Abstract

Our lab studies the structure and function of GalNAc-Ts. Nadine Samara and Amy Fernandez studied the structural basis for GalNAc-T12 substrate specificity using X-ray crystallography and kinetics. We collaborated with Tom Gerken and Jeffrey Grey on this work. A non-conserved GalNAc binding pocket in the GalNAc-T12 catalytic domain dictates its unique substrate specificity. A manuscript is in revision for PNAS. In collaboration with the Ten Hagen lab, and the Schjoldager lab, we studied the role of GalNAc-T11 on kidney function. Ligand binding of the endocytosis receptor megalin is dependent on GalNAc-T11 glycosylation. This work is in revision for PNAS.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Dental & Craniofacial Research (NIDCR)
Type
Investigator-Initiated Intramural Research Projects (ZIA)
Project #
1ZIADE000739-08
Application #
10003744
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
8
Fiscal Year
2019
Total Cost
Indirect Cost

  Institution

Name
National Institute of Dental & Craniofacial Research
Department
Type
DUNS #
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State
Country
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  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