Professor Dr Roger S. Goody

Research Priorities: Cell metabolism, structural, kinetic, and thermodynamic analysis of intercellular interactions, Rab/Ras protein families, post-translational modification of lipid molecules
Roger Sidney Goody is a British biochemist who specialises in cell metabolism in eukaryotic cells. His primary focus is on the intercellular transport of proteins and lipids, its physiological process, and possible pathological disruptions. The Rab protein family, which coordinates essential cell processes, is central to his research. Roger Goody studies disrupted transport processes linked to the hereditary eye disease choroideremia as well as tumour diseases resulting from a mutation of a related protein family.
Higher organisms have developed special reaction spaces, known as organelles, to coordinate complex metabolic processes in cells. Intensive transport of proteins and lipids between organelles takes places in vesicles. For a long time it was unclear how this transport was regulated. Goody and his team managed to obtain important insights using physical and chemical procedures such as x-ray crystal analysis and fluorescence microscopy. They were able to elucidate the structure and function of several molecules which play a key role in the logistics of healthy cells and which, if defective, can lead to cancer, blindness, or intellectual disability.
Rab proteins, a subgroup of Ras proteins, regulate the transport and fusing of vesicles with different organelles. To fulfil this function, Rab proteins have to be equipped with a lipid tag which allows them to bind to membranes. The importance of this binding can be seen, for example, with respect to choroideremia, which Roger Goody has been studying for years. This disease results from a Rab protein defect and leads to progressive degeneration of the retina. To date, it was assumed that gene therapy would be the only way to transfer a properly functioning Rab protein into the cells. However, Goody has shown that there may be an alternative option. Using novel methods, he and his colleagues succeeded in recording the interaction of the proteins involved and developed a way to increase the activity of a related protein and thus at least partially compensate for the defect.
Mutations in Ras proteins are also involved in 25 percent of all tumour diseases, including in especially aggressive forms such as lung, pancreatic, and bowel cancer. KRas is the most frequently mutated isoform. Despite intensive research since the discovery of the Ras oncogenes in 1981, therapeutic experiments have yielded little success so far. Currently, the selective focus on certain KRas mutations is giving cause for hope. This basic research made it possible to develop small molecules with specificity for disease-related Ras mutations. These mutations form covalent bonds with membranes and could potentially be targeted with drugs. Goody has developed methods to enable nucleotides to covalently bond to proteins. The aim is to first and foremost use these nucleotide derivatives as tools for biochemical and cell-biological research, while they might also form the basis of potential drug treatments.
Roger Goody combines chemistry, structural biology, and kinetics to make key contributions to various fields of biology. He has pioneered the use of nucleotide analogues, synthesised at the beginning of his career, in muscle research and later for Ras proteins. His fundamental, groundbreaking research has helped us better understand transport mechanisms and the role of proteins in these processes.