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

Decades old mystery now solved: A CK2-FBXW11 kinase-E3 ubiquitin ligase cascade is a metabolic sensor regulating Tryptophan 2,3-dioxygenase stability!

Decades old mystery now solved: A CK2-FBXW11 kinase-E3 ubiquitin ligase cascade is a metabolic sensor regulating Tryptophan 2,3-dioxygenase stability!

January 13, 2026
Our new preprint shows how tryptophan binding to an exosite on TDO2 regulates a phosphorylation‑dependent ubiquitin–E3 ligase cascade, providing a metabolite‑gated mechanism that links tryptophan levels to TDO2 degradation. Congratulations to all the authors, especially Alina!
New Preprint: The E3 ubiquitin ligase mechanism specifying target-directed microRNA degradation

New Preprint: The E3 ubiquitin ligase mechanism specifying target-directed microRNA degradation

January 05, 2026
This collaborative work with Bartel Lab established a two-RNA-factor authentication mechanism for E3 ligase substrate recognition, diverging from conventional degron-based recognition. Congratulations to all the authors, especially the co-first authors Jakob and Elena!
1st publication of the year!

1st publication of the year!

January 02, 2026
Great collaboration with Sidhu Lab! We are reporting in PNAS on a generalizable approach for engineering E2 enzymes to enhance their selectivity and affinity toward particular E3 ubiquitin ligases to probe their activities. Congratulations to all the other authors, especially the first author Jiale!  more
Best Talk and Poster Awards to Luca and Hannah!

Best Talk and Poster Awards to Luca and Hannah!

December 04, 2025
At the IMPRS-ML Winter Seminar 2025, Luca’s talk and Hannah’s poster were awarded the best in their categories. Congratulations!

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