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Duy T. Tran, Ph.D.

Duy Tran

Staff Scientist

Research Interests:

Mucin-type O-glycosylation is an evolutionarily conserved protein modification found across most eukaryotic species. This form of post-translational modification is initiated by a family of enzymes (ppGalNAc-Ts or GalNAc-Ts in mammals) that catalyze the initial addition of an N-Acetylgalactosamine (GalNAc) sugar onto the hydroxyl group of serine or threonine residues. There are 20 GalNAc-Ts in humans and 18 in mice. The differential tissue and substrate specificities of these enzymes suggest unique roles for each in the organs and tissues where they are expressed. I am utilizing real-time fluorescent imaging techniques to elucidate the importance of O-glycosylation in secretion and correlative light and electron microscopy (CLEM) to determine the localization of individual transferases during various biological processes.

Publications:

Tran D.T., Masedunskas A., Weigert R., and Ten Hagen K.G. Arp2/3-mediated F-actin formation controls regulated exocytosis in vivo. Nat. Commun. 6:10098 doi: 10.1038/ncomms10098 (2015).

News and Views: Merrifield C.J. Actin puts the squeeze on Drosophila glue secretion. Nat Cell Biol. 18, 142-144, doi:10.1038/ncb3305 (2016).

Tran D.T., and Ten Hagen K.G. Mucin-type O-glycosylation during development. J Biol Chem. 2013 Mar 8;288(10):6921-9.

Tran D.T., Lim J.M., Liu M, Stalnaker S.H., Wells L., Ten Hagen K.G., and Live D. Glycosylation of ·-dystroglycan: O-mannosylation influences the subsequent addition of GalNAc by UDP-GalNAc polypeptide N-acetylgalactosaminyltransferases. J Biol Chem. 2012 Jun 15;287(25):20967-74.

Tran, D.T., Zhang, L., Zhang, Y., Tian, E, Earl, LA., and Ten Hagen, K.G. Multiple members of the UDP:GalNAc:polypeptide N-acetylgalactosaminyltransferase family are essential for viability in Drosophila. J Biol Chem. 2012 Feb 17;287(8):5243-52.​​

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This page last updated: February 12, 2016