Natalie Ahn is recognized for her contributions to the discovery of signal transduction pathways and the application of proteomics technologies to cell regulatory mechanisms. She was among the first to describe enzymes in mammalian MAP kinase pathways, including MAP kinase kinases, and she established that sustained activation of MAP kinase signaling promotes cancer. She was an early investigator to adopt methods of of mass spectrometry and functional proteomics to identify targets of signaling pathways, and the use of hydrogen-deuterium exchange mass spectrometry to describe enzyme allosteric regulation. Ahn was born in San Francisco, CA, and grew up overseas in Korea and Japan. She graduated with a B.S. in Chemistry from the University of Washington, Seattle, received her Ph.D. in Chemistry from the University of California, Berkeley, and was a Merck postdoctoral fellow at the University of Washington. In 1992, she joined the Department of Chemistry and Biochemistry at the University of Colorado, Boulder. She was appointed as an HHMI Investigator from 1994-2014. She is now Distinguished Professor in the Department of Biochemistry and Associate Director of the BioFrontiers Institute. She has been president of the American Society of Biochemistry and Molecular Biology and the U.S. Human Proteome Organization, and she is a member of the National Academy of Sciences and the American Association of Arts and Sciences.

Research Interests

Natalie Ahn's laboratory investigates new mechanisms underlying the regulation and function of cell signaling, by integrating biochemical, biophysical, and cellular strategies with biomolecular analysis by mass spectrometry. Her research examines cell signaling mechanisms involving oncogenic B-Raf/MAPK and Wnt5a pathways, and structural and dynamic properties of protein kinases. Research projects include identification of cellular targets downstream of oncogenic B-Raf/MAPK pathways in cancer, using functional proteomics for large scale protein identification and mapping of protein post-translational modifications. Other projects explore mechanisms underlying a rear-polarized "WRAMP structure" complex assembled in response to the signaling ligand, Wnt5a, which controls directional cell movement through rear-directed Ca2+ signaling and membrane retraction. Finally, biophysical studies combine hydrogen-deuterium exchange mass spectrometry with NMR relaxation and enzyme kinetic measurements to investigate how MAP kinases are regulated at the level of conformational mobility and dynamics, and how this affects the behavior of tight binding kinase inhibitors.

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Primary Section

Section 21: Biochemistry

Secondary Section

Section 29: Biophysics and Computational Biology