Deborah K. Morrison
Data Management Services
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Primary Section: 41, Medical Genetics, Hematology, and Oncology Membership Type:
Member
(elected 2022)
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Biosketch
Deborah Morrison is a leader in the study of the RAF protein kinases, which play a key role in normal growth and development as well as in human cancer. Her work has provided critical insights into the biochemical and structural basis of RAF activation and has guided the design of new therapeutic strategies. Morrison was born and raised in Nashville, Tennessee. She graduated from David Lipscomb College with a degree in biology and obtained her Ph.D. in Cellular and Molecular Biology from Vanderbilt University School of Medicine in 1996. She began studying signal transduction as a postdoctoral fellow in the laboratory of Dr. Thomas Roberts at Harvard Medical School and as a Howard Hughes Research Fellow in the laboratory of Dr. Lewis Williams at University of California-San Francisco. In 1990, she joined the ABL-Basic Research Program at the Frederick Cancer Research Facility in Frederick, Maryland and became head of the Cellular Growth Mechanisms Section in 1995. Morrison joined the National Cancer Institute - Center for Cancer Research in 1999 and became Chief of the Laboratory of Cell and Developmental Signaling in 2006. She is a member of the American Association for Cancer Research and the National Academy of Sciences.
Research Interests
Deborah Morrison's research focuses on the signal transduction pathway regulated by the Ras family of GTPases. This pathway is required for normal growth and development, and mutations in various components of the pathway can function as disease drivers in human cancer and in a group of related developmental disorders known as the RASopathies. The RAF kinases are central intermediates in the RAS pathway functioning as direct effectors of activated RAS and as the initiating kinases in the ERK/MAPK cascade, comprised of the RAF, MEK and ERK protein kinases. Her laboratory has extensive expertise in the identification of protein phosphorylation sites and in the proteomic analysis of signaling complexes, which has been instrumental for their studies investigating the regulation of RAF kinase function. Their work also resulted in the first reported structure of a full-length, autoinhibited RAF kinase in which the critical RAS-binding domain is resolved. In addition, their studies have addressed the role of that the KSR and CNK protein scaffolds play in facilitating and modulating RAS-dependent signaling. Ultimately, the goal of hergroup's research is to identify critical regulatory mechanisms that may prove helpful in the diagnosis and/or treatment of human disease states with aberrant RAS pathway signaling.
