Several strategies currently exist to address all possible associations between proteins, not only on the single protein but also on a proteome-wide level. These strategies can be divided in the binary approaches which rely on the expression of both bait and prey to perform a test for the interaction, and the co-complex methods, wherein the protein complex is purified from a lysate. The result of this work is a physical interaction map of all possible associations between proteins, also referred to as the interactome. Popular methods include the yeast two-hybrid system and the MAPPIT platform for the binary approaches, and Affinity Purification coupled to Mass Spectrometry (AP-MS) as an example of an MS-based method. Although these contributions are clearly essential to grasp the inherent complexity of protein complex biology, the underlying technologies are not perfect, and are typically deployed in generic cell systems. Moreover, the functional implications of these associations remain hidden in the complex networks which are typically generated in high throughput studies.

The team develops new technologies with a focus on the analysis of protein complexes (see also www.virotrap.be), but our efforts are recently also shifting towards a systems-level understanding of cellular organization by the integration of different data types such as high-resolution microscopy or perturbance analysis. The ultimate goal of our research is a single-cell map of quantified protein complexes in their subcellular context. Such maps will guide high precision therapeutic development in diverse pathologies.  Our approaches are typically implemented in close collaboration with research groups in our Center and well beyond to tackle challenging questions in human biology or disease.