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Vladislav Panin

Panin, Vladislav
Vladislav Panin
BioBio / Room 341A
Undergraduate Education
B.Sc., M.Sc. Moscow University (1987)
Graduate Education
Ph.D. Moscow University (1990)
Postdoc. Rutgers University (1995-2001)
Joined Texas A&M in 2001

Developmental Biology / Glycosylation and Cell Interactions

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. We are using the advantages of Drosophila model system, including its decreased genetic redundancy, powerful arsenal of molecular genetic approaches, and comprehensively characterized development, to elucidate mechanisms underlying the function of glycosylation in development and physiology. We employ a multidisciplinary approach to study the roles 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 investigates the role of sialyltransferases in neural regulation. Vertebrate sialyltransferases have become the focus of intensive investigation because of their involvement in important biological processes, such as development and function of immune and nervous systems. However, the role of sialyltransferases in modulation of neural excitability remains to be elucidated. We have identified and characterized a Drosophila sialyltransferase, DSiaT, the first sialyltransferase discovered in protostomes. Our results indicate that Drosophila sialyltransferase regulates neuronal excitability and development of the CNS. 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 interested in elucidation of the relationship between phenotypes of DSiaT mutants and human neurological defects associated with abnormal neural excitability due to sialylation abnormalities.

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 dystroglycan with O-mannose. Our results demonstrated that O-mannosylation of dystroglycan is an evolutionarily ancient mechanism conserved between Drosophila and humans, indicating that Drosophila can be 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 controlling this process.

Recent Publications

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  1. Akishina, AA, Vorontsova, JE, Cherezov, RO, Mertsalov, IB, Zatsepina, OG, Slezinger, MS et al.. Xenobiotic-induced activation of human aryl hydrocarbon receptor target genes in Drosophila is mediated by the epigenetic chromatin modifiers. Oncotarget. 2017;8 (61):102934-102947.
    doi: 10.18632/oncotarget.22173. PubMed PMID:29262535. PubMed Central PMC5732701.

  2. Baker, R, Nakamura, N, Chandel, I, Howell, B, Lyalin, D, Panin, VM et al.. Protein O-Mannosyltransferases Affect Sensory Axon Wiring and Dynamic Chirality of Body Posture in the Drosophila Embryo. J. Neurosci. 2018;38 (7):1850-1865.
    doi: 10.1523/JNEUROSCI.0346-17.2017. PubMed PMID:29167399. PubMed Central PMC5815462.

  3. Mertsalov, IB, Novikov, BN, Scott, H, Dangott, L, Panin, VM. Characterization of Drosophila CMP-sialic acid synthetase activity reveals unusual enzymatic properties. Biochem. J. 2016;473 (13):1905-16.
    doi: 10.1042/BCJ20160347. PubMed PMID:27114558. PubMed Central PMC5086458.

  4. Scott, H, Panin, VM. N-glycosylation in regulation of the nervous system. Adv Neurobiol. ;9 :367-94.
    doi: 10.1007/978-1-4939-1154-7_17. PubMed PMID:25151388. PubMed Central PMC4476505.

  5. Scott, H, Panin, VM. The role of protein N-glycosylation in neural transmission. Glycobiology. 2014;24 (5):407-17.
    doi: 10.1093/glycob/cwu015. PubMed PMID:24643084. PubMed Central PMC3976283.

  6. Panin, VM, Wells, L. Protein O-mannosylation in metazoan organisms. Curr Protoc Protein Sci. 2014;75 :12.12.1-12.12.29.
    doi: 10.1002/0471140864.ps1212s75. PubMed PMID:24510673. PubMed Central PMC3984005.

  7. Islam, R, Nakamura, M, Scott, H, Repnikova, E, Carnahan, M, Pandey, D et al.. The role of Drosophila cytidine monophosphate-sialic acid synthetase in the nervous system. J. Neurosci. 2013;33 (30):12306-15.
    doi: 10.1523/JNEUROSCI.5220-12.2013. PubMed PMID:23884937. PubMed Central PMC3721841.

  8. Nakamura, M, Pandey, D, Panin, VM. Genetic Interactions Between Drosophila sialyltransferase and β1,4-N-acetylgalactosaminyltransferase-A Genes Indicate Their Involvement in the Same Pathway. G3 (Bethesda). 2012;2 (6):653-6.
    doi: 10.1534/g3.112.001974. PubMed PMID:22690374. PubMed Central PMC3362294.

  9. Repnikova, E, Koles, K, Nakamura, M, Pitts, J, Li, H, Ambavane, A et al.. Sialyltransferase regulates nervous system function in Drosophila. J. Neurosci. 2010;30 (18):6466-76.
    doi: 10.1523/JNEUROSCI.5253-09.2010. PubMed PMID:20445073. PubMed Central PMC3354699.

  10. Nakamura, N, Lyalin, D, Panin, VM. Protein O-mannosylation in animal development and physiology: from human disorders to Drosophila phenotypes. Semin. Cell Dev. Biol. 2010;21 (6):622-30.
    doi: 10.1016/j.semcdb.2010.03.010. PubMed PMID:20362685. PubMed Central PMC2917527.

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