998).

Claing, A., Laporte, S. A., Caron, M. G. & Lefkowitz, R. J. Endocytosis of G protein-coupled receptors: roles of G protein-coupled receptor kinases and β-arrestin proteins. Prog. Neurobiol. 66, 61–79 (2002).Reviews the complex mechanisms involved in 7TM-receptor endocytosis.

Claing, A. et al. Multiple endocytic pathways of G protein-coupled receptors delineated by GIT1 sensitivity. Proc. Natl Acad. Sci. USA 97, 1119–1124 (2000).

Smart, E. J. et al. Caveolins, liquid-ordered domains, and signal transduction. Mol. Cell. Biol. 19, 7289–7304 (1999).

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Goodman, O. B., Jr et al. β-Arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptor. Nature 383, 447–450 (1996).

Laporte, S. A. et al. The β-adrenergic receptor/β-arrestin complex recruits the clathrin adaptor AP-2 during endocytosis. Proc. Natl Acad. Sci. USA 96, 3712–3717 (1999).

Gaidarov, I. et al. Arrestin function in G protein-coupled receptor endocytosis requires phosphoinositide binding. EMBO J. 18, 871–881 (1999).

Scott, M. G., Benmerah, A., Muntaner, O. & Marullo, S. Recruitment of activated G protein-coupled receptors to pre-existing clathrin-coated pits in living cells. J. Biol. Chem. 277, 3552–3559 (2002).

Santini, F., Gaidarov, I. & Keen, J. H. G protein-coupled receptor/arrestin3 modulation of the endocytic machinery. J. Cell Biol. 156, 665–676 (2002).

Oakley, R. H. et al. Differential affinities of visual arrestin, β-arrestin1, and β-arrestin2 for GPCRs delineate two major classes of receptors. J. Biol. Chem. 275, 17201–17210 (2000).

Luttrell, L. M. et al. β-Arrestin-dependent formation of β2 adrenergic receptor–Src protein kinase complexes. Science 283, 655–661 (1999).

Ahn, S. et al. Src-mediated tyrosine phosphorylation of dynamin is required for β2-adrenergic receptor internalization and mitogen-activated protein kinase signaling. J. Biol. Chem. 274, 1185–1188 (1999).

Ahn, S. et al. c-Src dependent tyrosine phosphorylation regulates dynamin self-assembly and receptor-mediated endocytosis. J. Biol. Chem. 277, 26642–26651 (2002).

Shenoy, S. K., McDonald, P. H., Kohout, T. A. & Lefkowitz, R. J. Regulation of receptor fate by ubiquitination of activated β2-adrenergic receptor and β-arrestin. Science 294, 1307–1313 (2001).

Pickart, C. M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503–533 (2001).

McDonald, P. H. et al. Identification of NSF as a β-arrestin1-binding protein. Implications for β2-adrenergic receptor regulation. J. Biol. Chem. 274, 10677–10680 (1999).

Claing, A. et al. β-Arrestin-mediated ADP-ribosylation factor 6 activation and β2-adrenergic receptor endocytosis. J. Biol. Chem. 276, 42509–42513 (2001).

Premont, R. T. et al. β2-Adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein. Proc. Natl Acad. Sci. USA 95, 14082–14087 (1998).

Cong, M. et al. Binding of the β2 adrenergic receptor to N-ethylmaleimide-sensitive factor regulates receptor recycling. J. Biol. Chem. 276, 45145–45152 (2001).

Seachrist, J. L. et al. Rab5 association with the angiotensin II type 1A receptor promotes Rab5 GTP binding and vesicular fusion. J. Biol. Chem. 277, 679–685 (2002).

Kohout, T. A. et al. β-Arrestin 1 and 2 differentially regulate heptahelical receptor signaling and trafficking. Proc. Natl Acad. Sci. USA 98, 1601–1606 (2001).

Marchese, A. & Benovic, J. L. Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting. J. Biol. Chem. 276, 45509–45512 (2001).

Dodge, K. & Scott, J. D. AKAP79 and the evolution of the AKAP model. FEBS Lett. 476, 58–61 (2000).

Fraser, I. D. et al. Assembly of an A kinase-anchoring protein–β(2)-adrenergic receptor complex facilitates receptor phosphorylation and signaling. Curr. Biol. 10, 409–412 (2000).

Shih, M. et al. Dynamic complexes of β-adrenergic receptors with protein kinases and phosphatases and the role of gravin. J. Biol. Chem. 274, 1588–1595 (1999).

Diviani, D., Soderling, J. & Scott, J. D. AKAP-Lbc anchors protein kinase A and nucleates Gα12-selective Rho-mediated stress fiber formation. J. Biol. Chem. 276, 44247–44257 (2001).

Tsunoda, S. et al. A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade. Nature 388, 243–249 (1997).

Brakeman, P. R. et al. Homer: a protein that selectively binds metabotropic glutamate receptors. Nature 386, 284–288 (1997).

Cao, W. et al. Direct binding of activated c-Src to the β3-adrenergic receptor is required for MAP kinase activation. J. Biol. Chem. 275, 38131–38134 (2000).

Marrero, M. B. et al. Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor. Nature 375, 247–250 (1995).

Hall, R. et al. The β2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange. Nature 392, 626–630 (1998).

Hall, R. A. et al. A C-terminal motif found in the β2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins. Proc. Natl Acad. Sci. USA 95, 8496–8501 (1998).

Hu, L. A. et al. β1-adrenergic receptor association with PSD-95. Inhibition of receptor internalization and facilitation of β1-adrenergic receptor interaction with N-methyl-d-aspartate receptors. J. Biol. Chem. 275, 38659–38666 (2000).

Sheng, M. & Sala, C. PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24, 1–29 (2001).An authoritative review of a mechanism of protein–protein interactions that regulates several GPCR interactions.

Luttrell, L. M. et al. β-Arrestin-dependent formation of β2 adrenergic receptor Src protein kinase complexes. Science 283, 655–661 (1999).

Imamura, T. et al. β-Arrestin-mediated recruitment of the Src family kinase Yes mediates endothelin-1-stimulated glucose transport. J. Biol. Chem. 276, 43663–43667 (2001).

Barlic, J. et al. Regulation of tyrosine kinase activation and granule release through β-arrestin by CXCR1. Nature Immunol. 1, 227–233 (2000).

DeFea, K. A. et al. β-Arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2. J. Cell Biol. 148, 1267–1281 (2000).Describes a role for β-arrestin in mediating ERK activation by 7TM receptors.

Luttrell, L. M. et al. Activation and targeting of extracellular signal-regulated kinases by β-arrestin scaffolds. Proc. Natl Acad. Sci. USA 98, 2449–2454 (2001).

McDonald, P. H. et al. β-Arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3. Science 290, 1574–1577 (2000).

Tohgo, A. et al. β-Arrestin scaffolding of the ERK cascade enhances cytosolic ERK activity but inhibits ERK-mediated transcription following angiotensin AT1a receptor stimulation. J. Biol. Chem. 277, 9429–9436 (2002).

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Cerione, R. A. et al. The mammalian β2-adrenergic receptor: reconstitution of functional interactions between pure receptor and pure stimulatory nucleotide binding protein of the adenylate cyclase system. Biochemistry 23, 4519–4525 (1984).

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Jordan, B. A. & Devi, L. A. G-protein-coupled receptor heterodimerization modulates receptor function. Nature 399, 697–700 (1999).

Devi, L. A. Heterodimerization of G-protein-coupled receptors: pharmacology, signaling and trafficking. Trends Pharmacol. Sci. 22, 532–537 (2001).

Salahpour, A., Angers, S. & Bouvier, M. Functional significance of oligomerization of G-protein-coupled receptors. Trends Endocrinol. Metab. 11, 163–168 (2000).

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Hilairet, S. et al. Agonist-promoted internalization of a ternary complex between calcitonin receptor-like receptor, receptor activity-modifying protein 1 (RAMP1), and β-arrestin. J. Biol. Chem. 276, 42182–42190 (2001).

Dean, M. K. et al. Dimerization of G-protein-coupled receptors. J. Med. Chem. 44, 4595–4614 (2001).

Gilman, A. Please check EGO at door. Mol. Interventions 1, 14–21 (2001).

Brzostowski, J. A. & Kimmel, A. R. Signaling at zero G: G-protein-independent functions for 7-TM receptors. Trends Biochem. Sci. 26, 291–297 (2001).Reviews G-protein-independent signalling by 7TM receptors.

Zheng, B. et al. RGS-PX1, a GAP for GαS and sorting nexin in vesicular trafficking. Science 294, 1939–1942 (2001).

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