FAT10 is a small protein with a huge effect. Its attachment to a target protein is a signal for
its degradation. FAT10 is a marking system for degradation that seems to be inefficient. In
contrast to its biological competitor, ubiquitin, which is recycled, FAT10 is degraded along
with its target protein which appears wasteful at first glance.
So, why does this seemingly inefficient FAT10-system exist at all? Professor Marcus Groettrup,
head of the immunology working group at the University of Konstanz, and his team have been
carrying out research on FAT10 for many years. Now they achieved a break-through that made it
possible to determine the high-resolution structure of FAT10. This success was enabled through
another achievement. In collaboration with Dr Annette Aichem from the Biotechnology Institute
Thurgau (BITg), Konstanz chemist Professor Christine Peter and structural biologist Dr Silke
Wiesner from the University of Regensburg, the team developed a molecular technique to produce
stable and highly-concentrated FAT10 with a high degree of purity. As a consequence, the
researchers could carry out a structure analysis of FAT10 via x-ray crystallography and magnetic
resonance spectroscopy. The results have been published in the current issue of Nature
Communications. Read more...