Senior Investigator, NIDCR
Principal Deputy Director, NIH
30 Convent Dr.
Building 30, Room 524
Bethesda, MD 20892
National Institutes of Health
Building 1, Room 126
Bethesda, MD 20892-2290
Education/Previous Training and Experience:
Dr. Tabak was appointed as the principal deputy director of the NIH on August 23, 2010. Previously he served as acting principal deputy director of the NIH from November 13, 2008 through August 14, 2009. Named as the director of the National Institute of Dental and Craniofacial Research (NIDCR) in September 2000, he held that post through August 2010. Prior to joining NIH, Dr. Tabak served as the senior associate dean for research and professor of dentistry and biochemistry & biophysics in the School of Medicine and Dentistry at the University of Rochester in New York. A former NIH MERIT recipient, Dr. Tabak has received several honors and awards for his work including being elected as a member of the Institute of Medicine of the National Academies. He has also received teaching awards for his work with both graduate and medical students.
Revoredo, L., Wang, S. Bennett, E.P., Clausen, H., Moremen, K.W., Jarvis,D.L. Ten Hagen, K.G. Tabak, L.A., and Gerken, T.A., 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 2015, 1–17 doi: 10.1093/glycob/cwv10
Tian, E, Stevens, S.R., Springer, D.A., Anderson, S.A. Starost, M.F., Patel, V., Ten Hagen, K.G., and Tabak, L.A. Galnt1 is required for normal heart valve development and cardiac function. PLoS One, 10(1): e0115861.doi:10.1371/journal.pone.0115861, 2015
Gomez, H., Rojas, R., Patel, D., Tabak, L.A., Lluch, J., and Masgrau, L., A computational and experimental study of O-glycosylation. Catalysis by human UDP- GaINac polypeptide: GaINac transferase-T2. Org. Biomol. Chem., 12: 2645-2655, 2014.
Bennett, E.P., Mandel, U., Clausen, H., Gerken, T.A., Fritz, T.A., and Tabak, L.A. Control of Mucin-Type O-Glycosylation – A Classification of the Polypeptide GalNAc-transferase Gene Family, Glycobiology (2011)22:736-756, 2012.
Holleboom,A.G., Karlsson,H., Lin,R.-S., Beres, T.M., Sierts, J.A., Herman, D.S., Stroes, E.S.G., Aerts, J.M., Kastelein, J.J.P., Motazacker, M.M., Dallinga-Thie, G.M., Levels, J.H.M., Zwinderman, A.H., Seidman, J.G., Seidman, C.E., Ljunggren, S., Lefeber, D.J., Morava, E., Wevers, R.A., Fritz, T.A., Tabak, L.A., Lindahl, M., Hovingh, G.K., and Kuivenhoven, J.A. Heterozygosity for a Loss-of-Function Mutation in GALNT2 Improves Plasma Triglyceride Clearance in Man. Cell Metabolism 14:811–818, 2011.
Gerken, T.A., Jamison, O., Perrine, C.L., Collette, J.C., Moinova, H., Ravi, L., Markowitz, S.D.,, Shen, W., Patel, H., and Tabak, L.A. Emerging paradigms for the initiation of mucin type protein O-glycosylation by the polypeptide GalNAc transferase (ppGalNAc T) family of glycosyltransferases. J. Biol. Chem. 286:14493-14507, 2011.
Tabak, L. A. The Role of Mucin-type O-glycans in Eukaryotic Development. Seminars in Cell and Developmental Biology, 21:616-621, 2010.
Miwa, HE, Gerken, TA, Jamison, O and LA Tabak . Isoform-specific O-glycosylation of osteopontin and bone sialoprotein by polypeptide N-acetylgalactosaminyltransferase-1. J. Biol. Chem., 2010 285; 1208 –1219, 2010.
Perrine, CL, Ganguli, A, Wu, P, Bertozzi, CR, Fritz,TA, Raman, J, Tabak, LA and TA Gerken. Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2. J. Biol. Chem., 284; 20387-20397, 2009.
Raman, J, Fritz, TA., Gerken, TA, Jamison, O, Live, D, Liu,M and Tabak, LA. The catalytic and lectin domains of UDP-GalNAc:polypeptide α-N Acetylgalactosaminyltransferase function in concert to direct glycosylation site selection. J. Biol Chem., 283; 22942-22951, 2008.
Tenno M, Ohtsubo K, Hagen FK, Ditto D, Zarbock A, Schaerli P, von Andrian UH, Ley K, Le D, Tabak LA, Marth JD. Initiation of protein O glycosylation by the polypeptide GalNAcT-1 in vascular biology and humoral immunity. Mol Cell Biol (27): 8783-96, 2007.
Fritz TA, Raman J, Tabak LA. Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferase-2. J Biol Chem. 281(13):8613-9, 2006.