Professor David R. Poyner

Prof David Poyner
Prof David Poyner

Professor in Pharmacology

School of Life and Health Sciences
Aston University
Aston Triangle
Birmingham B4 7ET

email: d.r.poyner@aston.ac.uk
telephone: +44 (0) 121 204 3997
fax: +44 (0) 121359 5142

Member of the Pharmacy and Biology Teaching Programmes

Research Theme

Cellular and Molecular Biomedicine 

Research Centre

Aston Research Centre for Healthy Ageing (ARCHA) 


I graduated in Natural Sciences from Cambridge University in 1981and then stayed to do a Ph.D in the pharmacology department under the supervision of Prof. Sir Arnold Burgen. I subsequently did post-doctoral work at the National Institute for Medical Research, working with Drs Ed Hulme and Nigel Birdsall and then at the MRC Molecular Neurobiology Unit in Cambridge with Dr Mike Hanley. It was here that I first started to work on the pharmacology of calcitonin gene related peptide (CGRP). I was appointed to a lectureship at Aston University in 1991 where I have continued my work on this and allied peptides

Teaching Activity on the MPharm Programme

PH1401: Physiology.
PH2501 (module coordinator): Pharmacology

Qualifications & Education

  • 1982 - 1985 PhD University of Cambridge

  • 1978 - 1982 BA, Pharmacology (Class I), University of Cambridge


  • 2005 – date Reader Pharmacology, Aston University
  • 2000 – 2005 Senior Lecturer in Pharmacology, Aston University
  • 1991 – 2000 Lecturer in Pharmacology, Aston University
  • 1988 – 1991 MRC Short Term Staff Scientist, MRC Molecular Neurobiology Unit, Laboratory of Molecular Biology, Cambridge
  • 1985 – 1988 MRC Training Fellow, National Institute for Medical Research, London

Teaching activity

I specialise in the teaching of molecular pharmacology, especially cell receptors and signal transduction. I also teach general pharamacology and physiology, cell biology and biochemistry. I teach at all levels of the programme from 1st year to M.Sc. and I am head of the pharmacology teaching group.

Main modules taught:

  • Pharmacology of peripheral systems
  • Clinical and Molecular Endocrinology
  • Biochemistry
  • Physiology
  • Endocrinology
  • Human Physiology
  • Therapeutics of the Future

Research interests

My chief interest is in receptors for neuropeptides, especially those for calcitonin gene-related peptide (CGRP) and adrenomedullin. CGRP is a very abundant 37 amino acid peptide with many actions ranging from vasodilation to inhibition of some of the effects of insulin on metabolism. Adrenomedullin is a related peptide; it plays a very important role in the cardiovascular system. Drugs developed from CGRP and adrenomedullin may be of benefit in a variety of conditions such as migraine, heart disease and arthritis.

Both CGRP and adrenomedullin produce their effects at G-protein coupled receptors (GPCRs). Something like 70% of all drugs act at GPCRs; thus this family is of particular interest in drug discovery. However, the receptors for CGRP and adrenomedullin are of especial interest as they are made up of two subunits; a most unusual arrangement for GPCRs. They share a common subunit called calcitonin receptor-like receptor (CRLR or CL). This has the structure of a typical GPCR with seven transmembrane helices. However, to respond to CGRP a second protein is required, called receptor activity modifying protein 1 (RAMP1). When CL complexes with the related proteins RAMP2 or RAMP3, adrenomedullin receptors are formed.

In my laboratory we are interested in the molecular and pharmacological characterisation of CGRP and adrenomedullin receptors. Thus we wish to discover how CGRP and adrenomedullin bind to their receptors, how the receptors then activate the cells, how drugs discriminate between these receptors and what other receptors CGRP and adrenomedullin can activate besides CL/RAMP complexes.

We use a variety of techniques involving mutating receptors and expressing these in cell lines to measure binding and activation. We also look at endogenous receptors in cells and tissues. We collaborate with colleagues at Birmingham University, Auckland University and other institutes to further these studies.

Recent research funding

  • 2012-15 BBSRC The Use Of Novel Polymer-Lipid Nanoparticles To Study G-Protein-Coupled Receptor Activation And Dynamics (Co-applicant with Dr R.M. Bill and Dr T. Dafforn (Birmingham), PI Prof M. Wheatley (Birmingham). £ 303,302
    Further information on this project can be found here (courtesy of International Innovation*)  With additional details here.
  • 2011-13 The Wellcome Trust. The interaction of RAMPs with GCPRs; understanding structure-function relationships.            £209,825.00 (PI, co-applicants Dr R.M Bill and D.L. Rathbone

  • 2010 Wellcome Trust, SCAM to study the CGRP receptor, 088212/Z/09/Z, £56,054

  • 2008-9 AstraZeneca, The role of RAMPs, £70,000

Membership of professional bodies

Higher Education Academy, Biochemical Society, Britsh Pharmacological Society.

Selected publications

Full Papers

  • Extracellular loops 1 and 3 and their associated transmembrane regions of the calcitonin receptor-like receptor are needed for CGRP receptor function. Barwell J, Conner A, Poyner DR. Biochim Biophys Acta. 2011 Oct;1813(10):1906-16.

  • Structure-function analysis of amino acid 74 of human RAMP1 and RAMP3 and its role in peptide interactions with adrenomedullin and calcitonin gene-related peptide receptors. Qi T, Ly K, Poyner DR, Christopoulos G, Sexton PM, Hay DL. Peptides. 2011 May;32(5):1060-7.

  • Evidence that interaction between conserved residues in transmembrane helices 2, 3, and 7 are crucial for human VPAC1 receptor activation. Chugunov AO, Simms J, Poyner DR, Dehouck Y, Rooman M, Gilis D, Langer I. Mol Pharmacol. 2010 Sep;78(3):394-401.

  • Functional characterization of two human receptor activity-modifying protein 3 variants. Bailey RJ, Bradley JW, Poyner DR, Rathbone DL, Hay DL. Peptides. 2010 Apr;31(4):579-84.

  • Structure-function analysis of RAMP1-RAMP3 chimeras. Qi T, Simms J, Bailey RJ, Wheatley M, Rathbone DL, Hay DL, Poyner DR. Biochemistry. 2010 Jan 26;49(3):522-31.

  • Non-peptidic antagonists of the CGRP receptor, BIBN4096BS and MK-0974, interact with the calcitonin receptor-like receptor via methionine-42 and RAMP1 via tryptophan-74. Miller PS, Barwell J, Poyner DR, Wigglesworth MJ, Garland SL, Donnelly D. Biochem Biophys Res Commun. 2010 Jan 1;391(1):437-42.

  • Mapping interaction sites within the N-terminus of the calcitonin gene-related peptide receptor; the role of residues 23-60 of the calcitonin receptor-like receptor. Barwell J, Miller PS, Donnelly D, Poyner DR. Peptides. 2010 Jan;31(1):170-6. Epub 2009 Nov 11.

  • Novel peptide antagonists of adrenomedullin and calcitonin gene-related peptide receptors: identification, pharmacological characterization, and interactions with position 74 in receptor activity-modifying protein 1/3. Robinson SD, Aitken JF, Bailey RJ, Poyner DR, Hay DL. J Pharmacol Exp Ther. 2009 Nov;331(2):513-21. Epub 2009 Jul 30. Erratum in: J Pharmacol Exp Ther. 2011 Oct;339(1):321.

  • Altering the ribosomal subunit ratio in yeast maximizes recombinant protein yield. Bonander N, Darby RA, Grgic L, Bora N, Wen J, Brogna S, Poyner DR, O'Neill MA, Bill RM. Microb Cell Fact. 2009 Jan 29;8:10.

  • Structure-function analysis of RAMP1 by alanine mutagenesis. Simms J, Hay DL, Bailey RJ, Konycheva G, Bailey G, Wheatley M, Poyner DR. Biochemistry. 2009 Jan 13;48(1):198-205.

  • Functional and biophysical analysis of the C-terminus of the CGRP-receptor; a family B GPCR. Conner M, Hicks MR, Dafforn T, Knowles TJ, Ludwig C, Staddon S, Overduin M, Günther UL, Thome J, Wheatley M, Poyner DR, Conner AC. Biochemistry. 2008 Aug 12;47(32):8434-44.


  • Lifting The Lid On G-Protein-Coupled Receptors: The Role Of Extracellular Loops. Wheatley M, Wootten D, Conner M, Simms J, Kendrick R, Logan R, Poyner D, Barwell J. Br J Pharmacol. 2011 Aug 22. doi: 10.1111/j.1476-5381.2011.01629.x.

  • The pharmacology of Adrenomedullin 2/Intermedin. Hong Y, Hay DL, Quirion R, Poyner DR. Br J Pharmacol. 2011 Jun 9. doi: 10.1111/j.1476-5381.2011.01530.x.

  • Calcitonin and calcitonin receptor-like receptors: common themes with family B GPCRs? Barwell J, Gingell JJ, Watkins HA, Archbold JK, Poyner DR, Hay DL. Br J Pharmacol. 2011 Jun 7. doi: 10.1111/j.1476-5381.2011.01525.x.

  • Surfactant-free purification of membrane proteins with intact native membrane environment. Jamshad M, Lin YP, Knowles TJ, Parslow RA, Harris C, Wheatley M, Poyner DR, Bill RM, Thomas OR, Overduin M, Dafforn TR. Biochem Soc Trans. 2011 Jun;39(3):813-8. doi: 10.1042/BST0390813.

  • Adrenomedullin and calcitonin gene-related peptide receptors in endocrine-related cancers: opportunities and challenges. Hay DL, Walker CS, Poyner DR. Endocr Relat Cancer. 2010 Dec 13;18(1):C1-14. Print 2011 Feb.

  • Regulation of signal transduction by calcitonin gene-related peptide receptors. Walker CS, Conner AC, Poyner DR, Hay DL. Trends Pharmacol Sci. 2010 Oct;31(10):476-83. Epub 2010 Jul 13.

  • Calcitonin gene-related peptide, adrenomedullin and flushing. Hay DL, Poyner DR. Maturitas. 2009 Oct 20;64(2):104-8. Epub 2009 Sep 16. Review.

  • Modulating receptor function through RAMPs: can they represent drug targets in themselves? Sexton PM, Poyner DR, Simms J, Christopoulos A, Hay DL. Drug Discov Today. 2009 Apr;14(7-8):413-9. Epub 2009 Jan 16. Review.

  • Hay DL, Poyner DR, Quirion R; International Union of Pharmacology. International Union of Pharmacology. LXIX. Status of the calcitonin gene-related peptide subtype 2 receptor. Pharmacol Rev. 2008 Jun;60(2):143-5.


  • The use of site-directed mutagenesis to study GPCRs. Conner AC, Barwell J, Poyner DR, Wheatley M. Methods Mol Biol. 2011;746:85-98.

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