Abstract

Duy Tran and Jessi Becker evaluated the targeting signals in GalNAc-Ts that direct these enzymes to the Golgi and then retain them in the Golgi. This work was recently published. Nadine Samara and Amy Fernandez studied the structural basis for GalNAc-T substrate specificity using X-ray crystallography.In collaboration with the Ten Hagen lab, Nadine Samara studied the structural basis for enzyme-substrate specificity of two splice variants of pgant9. This work was recently published. We have a collaboration with Henrik Clausen in Denmark on the role of GalNAc-T11 in early mouse development. We also have a collaboration with J.A. Kuivenhoven, in the Netherlands on GalNAc-T2 and metabolism.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Dental & Craniofacial Research (NIDCR)
Type
Investigator-Initiated Intramural Research Projects (ZIA)
Project #
1ZIADE000739-07
Application #
9794589
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
7
Fiscal Year
2018
Total Cost
Indirect Cost

  Institution

Name
Dental & Craniofacial Research
Department
Type
DUNS #
City
State
Country
Zip Code

  Publications

Ji, Suena; Samara, Nadine L; Revoredo, Leslie et al. (2018) A molecular switch orchestrates enzyme specificity and secretory granule morphology. Nat Commun 9:3508
Becker, Jessica L; Tran, Duy T; Tabak, Lawrence A (2018) Members of the GalNAc-T family of enzymes utilize distinct Golgi localization mechanisms. Glycobiology 28:841-848
Herbomel, Gaetan G; Rojas, Raul E; Tran, Duy T et al. (2017) The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation. PLoS One 12:e0179241
Famiglietti, Amber L; Wei, Zheng; Beres, Thomas M et al. (2017) Characterization and expression analysis of Galnts in developing Strongylocentrotus purpuratus embryos. PLoS One 12:e0176479
Revoredo, Leslie; Wang, Shengjun; Bennett, Eric Paul et al. (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 26:360-76
Tian, E; Stevens, Sharon R; Guan, Yu et al. (2015) Galnt1 is required for normal heart valve development and cardiac function. PLoS One 10:e0115861
Raman, Jayalakshmi; Guan, Yu; Perrine, Cynthia L et al. (2015) Erratum: UDP-N-acetyl-?-D-galactosamine: polypeptide N-acetylgalactosaminyltransferases: completion of the family tree. Glycobiology 25:465
Gómez, Hansel; Rojas, Raúl; Patel, Divya et al. (2014) A computational and experimental study of O-glycosylation. Catalysis by human UDP-GalNAc polypeptide:GalNAc transferase-T2. Org Biomol Chem 12:2645-55
Gerken, Thomas A; Revoredo, Leslie; Thome, Joseph J C et al. (2013) The lectin domain of the polypeptide GalNAc transferase family of glycosyltransferases (ppGalNAc Ts) acts as a switch directing glycopeptide substrate glycosylation in an N- or C-terminal direction, further controlling mucin type O-glycosylation. J Biol Chem 288:19900-14
Patterson, Amy P; Tabak, Lawrence A; Fauci, Anthony S et al. (2013) Research funding. A framework for decisions about research with HPAI H5N1 viruses. Science 339:1036-7

Showing the most recent 10 out of 16 publications