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1. THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: Overview

Author

Alexander, Stephen PH, Kelly, Eamonn, Marrion, Neil, Peters, John A, Benson, Helen E, Faccenda, Elena, Pawson, Adam J, Sharman, Joanna L, Southan, Christopher, Buneman, Peter O, Catterall, William A, Cidlowski, John A, Davenport, Anthony P, Fabbro, Doriano, Fan, Grace, McGrath, John C, Spedding, Michael, Davies, Jamie A, Aldrich, R, Attali, B, Bäck, M l, Barnes, N M, Bathgate, R, Beart, P M, Becirovic, E, Biel, M, Birdsall, N J, Boison, D, Bräuner-Osborne, H, Bröer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, S L, Chandy, K G, Chiang, N, Christakos, S, Christopoulos, A, Chun, J J, Chung, J-J, Clapham, D E, Connor, M A, Coons, L, Cox, H M, Dautzenberg, F M, Dent, G, Douglas, S D, Dubocovich, M L, Edwards, D P, Farndale, R, Fong, T M, Forrest, D, Fowler, C J, Fuller, P, Gainetdinov, R R, Gershengorn, M A, Goldin, A, Goldstein, S AN, Grimm, S L, Grissmer, S, Gundlach, A L, Hagenbuch, B, Hammond, J R, Hancox, J C, Hartig, S, Hauger, R L, Hay, D L, Hébert, T, Hollenberg, A N, Holliday, N D, Hoyer, D, Ijzerman, A P, Inui, K I, Ishii, S, Jacobson, K A, Jan, L Y, Jarvis, G E, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, L K, Kanai, Y, Kang, H S, Karnik, S, Kerr, I D, Korach, K S, Lange, C A, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, S J, Macewan, D, Maguire, J J, May, J M, Mazella, J, Mcardle, C A, Mcdonnell, D P, Michel, M C, Miller, L J, Mitolo, V, Monie, T, Monk, P N, Mouillac, B, Murphy, P M, Nahon, J-L, Nerbonne, J, Nichols, C G, Norel, X, Oakley, R, Offermanns, S, Palmer, L G, Panaro, M A, Perez-Reyes, E, Pertwee, R G, Pike, J W, Pin, J P, Pintor, S, Plant, L D, Poyner, D R, Prossnitz, E R, Pyne, S, Ren, D, Richer, J K, Rondard, P, Ross, R A, Sackin, H, Safi, R, Sanguinetti, M C, Sartorius, C A, Segaloff, D L, Sladek, F M, Stewart, G, Stoddart, L A, Striessnig, J, Summers, R J, Takeda, Y, Tetel, M, Toll, L, Trimmer, J S, Tsai, M-J, Tsai, S Y, Tucker, S, Usdin, T B, Vilargada, J-P, Vore, M, Ward, D T, Waxman, S G, Webb, P, Wei, A D, Weigel, N, Willars, G B, Winrow, C, Wong, S S, Wulff, H, Ye, R D, Young, M, and Zajac, J-M

Published
2015
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3. THE CONCISE GUIDE TO PHARMACOLOGY 2017/18: Overview

Author

Alexander, Stephen PH, Kelly, Eamonn, Marrion, Neil V, Peters, John A, Faccenda, Elena, Harding, Simon D, Pawson, Adam J, Sharman, Joanna L, Southan, Christopher, Buneman, O Peter, Cidlowski, John A, Christopoulos, Arthur, Davenport, Anthony P, Fabbro, Doriano, Spedding, Michael, Striessnig, Jörg, Davies, Jamie A, Abbracchio, M. -P., Aldrich, R., Al-Hosaini, K., Arumugam, T. V., Attali, B., Bäck, M., Barnes, N. M., Bathgate, R., Beart, P. M., Becirovic, E., Bettler, B., Biel, M., Birdsall, N. J., Blaho, V., Boison, D., Bräuner-osborne, H., Bröer, S., Bryant, C., Burnstock, G., Calo, G., Catterall, W. A., Ceruti, S., Chan, S. L., Chandy, K. G., Chazot, P., Chiang, N., Chun, J. J., Chung, J. -J., Clapham, D. E., Clapp, L., Connor, M. A., Cox, H. M., Davies, P., Dawson, P. A., Decaen, P., Dent, G., Doherty, P., Douglas, S. D., Dubocovich, M. L., Fong, T. M., Fowler, C. J., Frantz, A., Fuller, P., Fumagalli, M., Futerman, A. H., Gainetdinov, R. R., Gershengorn, M. A., Goldin, A., Goldstein, S. A. N., Goudet, C., Gregory, K., Grissmer, S., Gundlach, A. L., Hagenbuch, B., Hamann, J., Hammond, J. R., Hancox, J. C., Hanson, J., Hanukoglu, I., Hay, D. L., Hobbs, A. J., Hollenberg, A. N., Holliday, N. D., Hoyer, D., Ijzerman, A. P., Inui, K. I., Irving, A. J., Ishii, S., Jacobson, K. A., Jan, L. Y., Jarvis, M. F., Jensen, R., Jockers, R., Kaczmarek, L. K., Kanai, Y., Karnik, S., Kellenberger, S., Kemp, S., Kennedy, C., Kerr, I. D., Kihara, Y., Kukkonen, J., Larhammar, D., Leach, K., Lecca, D., Leeman, S., Leprince, J., Lolait, S. J., Macewan, D., Maguire, J. J., Marshall, F., Mazella, J., Mcardle, C. A., Michel, M. C., Miller, L. J., Mitolo, V., Mizuno, H., Monk, P. N., Mouillac, B., Murphy, P. M., Nahon, J. -L., Nerbonne, J., Nichols, C. G., Norel, X., Offermanns, S., Palmer, L. G., Panaro, M. A., Papapetropoulos, A., Perez-reyes, E., Pertwee, R. G., Pintor, S., Pisegna, J. R., Plant, L. D., Poyner, D. R., Prossnitz, E. R., Pyne, S., Ramachandran, R., Ren, D., Rondard, P., Ruzza, C., Sackin, H., Sanger, G., Sanguinetti, M. C., Schild, L., Schiöth, H., Schulte, G., Schulz, S., Segaloff, D. L., Serhan, C. N., Singh, K. D., Slesinger, P. A., Snutch, T. P., Sobey, C. G., Stewart, G., Stoddart, L. A., Summers, R. J., Szabo, C., Thwaites, D., Toll, L., Trimmer, J. S., Tucker, S., Vaudry, H., Verri, T., Vilargada, J. -P., Waldman, S. A., Ward, D. T., Waxman, S. G., Wei, A. D., Willars, G. B., Wong, S. S., Woodruff, T. M., Wulff, H., Ye, R. D., Yung, Y., Zajac, J. -M., Alexander, Stephen PH, Kelly, Eamonn, Marrion, Neil V, Peters, John A, Faccenda, Elena, Harding, Simon D, Pawson, Adam J, Sharman, Joanna L, Southan, Christopher, Buneman, O Peter, Cidlowski, John A, Christopoulos, Arthur, Davenport, Anthony P, Fabbro, Doriano, Spedding, Michael, Striessnig, Jörg, Davies, Jamie A, Abbracchio, M. -P., Aldrich, R., Al-Hosaini, K., Arumugam, T. V., Attali, B., Bäck, M., Barnes, N. M., Bathgate, R., Beart, P. M., Becirovic, E., Bettler, B., Biel, M., Birdsall, N. J., Blaho, V., Boison, D., Bräuner-osborne, H., Bröer, S., Bryant, C., Burnstock, G., Calo, G., Catterall, W. A., Ceruti, S., Chan, S. L., Chandy, K. G., Chazot, P., Chiang, N., Chun, J. J., Chung, J. -J., Clapham, D. E., Clapp, L., Connor, M. A., Cox, H. M., Davies, P., Dawson, P. A., Decaen, P., Dent, G., Doherty, P., Douglas, S. D., Dubocovich, M. L., Fong, T. M., Fowler, C. J., Frantz, A., Fuller, P., Fumagalli, M., Futerman, A. H., Gainetdinov, R. R., Gershengorn, M. A., Goldin, A., Goldstein, S. A. N., Goudet, C., Gregory, K., Grissmer, S., Gundlach, A. L., Hagenbuch, B., Hamann, J., Hammond, J. R., Hancox, J. C., Hanson, J., Hanukoglu, I., Hay, D. L., Hobbs, A. J., Hollenberg, A. N., Holliday, N. D., Hoyer, D., Ijzerman, A. P., Inui, K. I., Irving, A. J., Ishii, S., Jacobson, K. A., Jan, L. Y., Jarvis, M. F., Jensen, R., Jockers, R., Kaczmarek, L. K., Kanai, Y., Karnik, S., Kellenberger, S., Kemp, S., Kennedy, C., Kerr, I. D., Kihara, Y., Kukkonen, J., Larhammar, D., Leach, K., Lecca, D., Leeman, S., Leprince, J., Lolait, S. J., Macewan, D., Maguire, J. J., Marshall, F., Mazella, J., Mcardle, C. A., Michel, M. C., Miller, L. J., Mitolo, V., Mizuno, H., Monk, P. N., Mouillac, B., Murphy, P. M., Nahon, J. -L., Nerbonne, J., Nichols, C. G., Norel, X., Offermanns, S., Palmer, L. G., Panaro, M. A., Papapetropoulos, A., Perez-reyes, E., Pertwee, R. G., Pintor, S., Pisegna, J. R., Plant, L. D., Poyner, D. R., Prossnitz, E. R., Pyne, S., Ramachandran, R., Ren, D., Rondard, P., Ruzza, C., Sackin, H., Sanger, G., Sanguinetti, M. C., Schild, L., Schiöth, H., Schulte, G., Schulz, S., Segaloff, D. L., Serhan, C. N., Singh, K. D., Slesinger, P. A., Snutch, T. P., Sobey, C. G., Stewart, G., Stoddart, L. A., Summers, R. J., Szabo, C., Thwaites, D., Toll, L., Trimmer, J. S., Tucker, S., Vaudry, H., Verri, T., Vilargada, J. -P., Waldman, S. A., Ward, D. T., Waxman, S. G., Wei, A. D., Willars, G. B., Wong, S. S., Woodruff, T. M., Wulff, H., Ye, R. D., Yung, Y., and Zajac, J. -M.

Subjects
Pharmacology
Abstract

The Concise Guide to PHARMACOLOGY 2017/18 is the third in this series of biennial publications. This version provides concise overviews of the key properties of nearly 1800 human drug targets with an emphasis on selective pharmacology (where available), plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide represents approximately 400 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point‐in‐time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13882/full. In addition to this overview, in which are identified ‘Other protein targets’ which fall outside of the subsequent categorisation, there are eight areas of focus: G protein‐coupled receptors, ligand‐gated ion channels, voltage‐gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid‐2017, and supersedes data presented in the 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the Nomenclature Committee of the Union of Basic and Clinical Pharmacology (NC‐IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate.

Published
2017

4. Modulation of Glucagon Receptor Pharmacology by Receptor Activity-modifying Protein-2 (RAMP2)

Author

Weston, C., Lu, J., Li, N., Barkan, K., Richards, G.O., Roberts, D.J., Skerry, T.M., Poyner, D., Pardamwar, M., Reynolds, C.A., Dowell, S.J., Willars, G.B., and Ladds, G.

Subjects
endocrine system, digestive, oral, and skin physiology, hormones, hormone substitutes, and hormone antagonists
Abstract

The glucagon and glucagon-like peptide-1 (GLP-1) receptors\ud play important, opposing roles in regulating blood glucose levels.\ud Consequently, these receptors have been identified as targets\ud for novel diabetes treatments. However, drugs acting at the\ud GLP-1 receptor, although having clinical efficacy, have been\ud associated with severe adverse side-effects, and targeting of the\ud glucagon receptor has yet to be successful. Here we use a combination\ud of yeast reporter assays and mammalian systems to\ud provide a more complete understanding of glucagon receptor\ud signaling, considering the effect of multiple ligands, association\ud with the receptor-interacting protein receptor activity-modifying\ud protein-2 (RAMP2), and the role of individual G protein\ud -subunits. We demonstrate that RAMP2 alters both ligand\ud selectivity and G protein preference of the glucagon receptor.\ud Importantly, we also uncover novel cross-reactivity of therapeutically\ud used GLP-1 receptor ligands at the glucagon receptor that\ud is abolished by RAMP2 interaction. This study reveals the glucagon\ud receptor as a previously unidentified target for GLP-1\ud receptor agonists and highlights a role for RAMP2 in regulating\ud its pharmacology. Such previously unrecognized functions of\ud RAMPs highlight the need to consider all receptor-interacting\ud proteins in future drug development.\ud

Published
2015

5. Microbial expression systems for membrane proteins

Author

Marvin V. Dilworth, Roslyn M. Bill, David R. Poyner, Stephane R. Gross, Peter J. F. Henderson, Bruno Miroux, Pikyee Ma, Karine Moncoq, Kim E. Bettaney, Mathilde S. Piel, Ji Luo, David Sharples, Laboratoire de biologie physico-chimique des protéines membranaires (LBPC-PM (UMR_7099)), Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Instituto de Tecnologia Química e Biológica António Xavier (ITQB), Universidade Nova de Lisboa = NOVA University Lisbon (NOVA), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), ANR-11-LABX-0011,DYNAMO,Dynamique des membranes transductrices d'énergie : biogénèse et organisation supramoléculaire.(2011), Bettaney, K, Ma, P, Luo, J, Sharples, D, Poyner, D, Gross, S, Moncoq, K, Miroux, B, and Bill, RM

Subjects
0301 basic medicine, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Bacteria, Chemistry, Membrane Proteins, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Promoter, Computational biology, General Biochemistry, Genetics and Molecular Biology, Recombinant Proteins, law.invention, 03 medical and health sciences, 030104 developmental biology, Membrane protein, Cell culture, law, Solubilization, Yeasts, Recombinant DNA, Promoter Regions, Genetic, Molecular Biology, ComputingMilieux_MISCELLANEOUS, Plasmids
Abstract

Despite many high-profile successes, recombinant membrane protein production remains a technical challenge; it is still the case that many fewer membrane protein structures have been published than those of soluble proteins. However, progress is being made because empirical methods have been developed to produce the required quantity and quality of these challenging targets. This review focuses on the microbial expression systems that are a key source of recombinant prokaryotic and eukaryotic membrane proteins for structural studies. We provide an overview of the host strains, tags and promoters that, in our experience, are most likely to yield protein suitable for structural and functional characterization. We also catalogue the detergents used for solubilization and crystallization studies of these proteins. Here, we emphasize a combination of practical methods, not necessarily high-throughput, which can be implemented in any laboratory equipped for recombinant DNA technology and microbial cell culture.

Published
2018

6. Interactions between RAMP2 and CRF receptors: The effect of receptor subtypes, splice variants and cell context.

Author

Bailey S, Harris M, Barkan K, Winfield I, Harper MT, Simms J, Ladds G, Wheatley M, and Poyner D

Subjects
Animals, COS Cells, Chlorocebus aethiops, HEK293 Cells, Humans, Models, Molecular, Receptor Activity-Modifying Protein 2 chemistry, Receptor Activity-Modifying Protein 2 genetics, Receptors, Corticotropin-Releasing Hormone chemistry, Receptors, Corticotropin-Releasing Hormone genetics, Alternative Splicing genetics, Receptor Activity-Modifying Protein 2 metabolism, Receptors, Corticotropin-Releasing Hormone metabolism
Abstract

Corticotrophin releasing factor (CRF) acts via two family B G-protein-coupled receptors, CRFR1 and CRFR2. Additional subtypes exist due to alternative splicing. CRFR1α is the most widely expressed subtype and lacks a 29-residue insert in the first intracellular loop that is present in CRFR1β. It has been shown previously that co-expression of CRFR1β with receptor activity modifying protein 2 (RAMP2) in HEK 293S cells increased the cell-surface expression of both proteins suggesting a physical interaction as seen with RAMPs and calcitonin receptor-like receptor (CLR). This study investigated the ability of CRFR1α, CRFR1β and CRFR2β to promote cell-surface expression of FLAG-tagged RAMP2. Four different cell-lines were utilised to investigate the effect of varying cellular context; COS-7, HEK 293T, HEK 293S and [ΔCTR]HEK 293 (which lacks endogenous calcitonin receptor). In all cell-lines, CRFR1α and CRFR1β enhanced RAMP2 cell-surface expression. The magnitude of the effect on RAMP2 was dependent on the cell-line ([ΔCTR]HEK 293 > COS-7 > HEK 293T > HEK 293S). RT-PCR indicated this variation may relate to differences in endogenous RAMP expression between cell types. Furthermore, pre-treatment with CRF resulted in a loss of cell-surface FLAG-RAMP2 when it was co-expressed with CRFR1 subtypes. CRFR2β co-expression had no effect on RAMP2 in any cell-line. Molecular modelling suggests that the potential contact interface between the extracellular domains of RAMP2 and CRF receptor subtypes is smaller than that of RAMP2 and CRL, the canonical receptor:RAMP pairing, assuming a physical interaction. Furthermore, a specific residue difference between CRFR1 subtypes (glutamate) and CRFR2β (histidine) in this interface region may impair CRFR2β:RAMP2 interaction by electrostatic repulsion., (Copyright © 2019 Elsevier B.V. All rights reserved.)

Published
2019
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7. The Structure of the CGRP and Related Receptors.

Author

Simms J, Routledge S, Uddin R, and Poyner D

Subjects
Calcitonin Receptor-Like Protein, Ligands, Receptors, G-Protein-Coupled genetics, Adrenomedullin, Calcitonin Gene-Related Peptide
Abstract

The canonical CGRP receptor is a complex between calcitonin receptor-like receptor (CLR), a family B G-protein-coupled receptor (GPCR) and receptor activity-modifying protein 1 (RAMP1). A third protein, receptor component protein (RCP) is needed for coupling to Gs. CGRP can interact with other RAMP-receptor complexes, particularly the AMY1 receptor formed between the calcitonin receptor (CTR) and RAMP1. Crystal structures are available for the binding of CGRP 27-37 [D 31 ,P 34 ,F 35 ] to the extracellular domain (ECD) of CLR and RAMP1; these show that extreme C-terminal amide of CGRP interacts with W84 of RAMP1 but the rest of the analogue interacts with CLR. Comparison with the crystal structure of a fragment of the allied peptide adrenomedullin bound to the ECD of CLR/RAMP2 confirms the importance of the interaction of the ligand C-terminus and the RAMP in determining pharmacology specificity, although the RAMPs probably also have allosteric actions. A cryo-electron microscope structure of calcitonin bound to the full-length CTR associated with Gs gives important clues as to the structure of the complete receptor and suggests that the N-terminus of CGRP makes contact with His 5.40b , high on TM5 of CLR. However, it is currently not known how the RAMPs interact with the TM bundle of any GPCR. Major challenges remain in understanding how the ECD and TM domains work together to determine ligand specificity, and how G-proteins influence this and the role of RCP. It seems likely that allosteric mechanisms are particularly important as are the dynamics of the receptors.

Published
2019
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8. Functional characterisation of G protein-coupled receptors.

Author

Uddin R, Simms J, and Poyner D

Subjects
Allosteric Regulation, Fluorescence Resonance Energy Transfer, Guanosine 5'-O-(3-Thiotriphosphate) metabolism, Humans, Protein Conformation, Receptors, G-Protein-Coupled chemistry, Receptors, G-Protein-Coupled physiology
Abstract

Characterisation of receptors can involve either assessment of their ability to bind ligands or measure receptor activation as a result of agonist or inverse agonist interactions. This review focuses on G protein-coupled receptors (GPCRs), examining techniques that can be applied to both receptors in membranes and after solubilisation. Radioligand binding remains a widely used technique, although there is increasing use of fluorescent ligands. These can be used in a variety of experimental designs, either directly monitoring ligand itself with techniques such as fluorescence polarisation or indirectly via resonance energy transfer (fluorescence/Forster resonance energy transfer, FRET and bioluminescence resonance energy transfer, BRET). Label free techniques such as isothermal titration calorimetry (ITC) and surface plasmon resonance (SPR) are also increasingly being used. For GPCRs, the main measure of receptor activation is to investigate the association of the G protein with the receptor. The chief assay measures the receptor-stimulated binding of GTP or a suitable analogue to the receptor. The direct association of the G protein with the receptor has been investigated via resonance energy techniques. These have also been used to measure ligand-induced conformational changes within the receptor; a variety of experimental techniques are available to incorporate suitable donors and acceptors within the receptor., (Copyright © 2018 Elsevier Inc. All rights reserved.)

Published
2018
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9. Modulation of Glucagon Receptor Pharmacology by Receptor Activity-modifying Protein-2 (RAMP2).

Author

Weston C, Lu J, Li N, Barkan K, Richards GO, Roberts DJ, Skerry TM, Poyner D, Pardamwar M, Reynolds CA, Dowell SJ, Willars GB, and Ladds G

Subjects
Glucagon-Like Peptide-1 Receptor genetics, HEK293 Cells, Humans, Ligands, Receptor Activity-Modifying Protein 2 genetics, Glucagon pharmacology, Glucagon-Like Peptide-1 Receptor agonists, Glucagon-Like Peptide-1 Receptor metabolism, Receptor Activity-Modifying Protein 2 metabolism
Abstract

The glucagon and glucagon-like peptide-1 (GLP-1) receptors play important, opposing roles in regulating blood glucose levels. Consequently, these receptors have been identified as targets for novel diabetes treatments. However, drugs acting at the GLP-1 receptor, although having clinical efficacy, have been associated with severe adverse side-effects, and targeting of the glucagon receptor has yet to be successful. Here we use a combination of yeast reporter assays and mammalian systems to provide a more complete understanding of glucagon receptor signaling, considering the effect of multiple ligands, association with the receptor-interacting protein receptor activity-modifying protein-2 (RAMP2), and the role of individual G protein α-subunits. We demonstrate that RAMP2 alters both ligand selectivity and G protein preference of the glucagon receptor. Importantly, we also uncover novel cross-reactivity of therapeutically used GLP-1 receptor ligands at the glucagon receptor that is abolished by RAMP2 interaction. This study reveals the glucagon receptor as a previously unidentified target for GLP-1 receptor agonists and highlights a role for RAMP2 in regulating its pharmacology. Such previously unrecognized functions of RAMPs highlight the need to consider all receptor-interacting proteins in future drug development., (© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.)

Published
2015
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