David Komander, of LMB’s Protein and Nucleic Acid Chemistry division, is a recipient of the 2012 Lister Prize. This prestigious award is given annually by The Lister Institute to three young researchers in the UK, to support quality research in the biomedical or related biological sciences.
The research in David’s group focuses on a versatile modification of proteins termed ubiquitination, which regulates all aspects of life. Ubiquitination has diverse consequences and regulates, amongst other things, degradation, localisation and activity of its substrates. This versatility is achieved by a variety of different ubiquitin polymers, only few of which are studied in detail. David’s lab aims to reveal cellular roles of unstudied ‘atypical’ ubiquitin polymers.
Protein ubiquitination is particularly important in infection and inflammatory signalling cascades. Interestingly, many pathogenic bacteria (including Salmonella, Yersinia, Escherichia and Legionella) modulate cellular ubiquitination cascades in a variety of ways, by injecting effector proteins into human cells. These effector proteins are exciting, as they are often structurally and mechanistically distinct from human enzymes.
The Lister prize will enable David to study bacterial effectors that will help to define roles of atypical ubiquitin chain types, and may become future drug targets for infectious diseases.