Professor Dr Brenda A. Schulman

Research priorities: Biochemistry, structural biology, post-translational modifications, ubiquitin, protein degradation, cell cycle, autophagy 
Brenda A. Schulman is a biochemist, structural biologist, and cell biologist. Her lab elucidates fundamental principles underlying cellular regulation by small proteins known as ubiquitin and ubiquitin-like proteins. Because this regulation is associated with numerous diseases - including cancers, neurodegenerative disorders, and viral infections - Schulman’s research enables deciphering physiologically important signaling pathways and their roles in diseases. 
Brenda Schulman elucidates biochemical pathways and structural mechanisms underlying how protein functions are dynamically switched to drive crucial biological regulatory pathways. In eukaryotes, a major form of regulation involves covalent protein modification by a diverse array of ubiquitin (UB) and ubiquitin-like proteins (UBLs). This is mediated by cascades of enzymes in classes known as E1, E2 and E3. It is estimated that the human genome encodes 500-1000 E1, E2, and E3 enzymes, rivaling the numbers of kinases. The vast numbers of these enzymes underscores their widespread roles in regulation. The foundation of Schulman’s work is a persistent drive to visualize dynamic protein complexes in their functional forms. 
The Schulman lab biochemically reconstitutes intricate regulation, devises new chemical or protein-design methods for trapping transient massive multiprotein assemblies in conformations representing fleeting ubiquitylation reaction intermediates, and in conjunction with structural techniques and genetics, defines the structural mechanisms underlying UB and UBL conjugation. 
Schulman’s group determined numerous structures (originally by X-ray crystallography, but more recently by cryo electron microscopy) that defined fundamental principles by which major classes of E1, E2 and E3 enzymes transfer UB and UBLs to specific targets. Schulman has also identified several previously unrecognized cellular pathways regulating ubiquitylation.