Kelly Ten Hagen, Ph.D.
NIH/NIDCR
Building 30, Room 407
30 Convent Dr. MSC 4370
Bethesda, MD 20892-4370
United States
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.
Biographical Sketch
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 is an elected Fellow of the American Association for the Advancement of Science (AAAS) and the American Society for Biochemistry and Molecular Biology (ASBMB). She received the Rosalind Kornfeld Award for Lifetime Achievement in Glycobiology and was selected for the Irwin J. Goldstein Lectureship. Dr. Ten Hagen has served as an editorial board member for The Journal of Biological Chemistry and for Glycobiology. She was a member of the Board of Directors for the Society for Glycobiology and served as a Council Member for the ASBMB. She is currently on the Board of Reviewing Editors for eLife. She has previously served on the NIH Central Tenure Committee and the NIH Board of Scientific Directors. Dr. Ten Hagen’s research advances our understanding of the molecular, cellular and organismal impact of protein glycosylation and how aberrations in this conserved modification lead to disease.
- Syed ZA, Zhang L, Tran DT, Bleck CKE, Ten Hagen KG. Regulated restructuring of mucins during secretory granule maturation in vivo. 2022 Oct 25;119(43):e2209750119. Proc Natl Acad Sci U S A. doi: 10.1073/pnas.2209750119.
- Ten Hagen KG, Wolinetz C, Clayton JA, Bernard MA. Community voices: NIH working toward inclusive excellence by promoting and supporting women in science. Nat Commun. 2022 Mar 25;13(1):1682. doi: 10.1038/s41467-022-28665-2.
- Zhang L, Mann M, Syed Z, Reynolds HM, Tian E, Samara NL, et al. Furin cleavage of the SARS-CoV-2 spike is modulated by O-glycosylation. Proc Natl Acad Sci U S A. 2021 Nov 23;118(47). doi: 10.1073/pnas.2109905118.
- May C, Ji S, Syed ZA, Revoredo L, Paul Daniel EJ, Gerken TA, et al. Differential splicing of the lectin domain of an O-glycosyltransferase modulates both peptide and glycopeptide preferences. J Biol Chem. 2020 Aug 28;295(35):12525-12536. doi: 10.1074/jbc.RA120.014700.
- Peluso G, Tian E, Abusleme L, Munemasa T, Mukaibo T, Ten Hagen KG. Loss of the disease-associated glycosyltransferase Galnt3 alters Muc10 glycosylation and the composition of the oral microbiome. J Biol Chem. 2020 Jan 31;295(5):1411-1425. doi: 10.1074/jbc.RA119.009807.
- Reynolds HM, Zhang L, Tran DT, Ten Hagen KG. Tango1 coordinates the formation of ER/Golgi docking sites to mediate secretory granule formation. J Biol Chem. 2019 Dec 20;294(51):19498-19510. doi:10.1074/jbc.RA119.011063.
- Tian E, Wang S, Zhang L, Zhang Y, Malicdan MC, Mao Y, et al. Galnt11 regulates kidney function by glycosylating the endocytosis receptor megalin to modulate ligand binding. Proc Natl Acad Sci U S A. 2019 Dec 10;116(50):25196-25202. doi: 10.1073/pnas.1909573116.
- Ji S, Samara NL, Revoredo L, Zhang L, Tran DT, Muirhead K, et al. A molecular switch orchestrates enzyme specificity and secretory granule morphology. Nat Commun. 2018 Aug 29;9(1):3508. doi: 10.1038/s41467-018-05978-9.
- Zhang L, Turner B, Ribbeck K, Ten Hagen KG. Loss of the mucosal barrier alters the progenitor cell niche via Janus kinase/signal transducer and activator of transcription (JAK/STAT) signaling. J Biol Chem. 2017 Dec 29;292(52):21231-21242. doi:10.1074/jbc.M117.809848.
- Tran DT, Masedunskas A, Weigert R, Ten Hagen KG. Arp2/3-mediated F-actin formation controls regulated exocytosis in vivo. Nat Commun. 2015 Dec 7;6:10098. doi: 10.1038/ncomms10098.
- Zhang L, Syed ZA, van Dijk Härd I, Lim JM, 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. doi: 10.1073/pnas.1322264111.
- Tian E, Hoffman MP, Ten Hagen KG. O-glycosylation modulates integrin and FGF signalling by influencing the secretion of basement membrane components. Nat Commun. 2012 May 29;3:869. doi: 10.1038/ncomms1874.