News from the Institute

An international team of scientists led by IBCII director Ivan Dikic developed specific Ubiquitin biosensors for in vivo application. This approach might mark a major technical breakthrough in detection of Ubiquitin signals in living cells. It is published in today's online issue of Molecular Cell.

The covalent attachment of the ubiquitin-like modifier SUMO to proteins serves an important mechanism for the control of protein-protein interactions. This is generally mediated via recognition of a SUMO-conjugate by an interaction partner that contains a specific SUMO interaction module, termed SIM (SUMO interaction motif). A major question is how the dynamics of SUMO/SIM interactions are regulated.

Cell shape and migration are controlled by RhoGTPases, a family of small GTPases whose activation is controlled by nucleotide binding.

Rac1 is an important member of this family and
studies from the Cell death Signalling group from IBCII has shed light into ubiquitin dependent inactivation of Rac1 signalling.

If you were granted one wish for the advancement of your research projects, what would this be?

Well, I've always valued and emphasized a creative atmosphere. It not only means being surrounded by intelligent people, but also having enough time
to think.

Not having countless administrative duties, committees, applying for funding, etc. Scientists need time to develop brilliant ideas that help address issues we normally would not have time to consider. So my wish would be that we scientists do not have to waste too much valuable time on administrative issues, but can dedicate ourselves to conducting research.

The ERC approved funding for his proposal on Xenophagy and bacterial avoidance (XABA). Briefly, microbial pathogens that successfully parasitize eukaryotic cells have evolved to evade autophagic microbial defenses (xenophagy) and subvert the host autophagic responses for their own survival and/or growth.

Central to xenophagy is cargo recognition and dynamic rearrangements of membrane-bound compartments to sequester and deliver pathogen load for lysosomal degradation.