Developmental Glycobiology Section
Building 30, Room 407
30 Convent Dr, MSC 4370
Bethesda, MD 20892-4370
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 BS from Cornell University (with distinction and honors) and earned a PhD in genetics at Stanford University. Dr. Ten Hagen has served as an editorial board member for The Journal of Biological Chemistry and currently serves on the Editorial Board for Glycobiology, 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) and was the co-recipient of the 2019 NIH Equity, Diversity and Inclusion Award of the year. She currently serves on the NIH Central Tenure Committee, the NIH Anti-Harassment Steering Committee and the NIH Women Scientists Advisors Committee. 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.
- May C, Ji S, Syed Z, Revoredo L, Paul Daniel EJ, Gerken TA, Tabak LA, Samara NL, Ten Hagen KG. 2020. Differential splicing of the lectin domain of an O-glycosyltransferase modulates both peptide and glycopeptide preferences. J Biol Chem. DOI:10.1074/jbc.RA120.014700.
- Peluso G, Tian E, Abusleme L, Munemasa T, Mukaibo T, Ten Hagen KG. 2020. Loss of the disease-associated glycosyltransferase Galnt3 alters Muc10 glycosylation and the composition of the oral microbiome. J Biol Chem. DOI:10.1074/jbc.RA119.009807.
- Reynolds HM, Zhang L, Tran DT, Ten Hagen KG. 2019. Tango1 coordinates the formation of ER/Golgi docking sites to mediate secretory granule formation. J Biol Chem. 294 (51): 19498-19510.
- Tian E, Wang S, Zhang L, Zhang Y, Malicdan MC, Mao Y, Christoffersen C, Tabak LA, Schjoldager KT, Ten Hagen KG. 2019. Galnt11 regulates kidney function by glycosylating the endocytosis receptor megalin to modulate ligand binding. Proc. Nat’l. Acad. Sci. USA, 116 (50): 25196-25202.
- Ji S, Samara NL, Revoredo L, Zhang L, Tran DT, Muirhead K, Tabak LA, Ten Hagen KG. 2018. A molecular switch orchestrates enzyme specificity and secretory granule morphology. Nature Comm. DOI: 10.1038/s41467-018-05978-9.
- Zhang L, Ribbeck K, Turner B, Ten Hagen KG. 2017. Loss of the mucosal barrier alters the progenitor cell niche via JAK/STAT signaling. J Biol Chem. DOI:10.1074/jbc.M117.809848.
- Tran DT, Masedunskas A, Weigert W, Ten Hagen KG. Arp2/3-mediated F-actin formation controls regulated exocytosis in vivo. Nat Commun. 2015 Dec 7;6:10098.
- Zhang L, Syed ZA, van Dijk Härd I, Lim J-M, Wells L, Ten Hagen KG. O-glycosylation regulates polarized secretion by modulating Tango1 stability. Proc Natl Acad Sci U S A. 2014 May 20;111(20):7296-301.
- Tian E, Hoffman MP, Ten Hagen KG. 2012. O-glycosylation modulates integrin and FGF signaling by influencing the secretion of basement membrane components. Nat Commun. 2012 May 29;3:869