460 W 12Th Ave
Columbus, OH 43210-2208
As a member of Department of Cancer Biology and Genetics, my research interests are largely directed toward understanding how protein posttranslational modifications (PTMs) affect the molecular regulation of protein kinases, and seek novel therapeutic opportunities for cancer treatment.
Our team is developing and applying protein chemoenzymatic approaches to site-specifically install PTMs such as phosphorylation and ubiquitin into target protein kinase, and employ a combination of biochemical, structural and cellular approaches to define kinase regulation mechanisms. Currently, we are investigating in three key Ser/Thr kinases S6K1 (mTORC1-S6K1 signaling), Cdk5 and LKB1.
Education and Training
PhD, Technical University of Munich, Munich, Germany, 2008-2013
Postdoctoral fellow, Johns Hopkins University School of Medicine, 2014-2017
Postdoctoral fellow, Harvard Medical School, 2017-2021
- Chu N.*, Viennet T.*, Bae H., Salguero A., Boeszoermenyi A., Arthanari H., Cole P. “Structural determinants of PH domain-mediated regulation of Akt revealed by segmental labeling”. eLife, 2020, 9:e59151
- Hsu JW., Bai M., Li K., Yang JS., Chu N., Cole P., Eck M., Li J., Hsu V. “The protein kinase Akt acts as a coat adaptor in endocytic recycling”. Nature Cell Biology, 2020, 22: 927-933
- Chu N., Salguero A., Liu A., Chen Z., Dempsey D., Ficarro S., Alexander W., Marto J., Li Y., Amzel M., Gabelli S., Cole P. “Akt kinase activation mechanisms revealed using protein semisynthesis”. Cell, 2018, 174: 897-907
- Henager S.*, Chu N.*, Chen Z., Bolduc D., Dempsey D., Hwang Y., Wells J., Cole P. “Enzyme-catalyzed expressed protein ligation”. Nature Methods, 2016, 13: 925-927
- Chu N., Shabbir W., Bove-Fenderson E., Araman C., Lemmens-Gruber R., Harris A.D., and Becker C.F.W. A C-terminal membrane anchor affects the interactions of prion proteins with lipid membranes. Journal of Biological Chemistry, 2014, 289(43):30144-60
- Tripsianes K.*, Chu N.*, Friberg A., Sattler M. and Becker C. “Studying Weak and Dynamic Interactions of Posttranslationally Modified Proteins using Expressed Protein Ligation”. ACS Chemical Biology, 2014, 9:347-352 *: equal contributions