Institute for Biophysics and Physical Biochemistry, University of Regensburg, Germany
1992 – 1998 Undergraduate studies in Biochemistry at the Free University of Berlin, Germany
1998 Diploma Thesis with Prof. Bertil Halle at Lund University, Sweden
1998 – 2003 Graduate student with Prof. Michael Sattler at EMBL Heidelberg, Germany
2003 – 2008 Postdoctoral fellow with Prof. Julie Forman-Kay at the Hospital for Sick Children, University of Toronto, Canada
2008 – 2017 Group Leader at the Max Planck Institute for Developmental Biology, Tübingen, Germany
Since 2017 Group Leader / Lecturer at the University of Regensburg, Germany
Enzyme activity is inherently linked to protein motions. Yet, how conformational dynamics correlates with enzyme activity is poorly understood. HECT-type ubiquitin ligases (E3s) covalently attach ubiquitin to substrates and thereby regulate the localization and abundance of proteins in the cell. Inhibition of HECT E3s prevents untimely ubiquitination and is essential for cellular homeostasis. In line with this, deregulation of HECT activity is closely associated with diseases such as cancer. I will discuss mechanisms that we have uncovered using NMR spectroscopy, x-ray crystallography and biochemical assays that underlie the down-regulation and activation of HECT-type ligases. I will delineate mechanistic commonalities and differences among distinct classes of HECT ligases and focus on the conformational dynamics that are essential for HECT activity.
Host: Mikael Borg
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