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Dr Evan Ingley
Dr 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. Dr 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.
Qualifications
| 1987 | BSc (Hons, first class) - Zoology, University of Canterbury, New Zealand |
| 1992 | PhD - Biochemisty and Molecular Biology, The Australian National University, Australia Thesis Title: "Molecular and cellular biology of human interleukin-5 and its receptor" |
Research Interests
- The role of the tyrosine kinase Lyn in erythropoiesis.
- Delineating novel signalling pathways intersected by Lyn.
- Analysing Lyn pathways involved in leukaemia and cancer.
- Structure/function analysis of Lyn signalling complexes.
- Techniques: Yeast two-hybrid, molecular biology, cell biology, protein complexes, protein expression, protein posttranslational modifications.
Scientific Involvement
- Australian Society for Biochemistry and Molecular Biology - Member 1989 onwards.
- Australian Society for Medical Research - Member 1997 onwards, State Committee Member 2005 onwards, State Treasurer 2006 onwards.
- American Society of Hematology - Member 2005 onwards.
- American Society for Biochemistry and Molecular Biology - Member 2006 onwards.
Major Grants Awarded
- NHMRC Project Grants, #139008 (2001-2003), #303101 (2004-2006), #403987 (2006-2008)
- NHMRC Equipment Grant #467204 (2007)
- Cancer Foundation of WA (1997-1998)
- RPH MRF Project Grants (1997-1998, 2001-2002, 2005-2006, 2006-2007)
Top 10 Publications
- Maira S-M, Galetic I, Brazil DP, Kaech S, Ingley E, Thelen M, Hemmings BA. 2001. Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane. Science 294:374-80.
[NCBI PubMed Entry]
- Ingley E, McCarthy DJ, Pore, JR, Sarna MK, Adenan AS, Wright MJ, Erber W, Tilbrook PA, Klinken SP. 2005. Lyn deficiency reduces GATA-1, EKLF and STAT5, and induces extramedullary stress erythropoiesis. Oncogene 24:336-43.
[NCBI PubMed Entry]
- Ingley E, Schneider JR, McCarthy DJ, Harder KW, Hibbs ML, Klinken SP. 2006. Csk-binding protein mediates sequential enzymatic down-regulation and degradation of Lyn in erythropoietin-stimulated cells. Journal of Biological Chemistry 281:31920-9.
[NCBI PubMed Entry]
- Frech M, Andjelkovic M, Ingley E, Reddy KK, Falck JR, Hemmings BA. 1997. High affinity binding of inositol phosphates and phospholipids to the pleckstrin homology domain of RAC / protein kinase B and their influence on kinase activity. Journal of Biological Chemistry 272:8474-81.
[NCBI PubMed Entry]
- Tilbrook PA, Ingley E, Williams JH, Hibbs ML, Klinken SP. 1997. Lyn tyrosine kinase is essential for erythropoietin-induced differentiation of J2E erythroid cells. EMBO Journal 16:1610-9.
[NCBI PubMed Entry]
- Williams JH, Daly LN, Ingley E, Beumont JG, Tilbrook PA, Lalonde J-P, Stillitano JP, Klinken SP. 1999. HLS7, a hemopoietic lineage switch gene homologous to the leukemia-inducing gene MLF1. EMBO Journal 18:5559-66.
[NCBI PubMed Entry]
- Ingley E, Young IG. 1991. Characterization of a Receptor for Interleukin 5 on Human Eosinophils and the Myeloid Leukaemia Line HL-60. Blood 78:339-44.
[NCBI PubMed Entry]
- Sarna MK, Ingley E, Busfield SJ, Cull VS, Lepere W, McCarthy DJ, Wright MJ, Palmer GA, Chappell D, Sayer MJ, Alexander WS, Hilton DJ, Starr R, Watowich SS, Bittorf T, Klinken SP, Tilbrook PA. 2003. Differential regulation of SOCS genes in normal and transformed erythroid cells. Oncogene 22:3221-30.
[NCBI PubMed Entry]
- Ingley E, Chappel D, Poon SYK, Sarna MK, Beaumont JG, Williams JH, Stillitano JP, Tsai S, Tilbrook PA, Leedman PJ, Klinken SP. 2001. Thyroid hormone receptor-interacting protein 1 modulates cytokine and nuclear hormone signaling in erythroid cells. Journal of Biological Chemistry 276:43428-34.
[NCBI PubMed Entry]
- Ingley E, Klinken SP. 2006. Cross-regulation of JAK and Src kinases. Growth Factors 24:89-95.
[NCBI PubMed Entry]
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