News from the Institute

Ubiquitin molecules can be attached to each other to build longer chains with unique 3D structures mediating diverse functions. About a decade ago, linear ubiquitin chains, in which the head of one ubiquitin is linked to the tail of another, were identified as a new chain type involved in inflammatory signalling.

However, target proteins of linear ubiquitination and their specific functions have largely remained elusive. A novel technology developed by an international team around IBC2 group leader Koraljka Husnjak now enables the systematic analysis of linear ubiquitination targets. Details are published in today’s online issue of Nature Methods.

Christian Münch, group leader at the IBC2, contributed to a study recently published in Nature. The work was led by Dipanjan Chowdhury at the Dana-Farber/Harvard Cancer Center and described the role of an uncharacterized protein – TIRR – in regulating DNA double-strand repair. TIRR binds to the tandem Tudor domain of 53BP1, a protein important for DNA double-strand repair, masking the histone methyl-lysine binding motif on 53BP1 and preventing chromatin binding. Also, TIRR stabilizes the nuclear-soluble 53BP1 fraction through direct binding. Through these mechanisms, TIRR affects 53BP1 activity and DNA double-strand repair efficiency.

The award ceremony for the 2016 Competition on International Research Marketing Ideas by the German Research Foundation (DFG) took place on 16th Feb 2017 in Potsdam. Besides Goethe University (GU) three other institutions were honored, and the prize was handed over by DFG’s Vice President Prof. Roland A. Fischer in a lively ceremony comprising interviews with all awardees.

Evgenij Fiskin has been selected to receive the 2017 Bayer HealthCare Prize to honor his outstanding PhD thesis, which he completed in the Dikic lab at IBC2. The award is donated by Bayer Pharmaceuticals and bestowed by the German Society for Biochemistry and Molecular Biology (GBM) at the Mosbacher Kolloquium (www.mosbacher-kolloquium.org/).

Autophagy is a cellular recycling and quality control pathway that is essential for maintaining cellular metabolism and homeostasis. Its malfunction contributes e.g. to neurodegenerative diseases and cancer.

Ubiquitin-like ATG8 proteins constitute central components of the autophagic machinery. However, until today, it is not completely clear why yeast harbors only one ATG8 protein while human cells contain six mammalian ATG8 orthologs, classified into the LC3 and GABARAP subfamilies.