Unconventional ubiquitin code in infection and inflammation

Ubiquitination of proteins regulates a number of key cellular processes including protein degradation, endocytosis, translation, innate immunity and DNA repair. The major progress has been accomplished in linking diverse Ubiquitin modifications (Ub code) with specific cellular functions. These include conventional (lysine-linked) and unconventional ubiquitin modifications – from ester linkages to hydroxyls on proteins, lipids, sugars, to linkage via a ubiquitin serine residue in phosphoribosyl-linked (PR) ubiquitination mediated by effector proteins of pathogenic Legionella pneumophila. Molecular insights into this novel chemistry of ubiquitination that can modulate host-pathogen interactions, inflammation and immune responses during bacterial infection will be discussed.

Ivan Đikić is a leading expert in the fields of ubiquitin biology and autophagy research. He is Professor and Director of the Institute of Biochemistry II at Goethe University Frankfurt and a fellow of Max Planck Society. He investigates molecular principles of life and their pathological alterations that lead to the development of human diseases such as cancer, neurodegeneration and infection. For his scientific work he received numerous awards, including the Louis-Jeantet Prize, Jung Prize for Medicine and the Leibniz Prize.

Moderation: Professorin Dr. Elke Krüger

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