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Vlad Panin

Vlad Panin

Associate Professor

Department of Biochemistry and Biophysics

Room 341A Biochemistry and Biophysics Building
2128 TAMU

College Station , TX 77843-2128
Office Phone: (979) 458-4630

Education:

  1. M.S., Moscow University, 1987
  2. Ph.D., Moscow University, 1990
  3. Postdoc., Rutgers University, 1995-2001

Biography:

Research Interests:

Our research interests belong to the intersection of developmental biology and neurobiology with the field of biochemistry/ glycobiology, and our research is focused on understanding the function of glycosylation in developmental events and nervous system functions. It has been long recognized that glycans play a wide spectrum of essential roles in metazoan organisms, while defects in glycosylation are involved in numerous human diseases and abnormalities, from cancer to brain malformation and defects of immune system. However, the complexity of glycosylation pathways and limitations of genetic and in vivo approaches available for studying glycosylation in higher animals significantly impede the research in mammals. Thus, studying glycosylation in model organisms is instrumental for elucidating molecular mechanisms of glycan functions. We are using the advantages of Drosophila model system, including its low genetic redundancy, powerful arsenal of genetic techniques, complete genome information, and comprehensively characterized development, to elucidate molecular mechanisms underlying biological roles of glycosylation in development and physiology. We employ a multidisciplinary approach to study functions of several novel glycosyltransferase genes at molecular, cellular, and organismal levels. Currently, our laboratory is involved in two main projects: one project focuses on studying the function of sialylation in the central nervous system, while another project is aimed at elucidation of molecular mechanisms of protein O-mannosylation.

The first project is directed towards detailed understanding of molecular and genetic mechanisms of Drosophila sialylation. Vertebrate sialyltransferases have become the focus of intensive investigation because of their involvement in important biological processes, such as immune and nervous system functioning. However, little is known about sialyltransferases in the protostome lineage of animals, including Drosophila. In our studies, we have identified and characterized a Drosophila sialyltransferase, DSiaT, the first discovered sialyltransferase in protostomes. In Drosophila, sialyltransferase is represented by a single gene which is expressed throughout all developmental stages. We found that the expression of this gene is tightly regulated and restricted to the central nervous system. Our results indicate that Drosophila sialyltransferase plays an important role in the CNS, being involved in regulating neuronal excitability and neurodevelopment. Our current research focuses on identifying molecular targets of sialylation and revealing its functional mechanisms at molecular, cellular and organismal levels. A human homologue of Drosophila sialyltransferase has enzymatic activity similar to that of DSiaT, while its expression is similarly elevated in the brain. Thus, we are also interested in elucidation of the relationship between neurological phenotypes of DSiaT mutants and human neurological defects associated with abnormal neural excitability and analogous defects of sialylation.

Our second project focuses on developing Drosophila model of dystroglycanopathies, human congenital muscular dystrophies resulting from abnormal glycosylation of alpha-dystroglycan. Drosophila has homologues of all essential components of the mammalian dystroglycan-mediated pathway, including dystroglycan and two protein O-mannosyltransferases that modify it with O-mannose. Our results demonstrated that O-mannosylation of dystroglycan is an evolutionarily ancient mechanism conserved between Drosophila and humans, suggesting that Drosophila can be used as a model system for studying human congenital muscular dystrophies. Our current research is aimed at elucidation of molecular and genetics mechanisms of dystroglycan O-mannosylation and identification of novel genes involved in its control.

Selected Publications:

Koles, K., Repnikova, E., Pavlova, G., Korochkin, L.I., and Panin, V.M. 2009. Sialylation in protostomes: a perspective from Drosophila genetics and biochemistry. Glycoconj J 26: 313-324.

Koles, K., Lim, J.M., Aoki, K., Porterfield, M., Tiemeyer, M., Wells, L., and Panin, V. 2007. Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster. Glycobiology 17: 1388-1403.

North, S.J., Koles, K., Hembd, C., Morris, H.R., Dell, A., Panin, V.M., and Haslam, S.M. 2006. Glycomic studies of Drosophila melanogaster embryos. Glycoconj J 23: 345-354.

Lyalin, D., Koles, K., Roosendaal, S.D., Repnikova, E., Van Wechel, L., and Panin, V.M. 2006. The twisted gene encodes Drosophila protein O-mannosyltransferase 2 and genetically interacts with the rotated abdomen gene encoding Drosophila protein O-mannosyltransferase 1. Genetics 172: 343-353.

Luo, Y., Koles, K., Vorndam, W., Haltiwanger, R.S., and Panin, V.M. 2006. Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1 repeats. J Biol Chem 281: 9393-9399.

Koles, K., Irvine, K.D., and Panin, V.M. 2004. Functional characterization of Drosophila sialyltransferase. J Biol Chem 279: 4346-4357.

Lei, L., Xu, A., Panin, V.M., and Irvine, K.D. 2003. An O-fucose site in the ligand binding domain inhibits Notch activation. Development 130: 6411-6421.

Correia, T., Papayannopoulos, V., Panin, V., Woronoff, P., Jiang, J., Vogt, T.F., and Irvine, K.D. 2003. Molecular genetic analysis of the glycosyltransferase Fringe in Drosophila. Proc Natl Acad Sci U S A 100: 6404-6409.

Panin, V.M., Shao, L., Lei, L., Moloney, D.J., Irvine, K.D., and Haltiwanger, R.S. 2002. Notch ligands are substrates for protein O-fucosyltransferase-1 and Fringe. J Biol Chem 277: 29945-29952.

Moloney, D.J., Panin, V.M., Johnston, S.H., Chen, J., Shao, L., Wilson, R., Wang, Y., Stanley, P., Irvine, K.D., Haltiwanger, R.S. et al. 2000. Fringe is a glycosyltransferase that modifies Notch. Nature 406: 369-375.

Papayannopoulos, V., Tomlinson, A., Panin, V.M., Rauskolb, C., and Irvine, K.D. 1998. Dorsal-ventral signaling in the Drosophila eye. Science 281: 2031-2034.

Panin, V.M. and Irvine, K.D. 1998. Modulators of Notch signaling. Semin Cell Dev Biol 9: 609-617.

Panin, V.M., Papayannopoulos, V., Wilson, R., and Irvine, K.D. 1997. Fringe modulates Notch-ligand interactions. Nature 387: 908-912.

Sergeev, P.V., Panin, V.M., Pavlova, G.V., Kopantseva, M.R., Shostak, N.G., Bashkirov, V.N., Georgiev, G.P., and Korochkin, L.I. 1995. The expression of esterase S gene of Drosophila virilis in Drosophila melanogaster. FEBS Lett 360: 194-196.

Korochkin, L.I., Panin, V.M., Pavlova, G.V., Kopantseva, M.R., Shostak, N.G., Bashkirov, V.N., Gabitova, L.B., and Sergeev, P.V. 1995. A relatively small 5' regulatory region of esterase S gene of Drosophila virilis determines the specific expression as revealed in transgenic experiments. Biochem Biophys Res Commun 213: 302-310.

Krajewski, W.A., Panin, V.M., and Razin, S.V. 1993. A simple and reproducible method for analysis of chromatin condensation. Biochem Biophys Res Commun 193: 113-118.

Krajewski, W.A., Panin, V.M., and Razin, S.V. 1993. Dynamics of unfolded nucleosomal fiber. J Biomol Struct Dyn 10: 1013-1022.

Krajewski, W.A., Panin, V.M., and Razin, S.V. 1993. Acetylation of core histones causes the unfolding of 30 nm chromatin fiber: analysis by agarose gel electrophoresis. Biochem Biophys Res Commun 196: 455-460.

Krajewski, W.A., Panin, V.M., Krylov, D., and Razin, S.V. 1993. Flexibility of DNA within transcriptionally active nucleosomes: analysis by circular dichroism measurements. J Biomol Struct Dyn 10: 1001-1011.

Publications from Genetics Graduate Students:

Koles, K., Repnikova, E., Pavlova, G., Korochkin, L.I., and Panin, V.M. 2009. Sialylation in protostomes: a perspective from Drosophila genetics and biochemistry. Glycoconj J 26: 313-324.

Lyalin, D., Koles, K., Roosendaal, S.D., Repnikova, E., Van Wechel, L., and Panin, V.M. 2006. The twisted gene encodes Drosophila protein O-mannosyltransferase 2 and genetically interacts with the rotated abdomen gene encoding Drosophila protein O-mannosyltransferase 1. Genetics 172: 343-353.

Current Genetics Students:

Hillary Scott

Alumni:

Mindy Carnahan

Dmitry Lyalin

Elena Repnikova

Courses:

GENE 302 Principles of Genetics
BICH 689 Glycobiology of Development and Disease