firc institute of molecular oncology

Brenda Schulman

Brenda Schulman

Member, St. Jude Faculty
Investigator, Howard Hughes Medical Institute
Co-Director, Cancer Genetics, Biochemistry & Cell Biology Program of the St. Jude Cancer Center

Brenda Schulman works on the mechanisms underlying protein modification by the family of ubiquitin-related proteins (UBLs). Post-translational covalent attachment of ubiquitin-like proteins (UBLs) is a predominant eukaryotic regulatory mechanism. More than a dozen UBLs - such as ubiquitin, NEDD8, ISG15, and SUMO - covalently modify myriad substrates. Different UBLs alter the functions of their target proteins in different ways, such as by changing the target's half-life, conformation, subcellular localization, enzymatic activity, and/or intermolecular interactions. Defects in UBL pathways have been associated with numerous diseases, including cancers, neurodegenerative disorders, and viral infections. Thus, determining mechanisms by which enzymes transfer UBLs will be of broad importance toward understanding signaling pathways and their roles in diseases.

Educated at the Johns Hopkins University (BA 1989) and the Whitehead Institute/MIT (PhD 1996), Schulman held postdoctoral fellowships at MGH Cancer Center at Harvard Medical School and at Memorial Sloan-Kettering Cancer Center. She joined the faculty of the St. Jude Children's Research Hospital in 2001.

She was elected to the National Academy of Sciences in 2013 and the American Academy of Arts and Sciences in 2012. She was joint recipient of the Dorothy Crowfoot Hodgkin Award from the Protein Society in 2011, and was honored by a Presidential Early Career Award for Scientists and Engineers in 2004, a Beckman Young Investigator Award in 2004, and a Pew Scholar in Biomedical Sciences Award in 2002.

Schulman's article

April 2014

Illuminating a ubiquitin transfer relay, step-by-step

Commentary on Simona Polo's paper published on Nature Structural & Molecular Biology.