Rachel Klevit is a structural biochemist recognized for her insights into critical questions in structural biology. Her research has made seminal contributions to understanding the mechanism of disease in breast cancer and Parkinson’s disease. Klevit grew up in Portland, Oregon and spent her early years training to become a ballet dancer. After graduating from high school, she danced with several professional and semi-professional dance companies prior to attending Reed College where she received a B.A. in Chemistry in 1978. As the first female Rhodes Scholar from Oregon, Klevit received her D. Phil. in Chemistry at Oxford University. She spent two years as a post-doctoral fellow at Duke University before moving to University of Washington as an American Cancer Society Fellow. She joined the Department of Biochemistry, University of Washington School of Medicine in 1986 and currently holds the Edmond H. Fischer/WRF Endowed Chair in Biochemistry and adjunct positions as Professor of Pharmacology and Chemistry. Her scientific contributions have been recognized by numerous awards, including Dupont Young Investigator Award, Fritz Lippmann Award, and Dorothy Crowfoot Hodgkins Award. Klevit is a Fellow of AAAS, a member of the Washington Academy of Science, and a member of the National Academy of Science.

Research Interests

An overarching theme of the Klevit lab is to understand guardians of the cell. We focus on two broad topics: guardians of the genome and guardians of the proteome. In the former category, we study mechanisms and the functional ramifications of modification of cellular proteins with ubiquitin. A long-standing interest is the breast cancer susceptibility protein, BRCA1, and its 'sister gene,' BARD1 which together place unique ubiquitin marks on nucleosomal histones that are involved in the DNA damage response, transcriptional regulation, and maintenance of epigenetic marks. In the second category, the small heat shock proteins play key roles both in cellular housekeeping and as a cell's first responders in times of stress. These enigmatic protein chaperones are involved in a growing number of human diseases and syndromes, especially neurodegenerative disease, cardiomyopathies, and cataract, but their mechanism of action remains virtually entirely undefined. In the broader area of structural and biophysical biology, we are fascinated by new ways to think about and investigate intrinsic disorder and its role in functional molecular recognition.

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Primary Section

Section 21: Biochemistry

Secondary Section

Section 29: Biophysics and Computational Biology