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Dr Tracey Gloster

Dr Tracey Gloster

Understanding Unusual Forms of Protein Glycosylation
Decoding of the human genome revealed that humans possess a relatively small number of genes, yet we are complex beings. The apparent inconsistency between the number of genes and complexity can, in part, be accounted for by ‘post-translational modifications' of human proteins. These modifications are additional groups added onto specific positions in the protein that can change its activity or structure. I am interested in one such modification where a single sugar molecule, called mannose, is added onto the protein in a process called C-mannosylation. Very little is known about this modification and the function it plays inside cells. Other post-translational modifications involving addition of sugars onto proteins are vital in cell processes including signalling and development, and when the modification fails can result in diseases such as cancer and inflammation. Research into C-mannosylation is still in its infancy, but analogy to other sugar modifications suggests it too could play an important role. Being awarded the L'Oreal-UNESCO For Women in Science Fellowship will allow me to establish a project in my laboratory to investigate C-mannosylation. The first step, which I hope to achieve over the next year, will be to identify the enzyme, Nature's catalyst, responsible for adding mannose onto proteins.

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