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).

CONFERENCE: Induced Proximity and Targeted Protein Degradation: Emerging Technologies and Therapeutic Applications

Feb 08–11, 2027 | Fairmont Banff Springs, Banff, AB, Canada
Deadlines:
o Scholarship ($1500): October 28, 2026
o Short Talk Abstract: October 28, 2026
o Early Registration: December 10, 2026
o Poster Abstract: January 19, 2027

Department News

Four new publications in one week!

October 18, 2026

Thielen et al. Molecular Cell: Solves a puzzle dating back to the 1950s by showing how an amino acid controls the stability of its metabolizing enzyme through a kinase and E3 ligase cascade.
Klose et al. Nature Structural & Molecular Biology: Two membrane machines with opposing jobs, one inserting membrane proteins and one pulling misplaced ones out, turn out to work as a single supercomplex.
Šepić et al. Nature Communications: A multi-purpose E3 ligase recognizes diverse degrons through a single substrate receptor.
Saco et al. Cancer Immunology Research: Collaborative work showing that the Cullin 5-RING E3 ligase limits the anti-tumor activity of T-cells.

Caro’s study is featured on the cover of Nature Structural & Molecular Biology!

October 13, 2026

This joint publication of the Schulman and Feige labs shows that the insertase ER Membrane protein Complex (EMC) and the dislocase Spf1, despite their oppposing functions, form a conserved supercomplex in the endoplasmic reticulum, poised to work together to ensure that membrane proteins are correctly embedded. Great collaboration with the Schuldiner (Weizmann Institute) and Fenech (University of Cologne) labs. Congratulations Caro and all the authors!

Image credit: Lucy Lambriex / Photodisc / Getty. Cover design: Allen Beattie

MoMaS at the EMBO Ubiquitin Workshop in Monopoli

September 28, 2026

Current and former members of the Schulman Department came together at the EMBO Workshop “Ubiquitin and ubiquitin-like proteins in health and disease” in Monopoli, Italy. Brenda gave a keynote lecture, introduced by former lab member Leo Kiss. Celine, Frank, Jakob, Juliane, Luca, and Sara presented posters, and Juliane won a Best Poster Prize. Congratulations Juliane! It was great to see former lab member Kirby Swatek and collaborator Cordula Enenkel there too.

Multimodal substrate recruitment enables CTLH-MKLN1 E3 ligase to target N-, C-, and internal degrons

September 16, 2026

Our new preprint reveals how a single E3 ligase receptor combinatorially uses its distinct domains to recognize a diverse repertoire of substrates. Congratulations to all the authors, especially to first author Sara!