Our research interests span the gap between biology and chemistry. We are intrigued by the roles of protein post-translational modifications in regulating human physiological and pathological processes. We focus on a unique type of protein glycosylation, termed O-linked β-N-acetylglucosamine (O-GlcNAc). This modification dynamically regulates various biological processes and its dysfunction has been detected in many diseases. Our research program integrates multidisciplinary approaches to elucidate the mechanism and function of this O-GlcNAc modification. Read more...

Dr. Jiaoyang Jiang earned her PhD in chemistry from Brown University with David Cane, where she elucidated natural product biosynthetic pathways in bacteria. Following that, Dr. Jiang performed postdoctoral research at Harvard Medical School in the laboratory of Suzanne Walker, where she characterized the glycosyltransferase & the unique proteolytic activities of human O-GlcNAc transferase (OGT), and discovered a small molecule with novel mechanism of inhibition. In August 2013, Dr. Jiang started her appointment as an Assistant Professor of Drug Discovery at the UW-Madison School of Pharmacy. She was promoted to Associate Professor with tenure in 2019, and Full Professor in 2024.

Education:

• Postdoc Chemical Biology - Harvard Medical School, 2013
• PhD Chemistry - Brown University, 2009
• BS Chemistry - Univ. of Science & Technology of China, 2004

• Hu CW, Wang A, Fan D, Worth M, Chen Z, Huang J, Xie J, Macdonald J, Li L, Jiang J*. OGA mutant aberrantly hydrolyzes O-GlcNAc modification from PDLIM7 to modulate p53 and cytoskeleton in promoting cancer cell malignancy. Proceedings of the National Academy of Sciences of the United States of America. 2024, 121(24): e2320867121. Previous preprint of the manuscript:  https://doi.org/10.21203/rs.3.rs-2709128/v1.
• Blankenship CM^#, Xie J^#, Benz C, Wang A, Ivarsson Y, Jiang J*. Motif-dependent binding on the intervening domain regulates O-GlcNAc transferase. Nature Chemical Biology. 2023, 19(11): 1423-1431. Previous preprint of the manuscript: https://doi.org/10.21203/rs.3.rs-2531412/v1. (#equal contribution)
• Hu CW^#, Worth M^#, Fan D^#, Li B^#, Li H^#, Lu L, Zhong X, Lin Z, Wei L, Ge Y, Li L, Jiang J*. Electrophilic probes for deciphering substrate recognition by O-GlcNAc transferase. Nature Chemical Biology (2017) 13, 1267-73. (#equal contribution)
• Liu F, Ma F, Wang Y, Hao L, Zeng H, Jia C, Wang Y, Liu P, Ong IM, Li B, Chen G, Jiang J, Gong S, Li L, Xu W. PKM2 methylation by CARM1 activates aerobic glycolysis to promote tumorigenesis. Nature Cell Biology (2017) 19, 1358-70.
• Li B^#, Li H^#, Hu CW, Jiang J*. Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase. Nature Communications (2017) 8:666. doi: 10.1038/s41467-017-00865-1. (#equal contribution)
• Li B, Li H, Lu L, Jiang J*. Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode. Nature Structural & Molecular Biology (2017) 24, 362-9. [News and Views, Nat Struct Mol Biol. 2017, 24, 433.]
• Worth M^#, Li H^#, Jiang J*. Deciphering the functions of protein O-GlcNAcylation with chemistry. ACS Chemical Biology (2017), 12, 326-35. (^#equal contribution)
• Lu L, Fan D, Hu CW, Worth M, Ma ZX, Jiang J*. Distributive O-GlcNAcylation on the highly repetitive C-terminal domain of RNA polymerase II. Biochemistry (2016), 55, 1149-58. 
• Lazarus MB*, Jiang J*, Kapuria V, Bhuiyan T, Janetzko J, Zandberg WF, Vocadlo DJ, Herr W, Walker S. HCF-1 is cleaved in the active site of O-GlcNAc transferase. (*equal contribution) Science (2013), 342, 1235-9.
• Lazarus, MB*; Jiang, J*; Gloster, TM; Zandberg, WF; Whitworth, GE; Vocadlo, DJ; Walker, S. Structural snapshots of the reaction coordinate for O-GlcNAc transferase. (*equal contribution) Nature Chemical Biology (2012), 8, 966-8.
• Jiang, J*; Lazarus, MB*; Pasquina, L; Sliz, P; Walker, S. A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase. (*equal contribution) Nature Chemical Biology (2012), 8, 72-7.
• Jiang, J; Tetzlaff, CN; Takamatsu, S; Iwatsuki, M; Komatsu, M; Ikeda, H; Cane, DE. Genome mining in Streptomyces avermitilis. A biochemical Baeyer-Villiger reaction and discovery of a new branch of the pentalenolactone family tree. Biochemistry (2009), 48, 6431-40.
• Jiang, J; Cane, DE. Geosmin biosynthesis. Mechanism of the fragmentation-rearrangement in the conversion of germacradienol to geosmin. Journal of the American Chemical Society (2008), 130, 428-9.
• Jiang, J; He, X; Cane, DE. Biosynthesis of the earthy odorant geosmin by a bifunctional Streptomyces coelicolor enzyme. Nature Chemical Biology (2007), 3, 711-5.
• Jiang, J; He, X; Cane, DE. Geosmin biosynthesis. Streptomyces coelicolor germacradienol/germacrene D synthase converts farnesyl diphosphate to geosmin. Journal of the American Chemical Society (2006), 128, 8128-9.