Cells of the body are decorated with a variety of carbohydrates (sugars) that serve diverse functions. Alterations in the presence of these sugars are associated with a number of human diseases, including familial tumoral calcinosis and various cancers. To better understand how alterations in glycosylation contribute to disease onset and progression, Dr. Ten Hagen’s group studies how sugar addition (O-glycosylation) is regulated and how it influences basic biological processes. Using Drosophila models, the group has demonstrated that O-glycosylation is an essential modification that is required in specific cells and tissues during development. Current research is directed at further defining the role this protein modification plays in secretion, secretory vesicle formation, cell adhesion, and cell signaling in both Drosophila and mammals. Ultimately, the aim is to elucidate how O-glycosylation regulates key cellular processes during development and disease.
Dr. Kelly Ten Hagen received a B.S. from Cornell University (with distinction and honors) and earned a Ph.D. in genetics at Stanford University. Dr. Ten Hagen has served as an editorial board member for The Journal of Biological Chemistry and for Glycobiology. She currently serves on the Board of Reviewing Editors for eLife and as a Council Member for the American Society for Biochemistry and Molecular Biology (ASBMB). She is a founding member of the Women in Biochemistry and Molecular Biology Committee within the ASBMB. Dr. Ten Hagen is an elected Fellow of the American Association for the Advancement of Science (AAAS). She was the co-recipient of the NIH Equity, Diversity and Inclusion Award in 2019 and received NIH Director’s Awards in 2019 and 2021 for her work promoting women and addressing structural racism in science. She has previously served on the NIH Central Tenure Committee and as the Chair of the NIH Women Scientists Advisors Committee (WSA). She currently serves on the NIH Board of Scientific Directors, the NIH UNITE Committee, the NIH Anti-Racism Steering Committee, the NIH Anti-Harassment Steering Committee and the NIH WSA. Dr. Ten Hagen’s lab studies the enzyme family and factors that regulate protein O-glycosylation and how this conserved protein modification influences organ development and function, to better understand how aberrations contribute to disease.
- Syed ZA, Zhang L, Tran DT, Bleck CKE, Ten Hagen KG. Regulated Restructuring of Mucins During Secretory Granule Maturation In Vivo. Proc Natl Acad Sci U S A. 2022;119(43):e2209750119.
- Zhang L, Mann M, Syed ZA, Reynolds HM, Tian E, Samara NL, Zeldin DC, Tabak LA, Ten Hagen KG. Furin cleavage of the SARS-CoV-2 spike is modulated by O-glycosylation. Proc Natl Acad Sci U S A. 2021;118(47).
- Tian E, Wang S, Zhang L, Zhang Y, Malicdan MC, Mao Y, Christoffersen C, Tabak LA, Schjoldager KT, Ten Hagen KG. Galnt11 regulates kidney function by glycosylating the endocytosis receptor megalin to modulate ligand binding. Proc Natl Acad Sci U S A. 2019;116(50):25196-25202.
- Reynolds HM, Zhang L, Tran DT, Ten Hagen KG. Tango1 coordinates the formation of endoplasmic reticulum/Golgi docking sites to mediate secretory granule formation. J Biol Chem. 2019;294(51):19498-19510.
- Ji S, Samara NL, Revoredo L, Zhang L, Tran DT, Muirhead K, Tabak LA, Ten Hagen KG. A molecular switch orchestrates enzyme specificity and secretory granule morphology. Nat Commun. 2018;9(1):3508.
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This page was last updated on Tuesday, November 14, 2023