Erin K. O'Shea
Howard Hughes Medical Institute
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Primary Section: 21, Biochemistry Secondary Section: 29, Biophysics and Computational Biology Membership Type:
Member
(elected 2004)
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Biosketch
O’Shea is HHMI’s sixth president and the first woman to lead the Institute. Under her leadership, HHMI has established key priorities for its work in discovery science and science education. She is responsible for new efforts at HHMI to increase diversity in science and improve the academic ecosystem. In addition, she has overseen strategic changes to HHMI’s core programs to ensure the Institute maintains its impact over time. O’Shea previously served as HHMI vice president and chief scientific officer. A leader in the fields of gene regulation, signal transduction, and systems biology, O’Shea maintains a lab at HHMI’s Janelia Research Campus. She has been an HHMI investigator since 2000. Prior to joining HHMI leadership in 2013, O’Shea was the director of Harvard’s Center for Systems Biology and served on the faculties of Harvard and the University of California, San Francisco. O’Shea is a member of the National Academy of Sciences, the American Academy of Arts and Sciences, and the American Academy of Microbiology. She serves on the board of Rescuing Biomedical Research and on the scientific advisory board of the Francis Crick Institute. Since 2017, Washingtonian magazine has twice named O’Shea one of the “most powerful women in Washington.” O’Shea received her undergraduate degree in biochemistry from Smith College and her PhD in chemistry from the Massachusetts Institute of Technology.
Research Interests
Cells survival depends on the ability to sense and respond to a dynamic and unpredictable environment. My lab is interested in how cells sense and coordinate their response to changing environmental conditions. We have focused primarily on deciphering the mechanisms by which budding yeast cells sense and respond to levels of inorganic phosphate in the environment. These studies have led to a detailed understanding of the regulation of protein function by phosphorylation and to fundamental insights into the control of protein trafficking into and out of the nucleus. We are now focused on determining how the network of proteins involved in these responses allow cells to maintain constant intracellular levels of nutrients and ions despite unpredictable fluctuations in the external environment. Recently, with Jonathan Weissman's group, we have also developed reagents that allow us to monitor properties of virtually the entire complement of proteins expressed by the yeast cell.
