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Kelly G. Ten Hagen, Ph.D.

Kelly Ten Hagen, Ph.D.Senior Investigator
Deputy Chief, Oral and Pharyngeal Cancer Branch​
Chief, Developmental Glycobiology Section

BETHESDA, MD 20892-4370

Phone: (301) 451-6318
Fax: (301) 402-0897

Biographical Sketch

Dr. Ten Hagen received her B.S. (magna cum laude) from Cornell University and earned her Ph.D. in genetics from Stanford University. She served as a Research Assistant Professor at the University of Rochester from 1992-2001, and then as a Senior Research Fellow in the NIDDK, NIH from 2001-2004. She was appointed Chief of the Developmental Glycobiology Unit in the NIDCR, NIH in 2004 and was promoted to Senior Investigator and Chief in 2012.  Her laboratory studies the mechanistic roles of protein glycosylation during eukaryotic development. She has served as an Editorial Board Member for The Journal of Biological Chemistry, as the Society for Glycobiology Representative to the International Glycoconjugate Organization and on the Board of Directors as a federal liaison for the Society for Glycobiology. She currently serves on the Promotion and Tenure Committee for NIDCR, the Woman Scientist Advisors Committee and Executive Committee for the NIH, the steering committees for the NIH Glycobiology and Developmental Biology Scientific Interest Groups and as an Editorial Board Member for the journal Glycobiology.

Research Interests/Scientific Focus

Cells of the body are decorated with a variety of carbohydrates (sugars) that serve many diverse functions. These sugars not only act as a protective barrier on the outside of cells, but are also involved in communication and signaling events in many organisms. Our group studies one type of sugar addition to proteins, known as mucin-type O-linked glycosylation, which is initiated by the polypeptide GalNAc transferase (PGANT) enzyme family. Alterations in this type of glycosylation are associated with a number of human diseases. However, the mechanistic roles of this protein modification are not fully understood. Hence, the overarching goal of the Developmental Glycobiology Section is to determine the mechanisms by which O-glycosylation influences basic biological processes to better understand the role of this modification in development and disease. As O-glycosyltransferases are components of the secretory apparatus and are responsible for the modification of secreted and membrane bound proteins, we hypothesize that they play crucial roles in conserved biological functions related to secretion, localization, stability, and function of proteins. Using Drosophila melanogaster, we have determined that at least 5 members of this multigene family are essential for viability. We have also elucidated a specific role for one O-glycosyltransferase in modulating matrix composition and cell adhesion during Drosophila development. We have further demonstrated that O-glycosyltransferases can influence matrix composition during mammalian development, indicating a conserved role for O-glycosylation in the establishment of cellular microenvironments across species. Mechanistically, we have discovered that O-glycosylation modulates secretion and secretory vesicle formation by protecting a conserved cargo receptor from proteolysis.  Taken together, our discoveries highlight novel roles for O-glycosylation in conserved cell biological processes that potentially impact all aspects of development. We will continue to elucidate the mechanisms by which O-glycosylation is acting to gain a fundamental understanding of how alterations in glycosylation can contribute to disease onset and progression.

Selected Publications

  1. Tran DT, Zhang L, Zhang Y, Tian E, Earl L, Ten Hagen KG. 2012. Multiple members of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase family are essential for viability in Drosophila. J Biol Chem. 287 (8): 5243-5252.
  2. Kakani S, Yardeni T, Poling J, Ciccone C, Niethamer T, Klootwijk RD, Manoli I, Darvish D, Hoogstraten-Miller S, Zerfas P, Speranksy V, Tian E, Ten Hagen KG, Kopp JB, Gahl WA, Huizing M. 2012. The Gne M712T mouse as a model for human glomerulopathy. Am J Pathol. 180(4): 1-10.
  3. Tian E, Hoffman MP, Ten Hagen KG. 2012. O-glycosylation modulates integrin and FGF signaling by influencing the secretion of basement membrane components. Nature Comm. 3:869 DOI: 10.1038/NCOMMS1874. (Our image was selected as the Featured Image for this issue. This was also the featured article on the NIH Deputy Director for Intramural Research Web Board for June 2012.)
  4. Tran DT, Lim JM, Liu M, Stalnaker SH, Wells L, Ten Hagen KG*, Live D*. 2012. Glycosylation of -dystroglycan: O-mannosylation influences the subsequent addition of GalNAc by the UDP-GalNAc polypeptide N-acetylgalactosaminyltransferases. J Biol Chem. 287 (25): 20967-20974. (* co-contributing authors).
  5. Tran DT, Ten Hagen KG. 2013. Mucin-type O-glycosylation during development. J Biol Chem. 288(10): 6921-6929. (Our image was selected as the cover image for this issue).
  6. Zhang L, Syed ZA, van Dijk Härd I, Lim J-M, Wells L, Ten Hagen KG. 2014. O-glycosylation regulates polarized secretion by modulating Tango1 stability. Proc. Nat’l. Acad. Sci. USA, 111(20): 7296-7301.
  7. Tian E, Stevens SR, Guan Y, Anderson SA, Springer DA, Starost MF, Patel V, Ten Hagen KG, Tabak L. 2015. Galnt1 is required for normal heart valve development and cardiac function. PLoS ONE 10(1): e0115861. doi:10.1371/journal.pone.0115861.
  8. Tran DT, Masedunskas A, Weigert W, Ten Hagen KG. 2015. Arp2/3-mediated F-actin formation controls regulated exocytosis in vivo. Nature Comm. DOI: 10.1038/NCOMMS10098. (This paper is featured in a Nature Cell Biology News and Views article).
  9. Revoredo L, Wang S, Bennett EP, Clausen H, Moremen KW, Jarvis DL, Ten Hagen KG, Tabak LA, Gerken TA 2016. Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family. Glycobiology 26(4): 360-376.

Complete CV and Publications (PDF File, 31KB)


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This page last updated: August 18, 2016