Cells regulate virtually all processes using the modification of proteins with the small protein ubiquitin. In addition, ubiquitin can be attached to itself in eight distinct ways. Moreover, a single ubiquitin can be modified with more than one ubiquitin, resulting in many branched chains. It is the ubiquitin chains that encode the information for the fate of the modified protein. We will decode the information stored in ubiquitin chains using a cellular biochemistry approach.
© Leo Kiss

We study which ubiquitin chains enable of the degradation of intracellular proteins ranging from single proteins to aggregates linked to neuro- degenerative diseases. We biochemically synthesize proteins that are modified with defined ubiquitin chains. Next, we deliver these proteins into cells and monitor their fate using our recently developed UbiREAD technology. Comparing the fates of proteins modified with different ubiquitin chains allows us to decode the ubiquitin chain.
© Leo Kiss

Projects in the lab will focus on establishing new technologies for studying the fate of ubiquitinated proteins, identifying intracellular interactomes of ubiquitinated proteins and biochemical reconstitution of complex protein degradation pathways.

We are building an international and interdisciplinary research team excited about all aspects of ubiquitin biology. We use the following techniques in the lab: molecular cloning, protein expression & purification, protein modifications using chemical biology, biochemical assays, cell culture, CRISPR genetics, flow cytometry, live cell imaging, microscopy, proteomics using mass spectrometry. Any new appraoch for decoding ubiquitin signals is welcomed in the lab!

To learn more about our work watch Leo’s Dana-Farber TPD Webinar on YouTube: