Joe Lynch completed a BSc majoring in Physics at the University of Melbourne. He then moved to the University of NSW to undertake a Masters of Biomedical Engineering and then a Ph.D. in Physiology with Peter Barry. His postdoctoral studies were undertaken in Germany, France and at the Garvan Institute of Medical Research in Sydney. He moved to University of QLD in 1996 as a Senior Lecturer in the School of Biomedical Sciences. He relocated to the QBI in October 2007 and was promoted to Professor in 2008. He is currently supported by an NHMRC Principal Research Fellowship (2014-2018).
The major research interest in the laboratory concerns the molecular structure and function of the structurally-related glycine and GABAA receptor chloride channels that mediate inhibitory neurotransmission in the central nervous system. The GABAA receptor is an important target for neuroactive drugs and the glycine receptor has recently emerged as a drug target for inflammatory pain. We try to understand the mechanisms by which these receptors open and close, their structure and their molecular pharmacology. His laboratory is also interested in identifying novel compounds active at these receptors as leads for therapeutic development and as pharmacological tools for basic research. A more complete description of our current research interests is given here. Experimental approaches include molecular biology, protein chemistry, manual and automated patch-clamp electrophysiology, fluorescence imaging, automated high throughput fluorescence-based screening, voltage-clamp fluorescence.
- Brett Cromer - RMIT University
- Pankaj Sah - The University of QLD
- Rob Capon - The University of QLD
- Mark Rees and Seo-kyung Chung - University of Swansea
- Daniel Gilbert - University of Erlangen
- Robert Harvey - London School of Pharmacy
- Chris Ulens - KU Leuven
- Andrew Jenkins - Emory University
- Lynch, J.W. 2004. Molecular structure and function of the glycine receptor chloride channel. Physiol. Rev. 84: 1050-1095.
- Lynch, J.W. 2009. Native glycine receptor subtypes and their physiological roles. Neuropharmacol. 56: 303-309.
- Lynagh, T., and J.W. Lynch. 2012. Ivermectin binding sites in human and invertebrate Cys-loop receptors. Trends Pharmacol. Sci. 33: 432-441.
- Yang, Z., E. Taran, T.I. Webb, and J.W. Lynch. 2012. Stoichiometry and subunit arrangement of glycine receptors as determined by atomic force microscopy. Biochemistry 51: 5229-5231.
- Chung, S.K., A. Bode, T.D. Cushion, C. Hunt, S.-E. Wood, O.W. Pickrell, C.J.G. Drew, S. Yamashita, R. Shiang, S. Leitz, A.C. Longhardt, V. Raile, B. Weschke, R.D. Puri, I.C. Verma, D.D. Ratnasinghe, R.J. Harvey, M. Parker, C. Rittey, A. Masri, L. Lingappa, O.W. Howells, J.F. Vanbellinghen, R.H. Thomas, J.G. Mullins, J.W. Lynch, and M.I. Rees. 2013. GLRB is the third major gene-of-effect in hyperekplexia. Hum. Mol. Genet. 22: 927-940.
- James, V.M., A. Bode, J.L. Gill, M. Nielsen, F.M. Cowan, M. Vujic, R.H. Thomas, M.I. Rees, K. Harvey, A. Keramidas, M. Topf, I. Ginjaar, J.W. Lynch, and R.J. Harvey. 2013. Novel missense mutations in the glycine receptor β subunit gene (GLRB) in startle disease. Neurobiol. Dis. 52: 137-149.
- Han, L., S. Talwar, and J.W. Lynch. 2013. The relative orientation of the TM3 and TM4 domains varies between α1 and α3 glycine receptors. ACS Chem. Neurosci. 4: 248-254.
- Keramidas, A., and J.W. Lynch. 2013. An outline of desensitization in Cys-loop ion channel receptors. Cell. Mol. Life Sci. 70: 1241-1253.