Dr Christoph Goebl

Research interests

Our team is interested in the molecular details of oxidation events. We study structures and interactions of proteins and aim to understand the molecular oxidation events.

We recently discovered that the tumour suppressor protein p16 can reversibly change into amyloid structures simply by creation of breaking of a single disulfide bond (Heath, S.G., et al. Nat Commun 2024 15, 5535, 2024). We currently are investigating the amyloid formation mechanism using recombinant protein and biophysical methods such as fluorescence assays. In parallel, we are studying the p16 state and its functional consequences in different human and zebrafish models, cancer cell lines and in human tumours.

We are further interested in the ligand-activated transcription factor Aryl hydrocarbon Receptor (AhR). This protein senses small molecules while in complex with heat-shock protein 90 (HSP90) and AhR-interacting protein (AIP). Upon activation, AhR migrates from the cytosol into the nucleus and is capable of activating a large number of different genes. We recently described the function of AhR in cancer cells (Kubli et al., PNAS 2019, 2019 116 (9) 3604-3613) and we are currently investigating the molecular mechanism of small molecule binding impacted by oxidation events.

We are collaborating with laboratories all over the world including Dr Nico Tjandra (National Institutes of Health, MD, USA), Professor Borries Demeler (University of Lethbridge, AL, Canada), Professor Bernd Reif (Technical University of Munich, Germany), Professor Alexander Buell (Technical University of Denmark), Associate Professor Chiara Gorrini (University of Leeds, UK) and Professor Margaret Sunde (University of Sydney, Australia). Our work is currently supported by Health Research Council grants and Marsden project grants.

We are always seeking highly motivated students that are open to potential research trips to our collaborators, please contact us if you are interested.