Modulating receptor function through RAMPs: can they represent drug targets in themselves?

Drug Discovery Today

Volumn 14, Issue 7-8, 2009, Pages 413-419

  Sexton, Patrick M ^a   Poyner, David R ^b   Simms, John ^a   Christopoulos, Arthur ^a   Hay, Debbie L ^c  

^a MONASH UNIVERSITY   (Australia)

^b ASTON UNIVERSITY   (United Kingdom)

^c UNIVERSITY OF AUCKLAND   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; RECEPTOR ACTIVITY MODIFYING PROTEIN;

CELL SURFACE; DRUG TARGETING; INTERNALIZATION; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; BINDING SITES; DRUG DELIVERY SYSTEMS; DRUG DESIGN; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MEMBRANE PROTEINS; MOLECULAR STRUCTURE; PROTEIN BINDING; PROTEIN TRANSPORT; RECEPTORS, G-PROTEIN-COUPLED; SIGNAL TRANSDUCTION;

EID: 62849124664     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.drudis.2008.12.009     Document Type: Review

References (59)

1. Ellis C. The state of GPCR research in 2004. Nat. Rev. Drug Discov. 3 (2004) 577-626
2. McLatchie L.M., et al. RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor. Nature 393 (1998) 333-339
3. Christopoulos A., et al. Novel receptor partners and function of receptor activity-modifying proteins. J. Biol. Chem. 278 (2003) 3293-3297
4. Fraser N.J., et al. The amino terminus of receptor activity modifying proteins is a critical determinant of glycosylation state and ligand binding of calcitonin receptor-like receptor. Mol. Pharmacol. 55 (1999) 1054-1059
5. Hay D.L., et al. CL/RAMP2 and CL/RAMP3 produce pharmacologically distinct adrenomedullin receptors: a comparison of effects of adrenomedullin22-52, CGRP8-37 and BIBN4096BS. Br. J. Pharmacol. 140 (2003) 477-486
6. Hay D.L., et al. GPCR modulation by RAMPs. Pharmacol. Ther. 109 (2006) 173-197
7. Poyner D.R., et al. International Union of Pharmacology. XXXII. The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors. Pharmacol. Rev. 54 (2002) 233-246
8. Christopoulos G., et al. Multiple amylin receptors arise from receptor-activity-modifying-proteins interaction with the calcitonin receptor gene product. In Mol. Pharmacol. 56 (1999) 235-242
9. Muff R., et al. An amylin receptor is revealed following co-transfection of a calcitonin receptor with receptor activity modifying proteins-1 or -3. Endocrinology 140 (1999) 2924-2927
10. Bouschet T., et al. Receptor-activity-modifying proteins are required for forward trafficking of the calcium-sensing receptor to the plasma membrane. J. Cell Sci. 118 (2005) 4709-4720
11. Udawela M., et al. The receptor activity modifying protein family of G protein coupled receptor accessory proteins. Semin. Cell Dev. Biol. 15 (2004) 299-308
12. Sexton P.M., et al. Receptor activity modifying proteins. Cell. Signal. 13 (2001) 73-83
13. Takei Y., et al. Identification of novel adrenomedullin in mammals: a potent cardiovascular and renal regulator. FEBS Lett. 556 (2004) 53-58
14. Roh J., et al. Intermedin is a calcitonin/calcitonin gene-related peptide family peptide acting through the calcitonin receptor-like receptor/receptor activity-modifying protein receptor complexes. J. Biol. Chem. 279 (2004) 7264-7274
15. Hay D.L., et al. Pharmacological discrimination of calcitonin receptor: receptor activity-modifying protein complexes. Mol. Pharmacol. 67 (2005) 1655-1665
16. Sexton P.M., et al. Procalcitonin has bioactivity at calcitonin receptor family complexes: potential mediator implications in sepsis. Crit. Care Med. 36 (2008) 1637-1640
17. Hay D.L., et al. Determinants of 1-piperidinecarboxamide, N-[2-[[5-amino-l-[[4-(4-pyridinyl)-l-piperazinyl]carbonyl]pentyl]amino]-1-[(3,5-dibromo-4-hydroxyphenyl)methyl]-2-oxoethyl]-4-(1,4-dihydro-2-oxo-3(2H)-quinazolinyl) (BIBN4096BS) affinity for calcitonin gene-related peptide and amylin receptors-the role of receptor activity modifying protein 1. Mol. Pharmacol. 70 (2006) 1984-1991
18. Zumpe E.T., et al. Multiple RAMP domains are required for generation of amylin receptor phenotype from the calcitonin receptor gene product. Biochem. Biophys. Res. Commun. 267 (2000) 368-372
19. Fitzsimmons T.J., et al. The extracellular domain of receptor activity-modifying protein 1 is sufficient for calcitonin receptor-like receptor function. J. Biol. Chem. 278 (2003) 14313-14320
20. Udawela M., et al. Distinct receptor activity-modifying protein domains differentially modulate interaction with calcitonin receptors. Mol. Pharmacol. 69 (2006) 1984-1989
21. Steiner S., et al. The transmembrane domain of receptor-activity-modifying protein 1 is essential for the functional expression of a calcitonin gene-related peptide receptor. Biochemistry 41 (2002) 11398-11404
22. Qi T., et al. Identification of N-terminal receptor activity-modifying protein residues important for CGRP, adrenomedullin and amylin receptor function. Mol. Pharmacol. 74 (2008) 1059-1071
23. Tilakaratne N., et al. Amylin receptor phenotypes derived from human calcitonin receptor/RAMP coexpression exhibit pharmacological differences dependent on receptor isoform and host cell environment. J. Pharmacol. Exp. Ther. 294 (2000) 61-72
24. Moore E.E., et al. Functionally different isoforms of the human calcitonin receptor result from alternative splicing of the gene transcript. Mol. Endocrinol. 9 (1995) 959-968
25. Udawela M., et al. A critical role for the short intracellular C terminus in receptor activity-modifying protein function. Mol. Pharmacol. 70 (2006) 1750-1760
26. Morfis M., et al. Receptor activity modifying proteins differentially modulate the G protein-coupling efficiency of amylin receptors. Endocrinology 149 (2008) 5423-5431
27. Prado M.A., et al. The role of the CGRP-receptor component protein (RCP) in adrenomedullin receptor signal transduction. Peptides 22 (2001) 1773-1781
28. Kuwasako K., et al. Visualization of the calcitonin receptor-like receptor and its receptor activity-modifying proteins during internalization and Recycling. J. Biol. Chem. 275 (2000) 29602-29609
29. Kuwasako K., et al. Functions of the cytoplasmic tails of the human receptor activity-modifying protein components of calcitonin gene-related peptide and adrenomedullin receptors. J. Biol. Chem. 281 (2006) 7205-7213
30. Cottrell G.S., et al. Post-endocytic sorting of calcitonin receptor-like receptor and receptor activity-modifying protein 1. J. Biol. Chem. 282 (2007) 12260-12271
31. Hilairet S., et al. Agonist-promoted internalization of a ternary complex between calcitonin receptor-like receptor, receptor activity-modifying protein 1 (RAMP1), and beta -arrestin. J. Biol. Chem. 276 (2001) 42182-42190
32. Bomberger J.M., et al. Novel function for receptor activity-modifying proteins (RAMPs) in post-endocytic receptor trafficking. J. Biol. Chem. 280 (2005) 9297-9307
33. Bomberger J.M., et al. Receptor activity-modifying protein (RAMP) isoform-specific regulation of adrenomedullin receptor trafficking by NHERF-1. J. Biol. Chem. 280 (2005) 23926-23935
34. Phelps E., et al. Parathyroid hormone induces receptor activity modifying protein-3 (RAMP3) expression primarily via 3′, 5′-cyclic adenosine monophosphate signaling in osteoblasts. Calcif. Tissue Int. 77 (2005) 96-103
35. Yue W., et al. Frequent inactivation of RAMP2, EFEMP1 and Dutt1 in lung cancer by promoter hypermethylation. Clin. Cancer Res. 13 (2007) 4336-4344
36. Dackor R., et al. Receptor activity-modifying proteins 2 and 3 have distinct physiological functions from embryogenesis to old age. J. Biol. Chem. 282 (2007) 18094-18099
37. Fritz-Six K.L., et al. Adrenomedullin signaling is necessary for murine lymphatic vascular development. J. Clin. Invest. 118 (2008) 40-50
38. Ichikawa-Shindo Y., et al. The GPCR modulator protein RAMP2 is essential for angiogenesis and vascular integrity. J. Clin. Invest. 118 (2008) 29-39
39. Tsujikawa K., et al. Hypertension and dysregulated proinflammatory cytokine production in receptor activity-modifying protein 1-deficient mice. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 16702-16707
40. Zhang Z., et al. Sensitization of calcitonin gene-related peptide receptors by receptor activity-modifying protein-1 in the trigeminal ganglion. J. Neurosci. 27 (2007) 2693-2703
41. Tam C.W., et al. Enhanced vascular responses to adrenomedullin in mice overexpressing receptor-activity-modifying protein 2. Circ. Res. 98 (2006) 262-270
42. Zhao Y., et al. Differential expression of components of the cardiomyocyte adrenomedullin/intermedin receptor system following blood pressure reduction in nitric oxide-deficient hypertension. J. Pharmacol. Exp. Ther. 316 (2006) 1269-1281
43. Pidasheva S., et al. Impaired cotranslational processing of the calcium-sensing receptor due to signal peptide missense mutations in familial hypocalciuric hypercalcemia. Hum. Mol. Genet. 14 (2005) 1679-1690
44. Leach K., et al. Allosteric GPCR modulators: taking advantage of permissive receptor pharmacology. Trends Pharmacol. Sci. 28 (2007) 382-389
45. Salvatore C.A., et al. Pharmacological characterization of MK-0974 [N-[(3R,6S)-6-(2,3-Difluorophenyl)-2-oxo-1-(2,2,2-trifluoroethyl)azepan-3-yl]-4-(2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-1-yl)piperidine-1-carboxamide], a potent and orally active calcitonin gene-related peptide receptor antagonist for the treatment of migraine. J. Pharmacol. Exp. Ther. 324 (2008) 416-421
46. Mallee J.J., et al. Receptor activity-modifying protein 1 determines the species selectivity of non-peptide CGRP receptor antagonists. J. Biol. Chem. 277 (2002) 14294-14298
47. Doods H., et al. Pharmacological profile of BIBN4096BS, the first selective small molecule CGRP antagonist. Br. J. Pharmacol. 129 (2000) 420-423
48. Doods H., et al. CGRP antagonists: unravelling the role of CGRP in migraine. Trends Pharmacol. Sci. 28 (2007) 580-587
49. Ho T.W., et al. Efficacy and tolerability of MK-0974 (telcagepant), a new oral antagonist of calcitonin gene-related peptide receptor, compared with zolmitriptan for acute migraine: a randomised, placebo-controlled, parallel-treatment trial. The Lancet 372 (2008) 2115-2123
50. Benemei S., et al. Pain pharmacology in migraine: focus on CGRP and CGRP receptors. Neurol. Sci. 28 (2007) S89-S93
51. Hay D.L., et al. A comparison of the actions of BIBN4096BS and CGRP8-37 on CGRP and adrenomedullin receptors expressed on SK-N-MC, L6, Col 29 and Rat 2 cells. Br. J. Pharmacol. 137 (2002) 80
52. Salvatore C.A., et al. Identification and pharmacological characterization of domains involved in binding of CGRP receptor antagonists to the calcitonin-like receptor. Biochemistry 45 (2006) 1881-1887
53. Pioszak A.A., and Xu H.E. Molecular recognition of parathyroid hormone by its G protein-coupled receptor. Proc. Natl. Acad. Sci. U.S.A. 105 (2008) 5034-5039
54. Ittner L.M., et al. The N-terminal extracellular domain 23-60 of the calcitonin receptor-like receptor in chimeras with the parathyroid hormone receptor mediates association with receptor activity-modifying protein 1. Biochemistry 44 (2005) 5749-5754
55. Hilairet S., et al. Protein-protein interaction and not glycosylation determines the binding selectivity of heterodimers between the calcitonin receptor-like receptor and the receptor activity-modifying proteins. J. Biol. Chem. 276 (2001) 29575-29581
56. Heroux M., et al. Functional calcitonin gene-related peptide receptors are formed by the asymmetric assembly of a calcitonin receptor-like receptor homo-oligomer and a monomer of receptor activity-modifying protein-1. J. Biol. Chem. 282 (2007) 31610-31620
57. Kusano S., et al. Crystal structure of the human receptor activity-modifying protein 1 extracellular domain. Protein Sci. 17 (2008) 1907-1914
58. Simms J., et al. Characterization of the structure of RAMP1 by mutagenesis and molecular modeling. Biophys. J. 91 (2006) 662-669
59. Kunz T.H., et al. Interaction of receptor-activity-modifying protein1 with tubulin. Biochimica et Biophysica Acta (BBA)-General Subjects 1770 (2007) 1145-1150