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Conceptual Progress for the Improvements in the Selectivity and Efficacy of G Protein-Coupled Receptor Therapeutics: An Overview

  • Received : 2016.11.24
  • Accepted : 2016.12.12
  • Published : 2017.01.01

Abstract

Keywords

References

  1. Agresti, J. J., Antipov, E., Abate, A. R., Ahn, K., Rowat, A. C., Baret, J. C., Marquez, M., Klibanov, A. M., Griffiths, A. D. and Weitz, D. A. (2010) Ultrahigh-throughput screening in drop-based microfluidics for directed evolution. Proc. Natl. Acad. Sci. U.S.A. 107, 4004-4009. https://doi.org/10.1073/pnas.0910781107
  2. Bjarnadottir, T. K., Gloriam, D. E., Hellstrand, S. H., Kristiansson, H., Fredriksson, R. and Schioth, H. B. (2006) Comprehensive repertoire and phylogenetic analysis of the G protein-coupled receptors in human and mouse. Genomics 88, 263-273. https://doi.org/10.1016/j.ygeno.2006.04.001
  3. Bologna, Z., Teoh, J., Bayoumi, A. S., Tang, Y. and Kim, I. M. (2017) Biased G protein-coupled receptor signaling: new player in modulating physiology and pathology. Biomol. Ther. (Seoul) 25, 12-25. https://doi.org/10.4062/biomolther.2016.165
  4. Cassel, D. and Selinger, Z. (1976) Catecholamine-stimulated GTPase activity in turkey erythrocyte membranes. Biochim. Biophys. Acta 452, 538-551. https://doi.org/10.1016/0005-2744(76)90206-0
  5. Chen, Y., Long, H., Wu, Z., Jiang, X. and Ma, L. (2008) EGF transregulates opioid receptors through EGFR-mediated GRK2 phosphorylation and activation. Mol. Biol. Cell 19, 2973-2983. https://doi.org/10.1091/mbc.E07-10-1058
  6. Cherezov, V., Rosenbaum, D. M., Hanson, M. A., Rasmussen, S. G., Thian, F. S., Kobilka, T. S., Choi, H. J., Kuhn, P., Weis, W. I., Kobilka, B. K. and Stevens, R. C. (2007) High-resolution crystal structure of an engineered human ${\beta}2$-adrenergic G-protein-coupled receptor. Science 318, 1258-1265. https://doi.org/10.1126/science.1150577
  7. Chou, M. M., Hou, W., Johnson, J., Graham, L. K., Lee, M. H., Chen, C. S., Newton, A. C., Schaffhausen, B. S. and Toker, A. (1998) Regulation of protein kinase C zeta by PI 3-kinase and PDK-1. Curr. Biol. 8, 1069-1077. https://doi.org/10.1016/S0960-9822(98)70444-0
  8. Daub, H., Weiss, F. .U, Wallasch, C. and Ullrich, A. (1996) Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors. Nature 379, 557-560. https://doi.org/10.1038/379557a0
  9. Dixon, R. A., Kobilka, B. K., Strader, D. J., Benovic, J. L., Dohlman, H. G., Frielle, T., Bolanowski, M. A., Bennett, C. D., Rands, E., Diehl, R. E., Mumford, R. A., Slater, E. E., Sigal, I. S., Caron, M. G., Lefkowitz, R. J. and Strader, C. D. (1986) Cloning of the gene and cDNA for mammalian ${\beta}$-adrenergic receptor and homology with rhodopsin. Nature 321, 75-79. https://doi.org/10.1038/321075a0
  10. Duc, N. M., Kim, H. R. and K. Y. Chung (2017) Recent progress in understanding the conformational mechanism of heterotrimeric G protein activation. Biomol. Ther. (Seoul) 25, 4-11. https://doi.org/10.4062/biomolther.2016.169
  11. Furlong, M. and Seong, J. Y. (2017) Evolutionary and comparative genomics to drive rational drug design, with particular focus on neuropeptide seven-transmembrane receptors. Biomol. Ther. (Seoul) 25, 57-68. https://doi.org/10.4062/biomolther.2016.199
  12. Gilman, A. G. (1987) G proteins: transducers of receptor-generated signals. Annu. Rev. Biochem. 56, 615-649. https://doi.org/10.1146/annurev.bi.56.070187.003151
  13. Lee, S., Chung, Y. H. and Lee, C. (2017) US28, a virally-encoded GPCR as an antiviral target for human cytomegalovirus infection. Biomol. Ther. (Seoul) 25, 69-79. https://doi.org/10.4062/biomolther.2016.208
  14. Lefkowitz, R. J. (2000) The superfamily of heptahelical receptors. Nat. Cell Biol. 2, E133-E136. https://doi.org/10.1038/35017152
  15. Lefkowitz, R. J. and Haber, E. (1971) A fraction of the ventricular myocardium that has the specificity of the cardiac ${\beta}$-adrenergic receptor. Proc. Natl. Acad. Sci. U.S.A. 68, 1773-1777. https://doi.org/10.1073/pnas.68.8.1773
  16. Mangmool, S., Denkaew, T., Parichatikanond, W. and Kurose, H. (2017) ${\beta}$-adrenergic receptor and insulin resistance in the heart. Biomol. Ther. (Seoul) 25, 44-56. https://doi.org/10.4062/biomolther.2016.128
  17. Nathans, J. and Hogness, D. S. (1983) Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin. Cell 34, 807-814. https://doi.org/10.1016/0092-8674(83)90537-8
  18. O'Hara, D. S. and Lefkowitz, R. J. (1974) Affinity chromatography of adrenergic receptors and binding proteins. Meth. Enzymol. 34, 695-700.
  19. Park, S. J. and Im, D. S. (2017) Sphingosine 1-phosphate receptor modulators and drug discovery. Biomol. Ther. (Seoul) 25, 80-90. https://doi.org/10.4062/biomolther.2016.160
  20. Reiter, E., Ahn, S., Shukla, A. K. and Lefkowitz, R. J. (2012) Molecular mechanism of ${\beta}$-arrestin-biased agonism at seven-transmembrane receptors. Annu. Rev. Pharmacol. Toxicol. 52, 179-197. https://doi.org/10.1146/annurev.pharmtox.010909.105800
  21. Robison, G. A., Butcher, R. W. and Sutherland, E. W. (1967) Adenyl cyclase as an adrenergic receptor. Ann. N. Y. Acad. Sci. 139, 703-723. https://doi.org/10.1111/j.1749-6632.1967.tb41239.x
  22. Rodbell, M., Birnbaumer, L., Pohl, S. L. and Krans, H. M. (1971) 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.
  23. Rosenbaum, D. M., Cherezov, V., Hanson, M. A., Rasmussen, S. G., Thian, F. S., Kobilka, T. S., Choi, H. J., Yao, X. J., Weis, W. I., Stevens, R. C. and Kobilka, B. K. (2007) GPCR engineering yields high-resolution structural insights into ${\beta}$2-adrenergic receptor function. Science 318, 1266-1273. https://doi.org/10.1126/science.1150609
  24. Sodhi, A., Montaner, S. and Gutkind, J. S. (2004) Viral hijacking of Gprotein-coupled-receptor signalling networks. Nat. Rev. Mol. Cell Biol. 5, 998-1012. https://doi.org/10.1038/nrm1529
  25. Stryer, L. (1986) Cyclic GMP cascade of vision. Annu. Rev. Neurosci. 9, 87-119. https://doi.org/10.1146/annurev.ne.09.030186.000511
  26. van Biesen, T., Hawes, B. E., Luttrell, D. K., Krueger, K. M., Touhara, K., Porfiri, E., Sakaue, M., Luttrell, L. M. and Lefkowitz, R. J. (1995) Receptor-tyrosine-kinase- and $G{\beta}{\gamma}$-mediated MAP kinase activation by a common signalling pathway. Nature 376, 781-784. https://doi.org/10.1038/376781a0
  27. Violin, J. D. and Lefkowitz, R. J. (2007) ${\beta}$-arrestin-biased ligands at seven-transmembrane receptors. Trends Pharmacol. Sci. 28, 416-422. https://doi.org/10.1016/j.tips.2007.06.006
  28. Wei, H., Ahn, S., Shenoy, S. K., Karnik, S. S., Hunyady, L., Luttrell, L. M. and Lefkowitz, R. J. (2003) Independent ${\beta}$-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2. Proc. Natl. Acad. Sci. U.S.A. 100, 10782-10787. https://doi.org/10.1073/pnas.1834556100
  29. Weichert, D., Banerjee, A., Hiller, C., Kling, R. C., Hubner, H. and Gmeiner, P. (2015) Molecular determinants of biased agonism at the dopamine $D_2$ receptor. J. Med. Chem. 58, 2703-2717. https://doi.org/10.1021/jm501889t
  30. Whalen, E. J., Rajagopal, S. and Lefkowitz, R. J. (2011) Therapeutic potential of ${\beta}$-arrestin- and G protein-biased agonists. Trends Mol. Med. 17, 126-139. https://doi.org/10.1016/j.molmed.2010.11.004
  31. Zhang, X. and Kim, K. M. (2017) Multifactorial regulation of G proteincoupled receptor endocytosis. Biomol. Ther. (Seoul) 25, 26-43. https://doi.org/10.4062/biomolther.2016.186
  32. Zheng, M., Zhang, X., Guo, S., Zhang, X., Min, C., Cheon, S. H., Oak, M. H., Kim, Y. R. and Kim, K. M. (2016) Agonist-induced changes in RalA activities allows the prediction of the endocytosis of G proteincoupled receptors. Biochim. Biophys. Acta 1863, 77-90. https://doi.org/10.1016/j.bbamcr.2015.10.007

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