Robert Burgoyne - Curriculum vitae#

Born in 1953. B.Sc. Bacteriology, University of Birmingham, 1974. Ph.D. Microbiology, University of Birmingham, 1977. Previously worked in the Department of Biology, Open University and the MRC National Institute for Medical Research, Mill Hill, London. Joined the University of Liverpool as a Lecturer in 1983 and was promoted to a Personal Chair in 1990. Founding Director of the first Wellcome Trust 4-year PhD programme established in Liverpool in 1994. Served as Head of the School of Biomedical Sciences from 2004-2009. Current role is Academic Lead for Research and Knowledge Exchange for the Faculty of Health and Life Sciences.

Awarded the Drs. C. & F. Demuth Swiss Medical Research Foundation's Annual International Award for Young Investigators in the Neurosciences in 1988. Elected member of the Academia Europaea in 2001. Elected Fellow of the Academy of Medical Sciences in 2002.

Current Research Interests

Analysis of the mechanisms underlying neurotransmission and neurodegeneration.

Stored neurotransmitters are released by the process of exocytosis in response to a calcium signal. Many of the proteins involved in the exocytotic machinery have been identified as part of a conserved family of proteins for membrane fusion. We have studied the functions of several of these proteins with an emphasis on the mammalian proteins Munc18-1 and cysteine string protein (Csp). Current work is focused on the use of the nematode worm Caenorhabditis elegans as a model in which to study the function of UNC-18 (the orthologue of Munc18-1) based on analysis of the effects of mutations in the protein in behavioural and other assays. In addition, we are exploring the role of synaptic proteins in the protection of neurons from age-related neurodegeneration in the worm model.

The functions of calcium sensor proteins

Many aspects of cell function are regulated by changes in cytosolic Ca2+ concentration through the actions of Ca2+-binding proteins. We are interested in the roles of a two families of Ca2+-binding proteins, the NCS proteins and the CaBPs. Using various approaches, we are investigating the physiological roles of NCS-1 and related family members including the KChIPs which regulate the traffic of Kv4 potassium channels. We are also interested in the cell biology of the ER Ca2+ sensor Stim1 in store-operated Ca2+ entry. Biochemical and structural approaches are being used to identify interacting proteins and the molecular basis by which they act. Localisation of the proteins is being characterised using fluorescent-tagged proteins in living cells. See NCS family web pages NCS protein family for further information.

Recent publications

Barclay, J. W., Graham, M. E., Edwards, M. R., Johnson, J. R., Morgan, A. and Burgoyne, R. D. (2010) Presynaptic targets for acute ethanol sensitivity. Biochem Soc Trans. 38, 172-176

Handley, M. T., Lian, L. Y., Haynes, L. P. and Burgoyne, R. D. (2010) Structural and functional deficits in a neuronal calcium sensor-1 mutant identified in a case of autistic spectrum disorder. PLoS One. 5, e10534

Johnson, J. R., Jenn, R. C., Barclay, J. W., Burgoyne, R. D. and Morgan, A. (2010) Caenorhabditis elegans: a useful tool to decipher neurodegenerative pathways. Biochem Soc Trans. 38, 559-563

McCue, H. V., Haynes, L. P. and Burgoyne, R. D. (2010) Bioinformatic analysis of CaBP/calneuron proteins reveals a family of highly conserved vertebrate Ca2+-binding proteins. BMC Res Notes. 3, 118

Walsh, C. M., Chvanov, M., Haynes, L. P., Petersen, O. H., Tepikin, A. V. and Burgoyne, R. D. (2010) Role of phosphoinositides in STIM1 dynamics and store-operated calcium entry. Biochem J. 425, 159-168