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Alex Bullock


Secreted growth hormones and cytokines regulate the key physiological processes of growth and differentiation as well as responses to injury and infection. They include some notable therapies such as growth hormone (GH), insulin and interferons. However, inappropriate growth signals can drive human cancer while excessive cytokine (interferon and interleukin) responses underlie autoimmune and inflammatory diseases such as rheumatoid arthritis, diabetes and asthma.

My group is interested in how these signals are regulated inside the cell by phosphorylation and uses the tools of structural biology. Classically, the receptor (RTK) and non-receptor (PTK) protein tyrosine kinases create docking sites for the recruitment of SH2 effector proteins (e.g. GRB2, STATs) regulated by the action of phosphatases (PTPs). Similarly, TGF-ß/BMP receptor serine kinases (RSK) recruit SMAD MH2 domains for the control of embryogenesis and stem cell development. More recently phosphorylation has been recognized as a control switch for protein degradation by E3 ubiquitin ligases.

As part of the structural genomics consortium (SGC) we are targeting the kinase receptors and their interaction with E3 ligases, with particular interest in their relevance for human disease. We recently solved several crystal structures of the TGF-ß/BMP receptor family which is under investigation in clinical trials for tumour angiogenesis, muscular dystrophy and multiple myeloma. Together with the group of Prof. Stefan Knapp we have also dentified anti-leukemic inhibitors of the PIM1 survival kinase that is known to be essential for v-Abl transformation. Recent work has focussed on the BTB-Kelch family of E3 ubiquitin ligases which are linked to the development of certain cancers, development and neurodegeneration.