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Volumn 2, Issue , 2016, Pages

An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology

Author keywords

accessory protein; Amylin; CGRP; G protein coupled receptor; RAMP

Indexed keywords

AMYLIN; C PEPTIDE; CALCITONIN; CALCITONIN GENE RELATED PEPTIDE RECEPTOR; CALCITONIN RECEPTOR; G PROTEIN COUPLED RECEPTOR; RECEPTOR; RECEPTOR ACTIVITY MODIFYING PROTEIN; RECEPTOR ACTIVITY MODIFYING PROTEIN 1; RECEPTOR ACTIVITY MODIFYING PROTEIN 2; RECEPTOR ACTIVITY MODIFYING PROTEIN 3;

EID: 85018030657     PISSN: None     EISSN: 20565968     Source Type: Journal    
DOI: 10.1038/celldisc.2016.12     Document Type: Article
Times cited : (48)

References (49)
  • 1
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of G protein-coupled receptors and significance for drug discovery
    • Lagerstrom MC, Schioth HB. Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat Rev Drug Discov 2008; 7: 339-357.
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 339-357
    • Lagerstrom, M.C.1    Schioth, H.B.2
  • 2
    • 77952354490 scopus 로고    scopus 로고
    • Seven transmembrane receptors as shapeshifting proteins: The impact of allosteric modulation and functional selectivity on new drug discovery
    • Kenakin T, Miller LJ. Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery. Pharmacol Rev 2010; 62: 265-304.
    • (2010) Pharmacol Rev , vol.62 , pp. 265-304
    • Kenakin, T.1    Miller, L.J.2
  • 3
    • 0032574982 scopus 로고    scopus 로고
    • RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor
    • McLatchie LM, Fraser NJ, Main MJ et al. RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor. Nature 1998; 393: 333-339.
    • (1998) Nature , vol.393 , pp. 333-339
    • McLatchie, L.M.1    Fraser, N.J.2    Main, M.J.3
  • 4
    • 62849124664 scopus 로고    scopus 로고
    • Modulating receptor function through RAMPs: Can they represent drug targets in themselves?
    • Sexton PM, Poyner DR, Simms J, Christopoulos A, Hay DL. Modulating receptor function through RAMPs: can they represent drug targets in themselves? Drug Discov Today 2009; 14: 413-419.
    • (2009) Drug Discov Today , vol.14 , pp. 413-419
    • Sexton, P.M.1    Poyner, D.R.2    Simms, J.3    Christopoulos, A.4    Hay, D.L.5
  • 6
    • 71549119499 scopus 로고    scopus 로고
    • Molecular basis of association of receptor activity-modifying protein 3 with the family B G protein-coupled secretin receptor
    • Harikumar KG, Simms J, Christopoulos G, Sexton PM, Miller LJ. Molecular basis of association of receptor activity-modifying protein 3 with the family B G protein-coupled secretin receptor. Biochemistry 2009; 48: 11773-11785.
    • (2009) Biochemistry , vol.48 , pp. 11773-11785
    • Harikumar, K.G.1    Simms, J.2    Christopoulos, G.3    Sexton, P.M.4    Miller, L.J.5
  • 7
    • 0033039911 scopus 로고    scopus 로고
    • Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product
    • Christopoulos G, Perry KJ, MorfisMet al. Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. Mol Pharmacol 1999; 56: 235-242.
    • (1999) Mol Pharmacol , vol.56 , pp. 235-242
    • Christopoulos, G.1    Perry, K.J.2    Morfis, M.3
  • 8
    • 0037474327 scopus 로고    scopus 로고
    • Novel receptor partners and function of receptor activitymodifying proteins
    • Christopoulos A, Christopoulos G, Morfis M et al. Novel receptor partners and function of receptor activitymodifying proteins. J Biol Chem 2003; 278: 3293-3297.
    • (2003) J Biol Chem , vol.278 , pp. 3293-3297
    • Christopoulos, A.1    Christopoulos, G.2    Morfis, M.3
  • 9
    • 27844496106 scopus 로고    scopus 로고
    • Receptor-activitymodifying proteins are required for forward trafficking of the calcium-sensing receptor to the plasma membrane
    • Bouschet T, Martin S, Henley JM. Receptor-activitymodifying proteins are required for forward trafficking of the calcium-sensing receptor to the plasma membrane. J Cell Sci 2005; 118: 4709-4720.
    • (2005) J Cell Sci , vol.118 , pp. 4709-4720
    • Bouschet, T.1    Martin, S.2    Henley, J.M.3
  • 10
    • 84872946955 scopus 로고    scopus 로고
    • Receptor activity modifying proteins (RAMPs) interact with the VPAC2 receptor and CRF1 receptors and modulate their function
    • Wootten D, Lindmark H, Kadmiel M et al. Receptor activity modifying proteins (RAMPs) interact with the VPAC2 receptor and CRF1 receptors and modulate their function. Brit J Pharmacol 2013; 168: 822-834.
    • (2013) Brit J Pharmacol , vol.168 , pp. 822-834
    • Wootten, D.1    Lindmark, H.2    Kadmiel, M.3
  • 11
    • 84879985064 scopus 로고    scopus 로고
    • G-protein-coupled receptor 30 interacts with receptor activity-modifying protein 3 and confers sex-dependent cardioprotection
    • Lenhart PM, Broselid S, Barrick CJ, Leeb-Lundberg LM, Caron KM. G-protein-coupled receptor 30 interacts with receptor activity-modifying protein 3 and confers sex-dependent cardioprotection. J Mol Endocrinol 2013; 51: 191-202.
    • (2013) J Mol Endocrinol , vol.51 , pp. 191-202
    • Lenhart, P.M.1    Broselid, S.2    Barrick, C.J.3    Leeb-Lundberg, L.M.4    Caron, K.M.5
  • 12
    • 84942860294 scopus 로고    scopus 로고
    • Modulation of glucagon receptor pharmacology by receptor activity-modifying protein-2 (RAMP2)
    • Weston C, Lu J, Li N et al. Modulation of glucagon receptor pharmacology by receptor activity-modifying protein-2 (RAMP2). J Biol Chem 2015; 290: 23009-23022.
    • (2015) J Biol Chem , vol.290 , pp. 23009-23022
    • Weston, C.1    Lu, J.2    Li, N.3
  • 15
    • 84940026739 scopus 로고    scopus 로고
    • A second trigeminal CGRP receptor: Function and expression of the AMY1 receptor
    • Walker CS, Eftekhari S, Bower RL et al. A second trigeminal CGRP receptor: function and expression of the AMY1 receptor. Ann Clin Transl Neurol 2015; 2: 595-608.
    • (2015) Ann Clin Transl Neurol , vol.2 , pp. 595-608
    • Walker, C.S.1    Eftekhari, S.2    Bower, R.L.3
  • 16
    • 84937629357 scopus 로고    scopus 로고
    • Structural basis for receptor activity-modifying protein-dependent selective peptide recognition by a G protein-coupled receptor
    • Booe JM, Walker CS, Barwell J et al. Structural basis for receptor activity-modifying protein-dependent selective peptide recognition by a G protein-coupled receptor. Mol Cell 2015; 58: 1040-1052.
    • (2015) Mol Cell , vol.58 , pp. 1040-1052
    • Booe, J.M.1    Walker, C.S.2    Barwell, J.3
  • 17
    • 35348845217 scopus 로고    scopus 로고
    • Crystal structure of the incretin-bound extracellular domain of a G protein-coupled receptor
    • Parthier C, Kleinschmidt M, Neumann P et al. Crystal structure of the incretin-bound extracellular domain of a G protein-coupled receptor. Proc Natl Acad Sci USA 2007; 104: 13942-13947.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 13942-13947
    • Parthier, C.1    Kleinschmidt, M.2    Neumann, P.3
  • 18
    • 42449160533 scopus 로고    scopus 로고
    • Molecular recognition of parathyroid hormone by its G protein-coupled receptor
    • Pioszak AA, Xu HE. Molecular recognition of parathyroid hormone by its G protein-coupled receptor. Proc Natl Acad Sci USA 2008; 105: 5034-5039.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5034-5039
    • Pioszak, A.A.1    Xu, H.E.2
  • 19
    • 70350504319 scopus 로고    scopus 로고
    • Structural basis for parathyroid hormone-related protein binding to the parathyroid hormone receptor and design of conformation-selective peptides
    • Pioszak AA, Parker NR, Gardella TJ, Xu HE. Structural basis for parathyroid hormone-related protein binding to the parathyroid hormone receptor and design of conformation-selective peptides. J Biol Chem 2009; 284: 28382-28391.
    • (2009) J Biol Chem , vol.284 , pp. 28382-28391
    • Pioszak, A.A.1    Parker, N.R.2    Gardella, T.J.3    Xu, H.E.4
  • 20
    • 45549086826 scopus 로고    scopus 로고
    • Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain
    • Runge S, Thogersen H, Madsen K, Lau J, Rudolph R. Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain. J Biol Chem 2008; 283: 11340-11347.
    • (2008) J Biol Chem , vol.283 , pp. 11340-11347
    • Runge, S.1    Thogersen, H.2    Madsen, K.3    Lau, J.4    Rudolph, R.5
  • 21
    • 73649107900 scopus 로고    scopus 로고
    • Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor
    • Underwood CR, Garibay P, Knudsen LB et al. Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor. J Biol Chem 2010; 285: 723-730.
    • (2010) J Biol Chem , vol.285 , pp. 723-730
    • Underwood, C.R.1    Garibay, P.2    Knudsen, L.B.3
  • 22
    • 80053374553 scopus 로고    scopus 로고
    • Structural insights into RAMP modification of secretin family G protein-coupled receptors: Implications for drug development
    • Archbold JK, Flanagan JU, Watkins HA, Gingell JJ, Hay DL. Structural insights into RAMP modification of secretin family G protein-coupled receptors: implications for drug development. Trends Pharmacol Sci 2011; 32: 591-600.
    • (2011) Trends Pharmacol Sci , vol.32 , pp. 591-600
    • Archbold, J.K.1    Flanagan, J.U.2    Watkins, H.A.3    Gingell, J.J.4    Hay, D.L.5
  • 23
    • 17844365264 scopus 로고    scopus 로고
    • Pharmacological discrimination of calcitonin receptor: Receptor activity-modifying protein complexes
    • Hay DL, Christopoulos G, Christopoulos A, Poyner DR, Sexton PM. Pharmacological discrimination of calcitonin receptor: receptor activity-modifying protein complexes. Mol Pharmacol 2005; 67: 1655-1665.
    • (2005) Mol Pharmacol , vol.67 , pp. 1655-1665
    • Hay, D.L.1    Christopoulos, G.2    Christopoulos, A.3    Poyner, D.R.4    Sexton, P.M.5
  • 24
    • 0033932339 scopus 로고    scopus 로고
    • Amylin receptor phenotypes derived from human calcitonin receptor/RAMP coexpression exhibit pharmacological differences dependent on receptor isoform and host cell environment
    • Tilakaratne N, Christopoulos G, Zumpe ET, Foord SM, Sexton PM. 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 2000; 294: 61-72.
    • (2000) J Pharmacol Exp Ther , vol.294 , pp. 61-72
    • Tilakaratne, N.1    Christopoulos, G.2    Zumpe, E.T.3    Foord, S.M.4    Sexton, P.M.5
  • 25
    • 54349103237 scopus 로고    scopus 로고
    • Receptor activity-modifying proteins differentially modulate the G protein-coupling efficiency of amylin receptors
    • Morfis M, Tilakaratne N, Furness SG et al. Receptor activity-modifying proteins differentially modulate the G protein-coupling efficiency of amylin receptors. Endocrinology 2008; 149: 5423-5431.
    • (2008) Endocrinology , vol.149 , pp. 5423-5431
    • Morfis, M.1    Tilakaratne, N.2    Furness, S.G.3
  • 26
    • 84930226866 scopus 로고    scopus 로고
    • Structural insights into the dynamic process of β2-adrenergic receptor signaling
    • Manglik A, Kim TH, Masureel M et al. Structural insights into the dynamic process of β2-adrenergic receptor signaling. Cell 2015; 161: 1101-1111.
    • (2015) Cell , vol.161 , pp. 1101-1111
    • Manglik, A.1    Kim, T.H.2    Masureel, M.3
  • 27
    • 84939795137 scopus 로고    scopus 로고
    • Structural insights into μ-opioid receptor activation
    • Huang W, Manglik A, Venkatakrishnan AJ et al. Structural insights into μ-opioid receptor activation. Nature 2015; 524: 315-321.
    • (2015) Nature , vol.524 , pp. 315-321
    • Huang, W.1    Manglik, A.2    Venkatakrishnan, A.J.3
  • 28
    • 84939832832 scopus 로고    scopus 로고
    • Propagation of conformational changes during μ-opioid receptor activation
    • Sounier R, Mas C, Steyaert J et al. Propagation of conformational changes during μ-opioid receptor activation. Nature 2015; 524: 375-378.
    • (2015) Nature , vol.524 , pp. 375-378
    • Sounier, R.1    Mas, C.2    Steyaert, J.3
  • 29
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the β2 adrenergic receptor-Gs protein complex
    • Rasmussen SG, DeVree BT, Zou Y et al. Crystal structure of the β2 adrenergic receptor-Gs protein complex. Nature 2011; 477: 549-555.
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.1    DeVree, B.T.2    Zou, Y.3
  • 30
    • 84887620421 scopus 로고    scopus 로고
    • Structural basis for modulation of a G-protein-coupled receptor by allosteric drugs
    • Dror RO, Grren HF, Valant C et al. Structural basis for modulation of a G-protein-coupled receptor by allosteric drugs. Nature 2013; 503: 295-299.
    • (2013) Nature , vol.503 , pp. 295-299
    • Dror, R.O.1    Grren, H.F.2    Valant, C.3
  • 32
    • 84938900365 scopus 로고    scopus 로고
    • Adaptability of protein structures to enable functional interactions and evolutionary implications
    • Haliloglu T, Bahar I. Adaptability of protein structures to enable functional interactions and evolutionary implications. Curr Opin Struct Biol 2015; 35: 17-23.
    • (2015) Curr Opin Struct Biol , vol.35 , pp. 17-23
    • Haliloglu, T.1    Bahar, I.2
  • 33
    • 84895745240 scopus 로고    scopus 로고
    • A unified view of 'how allostery works'
    • Tsai CJ, Nussinov R. A unified view of 'how allostery works'. PLoS Comput Biol 2014; 10: e1003394.
    • (2014) PLoS Comput Biol , vol.10 , pp. e1003394
    • Tsai, C.J.1    Nussinov, R.2
  • 34
    • 84979742824 scopus 로고    scopus 로고
    • Calcitonin and amylin receptor peptide interaction mechanisms: Insights into peptide-binding modes and allosteric modulation of the calcitonin receptor by receptor activity-modifying proteins
    • (e-pub ahead of print 19 February; doi: pii:jbc.M115.713628)
    • Lee SM, Hay DL, Pioszak AA. Calcitonin and amylin receptor peptide interaction mechanisms: Insights into peptide-binding modes and allosteric modulation of the calcitonin receptor by receptor activity-modifying proteins. J Biol Chem. (e-pub ahead of print 19 February 2016; doi: pii:jbc.M115.713628).
    • (2016) J Biol Chem.
    • Lee, S.M.1    Hay, D.L.2    Pioszak, A.A.3
  • 35
    • 33745164943 scopus 로고    scopus 로고
    • Distinct receptor activity-modifying protein domains differentially modulate interaction with calcitonin receptors
    • Udawela M, Christopoulos G, Tilakaratne N et al. Distinct receptor activity-modifying protein domains differentially modulate interaction with calcitonin receptors. Mol Pharmacol 2006a; 69: 1984-1989.
    • (2006) Mol Pharmacol , vol.69 , pp. 1984-1989
    • Udawela, M.1    Christopoulos, G.2    Tilakaratne, N.3
  • 36
    • 33751173881 scopus 로고    scopus 로고
    • A critical role for the short intracellular C terminus in receptor activity-modifying protein function
    • Udawela M, Christopoulos G, Morifs M et al. A critical role for the short intracellular C terminus in receptor activity-modifying protein function. Mol Pharmacol 2006b; 70: 1750-1760.
    • (2006) Mol Pharmacol , vol.70 , pp. 1750-1760
    • Udawela, M.1    Christopoulos, G.2    Morifs, M.3
  • 37
    • 84882709451 scopus 로고    scopus 로고
    • Role of CGRP-receptor component protein (RCP) in CLR/RAMP function
    • Dickerson IM. Role of CGRP-receptor component protein (RCP) in CLR/RAMP function. Curr Protein Pept Sci 2013; 14: 407-415.
    • (2013) Curr Protein Pept Sci , vol.14 , pp. 407-415
    • Dickerson, I.M.1
  • 38
    • 84891274041 scopus 로고    scopus 로고
    • Structure-activity relationships of the N-terminus of calcitonin gene-related peptide: Key roles of alanine-5 and threonine-6 in receptor activation
    • Hay DL, Harris PW, Kowalczyk R et al. Structure-activity relationships of the N-terminus of calcitonin gene-related peptide: key roles of alanine-5 and threonine-6 in receptor activation. Brit J Pharmacol 2014; 171: 415-426.
    • (2014) Brit J Pharmacol , vol.171 , pp. 415-426
    • Hay, D.L.1    Harris, P.W.2    Kowalczyk, R.3
  • 39
    • 1342282976 scopus 로고    scopus 로고
    • Spatial proximity between a photolabile residue in position 19 of salmon calcitonin and the amino terminus of the human calcitonin receptor
    • Pham V, Wade JD, Purdue BW, Sexton PM. Spatial proximity between a photolabile residue in position 19 of salmon calcitonin and the amino terminus of the human calcitonin receptor. J Biol Chem 2004; 279: 6720-6729.
    • (2004) J Biol Chem , vol.279 , pp. 6720-6729
    • Pham, V.1    Wade, J.D.2    Purdue, B.W.3    Sexton, P.M.4
  • 40
    • 0036266044 scopus 로고    scopus 로고
    • International union of pharmacology. XXXII. The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors
    • Poyner DR, Sexton PM, Marshall I et al. International Union of Pharmacology. XXXII. The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors. Pharmacol Rev 2002; 54: 233-246.
    • (2002) Pharmacol Rev , vol.54 , pp. 233-246
    • Poyner, D.R.1    Sexton, P.M.2    Marshall, I.3
  • 41
    • 84872381155 scopus 로고    scopus 로고
    • Receptor activitymodifying protein-dependent impairment of calcitonin receptor splice variant delta(1-47)hCT((a)) function
    • Qi T, Dong M, Watkins HA et al. Receptor activitymodifying protein-dependent impairment of calcitonin receptor splice variant Delta(1-47)hCT((a)) function. Brit J Pharmacol 2013; 168: 644-657.
    • (2013) Brit J Pharmacol , vol.168 , pp. 644-657
    • Qi, T.1    Dong, M.2    Watkins, H.A.3
  • 42
    • 34347349008 scopus 로고    scopus 로고
    • Agonist-dependent consequences of proline to alanine substitution in the transmembrane helices of the calcitonin receptor
    • Bailey RJ, Hay DL. Agonist-dependent consequences of proline to alanine substitution in the transmembrane helices of the calcitonin receptor. Brit J Pharmacol 2007; 151: 678-687.
    • (2007) Brit J Pharmacol , vol.151 , pp. 678-687
    • Bailey, R.J.1    Hay, D.L.2
  • 43
    • 58549084401 scopus 로고    scopus 로고
    • Structure-function analysis of RAMP1 by alanine mutagenesis
    • Simms J, Hay DL, Bailey RJ et al. Structure-function analysis of RAMP1 by alanine mutagenesis. Biochemistry 2009; 48: 198-205.
    • (2009) Biochemistry , vol.48 , pp. 198-205
    • Simms, J.1    Hay, D.L.2    Bailey, R.J.3
  • 44
    • 77952581108 scopus 로고    scopus 로고
    • A key role for tryptophan 84 in receptor activity-modifying protein 1 in the amylin 1 receptor
    • Gingell JJ, Qi T, Bailey RJ, Hay DL. A key role for tryptophan 84 in receptor activity-modifying protein 1 in the amylin 1 receptor. Peptides 2010; 31: 1400-1404.
    • (2010) Peptides , vol.31 , pp. 1400-1404
    • Gingell, J.J.1    Qi, T.2    Bailey, R.J.3    Hay, D.L.4
  • 45
    • 0043123123 scopus 로고    scopus 로고
    • Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments
    • Poirot O, O'Toole E, Notredame C. Tcoffee@igs: a web server for computing, evaluating and combining multiple sequence alignments. Nucleic Acids Res 2003; 31: 3503-3506.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3503-3506
    • Poirot, O.1    O'Toole, E.2    Notredame, C.3
  • 46
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993; 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 47
    • 0035175679 scopus 로고    scopus 로고
    • PDBsum: Summaries and analyses of PDB structures
    • Laskowski RA. PDBsum: summaries and analyses of PDB structures. Nucleic Acids Res 2001; 29: 221-222.
    • (2001) Nucleic Acids Res , vol.29 , pp. 221-222
    • Laskowski, R.A.1
  • 48
    • 28644432877 scopus 로고    scopus 로고
    • Very fast empirical prediction and rationalization of protein pKa values
    • Li H, Robertson AD, Jensen JH. Very fast empirical prediction and rationalization of protein pKa values. Proteins 2005; 61: 704-721.
    • (2005) Proteins , vol.61 , pp. 704-721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 49
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky TJ, Czodrowski P, Li H et al. PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic Acids Res 2007; 35: W522-W525.
    • (2007) Nucleic Acids Res , vol.35 , pp. W522-W525
    • Dolinsky, T.J.1    Czodrowski, P.2    Li, H.3


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