Associate Professor Evan Ingley heads the Cell Signalling group, which has an interest in understanding the signalling networks or "information highways" of both normal and diseased cells. Many of the new generation anti-cancer/leukaemia drugs disrupt these signalling networks and bring about a "normalization" of protein interactions. One of the underlying control principles of these processes is that of regulated protein-protein interactions. A/Prof Ingley's group focuses on an enzyme, Lyn, which modifies proteins and through this process mediates specific protein interactions that can enhance or hinder particular cellular processes including cell growth, shape, movement, differentiation and death.  

Evan's Honours degree at the University of Canterbury (New Zealand) included a research project on the hormonal control of genes important for cockroach reproduction, but developed an interest in understanding molecular interactions involved in cancer/leukaemia. 

Evan completed his PhD at The Australian National University in the John Curtin School of Medical Research (Canberra) under the direction of Professor Ian Young, working on the interaction between the cytokine Interleukin-5 (IL-5) and its receptor.

For his postdoctoral studies he move to Switzerland working with Dr Brian Hemmings at the Friedrich Miescher Institute, the flagship research institute of the pharmaceutical company Novartis. Dr Hemmings had recently identified the new oncogene Akt/PKB and Evan worked on its regulation through protein-protein as well as protein-lipid interactions.

On returning to Australia Evan began working in the Laboratory for Cancer Medicine at WAIMR bringing his expertise on protein-protein interactions involved in signal transduction to the labs interest in red blood cell development and lineage determination. After the labs discovery of the importance of Lyn in erythropoiesis he began establishing a focus on the signalling pathways of this molecule and set up the Cell Signalling Group.

Currently his research group is analysing the biological and signalling consequences of mice expressing different mutations of Lyn, how the Lyn substrate Csk binding protein (Cbp) can be used to disrupt Lyn signals in cancer and leukaemia cells, and detailing two novel Lyn signalling pathways mediated by LACM and Liar, which regulate cell shape and nuclear/cytoplasmic shuttling, respectively. 

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