Brenda Schulman

Brenda Schulman

Research Department Molecular Machines and Signaling (MoMaS)

Structural Biology, Ubiquitin Proteasome System, Ubiquitin-like Protein

An important form of regulation is the modification of proteins and membranes by linking them to the small protein ubiquitin or structurally related ubiquitin-like proteins (UBLs). Ubiquitin and UBLs control timing, subcellular location, composition, conformation and activity of thousands of different proteins and macromolecules. In addition, defects in ubiquitin and UBL pathways are associated with numerous diseases such as cancer, neurodegenerative disorders and viral infections. Brenda Schulman's Department “Molecular Machines and Signaling” has shown that hundreds of microscopic, dynamic, multiprotein molecular machines are transiently transformed into different conformations by specialized regulatory factors to control ubiquitin and UBLs in order to regulate virtually all aspects of cell biology.

 

Research Overview
A widespread mechanism regulating the functions of eukaryotic proteins involves post-translational modification by the small protein ubiquitin (UB) or structurally related ubiquitin-like proteins (UBLs). more

 

Department News

48th FEBS Congress, Milano, Italy
Brenda gave a talk titled “Signaling through the ubiquitin-proteasome system” as invited speaker at the 48th FEBS Congress. more
2024 Vallee Summer Symposium, Stresa, Italy
Brenda (Vallee Visiting Professor) and Lukas (poster) attended this invitation only event which brings together a multidisciplinary team of Vallee Visitng Professors, Vallee Scholars, a guest scientist and ~10 nominated early career researchers. more
Alkylamine-tethered molecules recruit FBXO22 for targeted protein degradation
New Publication - Great collaborative work! Congratulations to MoMaS member Jakob and alumna Asia, and all the other authors. more
Dawa is an Otto Hahn Medal Honoree
MoMaS Alumna Dawafuti Sherpa is awarded the prestigious Otto Hahn Medal of the Max Planck Society for establishing a new paradigm for substrate targeting by E3 ubiquitin ligases and ubiquitin dependent regulation of metabolism more

more...

Go to Editor View