Proceedings of the National Academy of Sciences of the United States of America

About the PNAS Member Editor
Name Schulman, Brenda A.
Location Max Planck Institute of Biochemistry
Primary Field Biochemistry
 Election Citation
Schulman discovered key components and critical features of structural mechanisms of ubiquitin-like (UBL) conjugation, including activation by E1 enzymes, ligation of NEDD8, and mechanisms that activate RING E3 ligase activity of the largest family of ubiquitin ligases. She also demonstrated how N-terminal acetylation of proteins can mediate protein interactions.
 Research Interests
I am fascinated by how protein functions are dynamically switched to drive regulatory pathways. In eukaryotes, a major form of regulation involves covalent protein modification by a diverse array of ubiquitin-like proteins (UBLs), which impart extraordinary changes in the fates of their targets. As examples, some polyubiquitin chains mediate proteasomal degradation, whereas ubiquitin?s closest relative, NEDD8, has the distinct function of activating hundreds of ubiquitinating enzymes. By contrast, Atg8 is ligated to a lipid, regulating numerous features of bulk degradation via autophagy. We are interested in how dedicated cascades of E1 activating, E2 conjugating, and E3 ligase enzymes direct these UBLs to their targets to regulate the cell cycle, autophagy, and other processes. Regulation depends on numerous E2 and E3 enzymes (roughly 30 and 600, respectively, in humans) coordinately matching particular UBLs and substrates in a highly specific manner. My lab has determined a series of crystal structures that serve as molecular "snapshots" revealing how UBLs are activated by E1 enzymes, transferred between E1s, E2s and different types of E3 enzymes to particular target proteins, and how UBL attachment can transform the functions of modified proteins. Our current research focuses on understanding how E3 ligases are regulated to ensure that targets are modified under the right circumstances to mediate proper regulation, how UBL modifications alter the functions of targets, and consequences of defects in UBL pathways associated with certain cancers and neurodegenerative disorders.

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