Dr Patrick Eyers
YCR Institute for Cancer Studies
Molecular Biology & Biotechnology
Institute for Cancer Studies
Department of Oncology
The Medical School
Beech Hill Road
Telephone: +44 (0)114 271 1295/3774
Facsimilie: +44 (0)114 271 1602
University of Bristol BSc (Hons) Biochemistry with Industrial Experience
University of Dundee PhD Biochemistry
University of Colorado, HHMI and Dept. Pharmacology
University of Manchester, Faculty of Life Sciences
Positions and Employment
Postdoctoral Research Associate, HHMI, University of Colorado
Postdoctoral Research Associate, Faculty of Life Sciences, University of Manchester
MRC Career Development Fellow and Honorary Lecturer, University of Manchester
Lecturer, Institute for Cancer Studies, University of Sheffield
Senior Lecturer, Institute for Cancer Studies, University of Sheffield
Our primary research goal is to understand the regulation and function of therapeutically important protein kinases. We are particularly interested in how cell cycle-regulated protein kinases are controlled through phosphorylation-dependent signalling pathways, and how the largely unexplored "pseudokinase" subfamily regulate the eukaryotic cell cycle.
Our major research themes are:
• Regulation of the eukaryotic cell cycle by protein kinases and protein phosphatases
• The mechanism of mitotic protein kinase activation by regulatory subunits
• Structural and chemical biology to elucidate protein kinase function and small molecule design (see Figure 1)
• Translational research: protein kinase inhibitors as therapeutic agents in proliferative disorders
See the Cancer Studies web page for more details.
Hegarat N, Smith E, Nayak G, Takeda S, Eyers PA and Hochegger H
Aurora A and Aurora B jointly coordinate chromosome segregation.
The Journal of Cell Biology (2011) 195:1103-13.
Mant A, Elliott D, Eyers PA and O’Kelly IM
Phosphorylation by Protein Kinase A (PKA) enables forward transport of K2P3.1 and K2P9.1, two pore domain potassium channels.
The Journal of Biological Chemistry (2011) 286:14110-14119.
Girdler F, Gascoigne KE, Eyers PA, Hartmuth S, Crafter C, Foote KM, Keen NJ and Taylor SS.
Validating Aurora B as an anti-cancer drug target
Journal of Cell Science (2006) 119: 3664-3675.
Tyler RK, Shpiro N, Marquez R and Eyers PA.
VX-680 inhibits Aurora A and Aurora B kinase activity in human cells
Cell Cycle (2007) 6: 2846-2854.
Eckerdt F, Eyers PA Lewellyn A, Prigent C and Maller JL.
Spindle Pole Regulation by a Discrete Eg5-interacting domain in TPX2
Current Biology (2008) 18: 519-525.
Chu MLH, Chavas LMG, Douglas KT Eyers PA and Tabernero L.
Crystal structure of the catalytic domain of the mitotic checkpoint kinase Mps1 in complex with SP600125
Journal of Biological Chemistry (2008) 283: 21495-21500.
Tyler RK, Chu MLH, Johnson H, McKenzie EA, Gaskell SJ and Eyers PA
Phosphoregulation of human Mps1 kinase
Biochemical Journal (2009) 417: 173-181.
Scutt PJ, Chu, MLH, Sloane DA, Cherry M, Bignell CR, Williams DH and Eyers PA.
Discovery and exploitation of inhibitor-resistant Aurora and Polo kinase mutants for the analysis of mitotic networks
Journal of Biological Chemistry (2009) 284: 15880-15893
Johnson H, Eyers CE, Eyers PA, Benyon RJ and Gaskell SJ.
Rigorous determination of the stoichiometry of protein phosphorylation using mass spectrometry
Journal of the American Society for Mass Spectrometry (2009) 20: 2211-2220
Chu MLH, Lang Z, Chavas LMG, Neres J, Federova OS, Tabernero L, Cherry M, Williams DH, Douglas KT and Eyers PA.
Biophysical and X-ray crystallographic analysis of Mps1 kinase inhibitor complexes.
Biochemistry (2010) 49: 1689-1701
Chu MLH and Eyers PA.
UCSD/Nature Signaling Gateway, Molecule Pages: Mps1
Sloane DA Trikic MZ, Lang Z, Chu MLH, Lamers MBAC, Mason CS, Mueller I, Savory WJ, Williams DH and Eyers PA.
Drug-Resistant Aurora A Mutants for Cellular Target Validation of the Small Molecule Kinase Inhibitors MLN8054 and MLN8237
ACS Chem. Biol. (2010) 5: 563-576.
To hear a podcast describing aspects of this work please click here
Enquiries from prospective PhD and postdoctoral researchers are welcome at any time.