Modification of proteins by so-called post-translational modifications (PTMs) can change the activity and/or localisation of cellular proteins and often generates an important signal in a cell. Van der Heden van Noort and his team study two of these PTMs; ubiquitylation and ADPribosylation. It turns out these systems are not fully independent and on occasion also 'communicate' with each other, for instance during bacterial infections of humans (by the Legionella bacterium causing Legionnaires disease), but also during DNA damage responses or cancer progression. How these very different processes, that do share a common ground, function in detail is largely unknown and the researchers in the Department of Cell and Chemical Biology aim to explain the molecular basis of enzymes installing and removing these modifications, explore the cell biology pathways affected by them and exploit this knowledge to prepare new small molecule inhibitors that can be applied as research tools and that in a later stage might form the basis of novel medication.
A press release in Dutch can be found here.