Molecular Cloning of Synucleins in River Lamprey Lampetra fluviatilis

  • O. V. Vorontsova
  • E. E. Akkuratov
  • O. M. Korenkova
  • O. ShupliakovEmail author


Synaptic proteins synucleins are found in pathologic aggregates in human brain during neurodegenerative diseases and in some tumors. Normal functions of these proteins in synapses are still unclear. In the present study, we used cDNA cloning to determine amino acid sequences of synucleins in the central nervous system of river lamprey (Lampetra fluviatilis), which is used as a model organism to study molecular mechanisms of synaptic transmission. Three genes are identified. High similarity in amino acid sequences as compared to other vertebrate species is revealed. The bioinformatic analysis predicts that the river lamprey synucleins relate to the group of gamma-synucleins. High homology with human alpha-synuclein is reported. The hydrophobic region required for the formation of alpha-synuclein amyloid fibers is also present in the river lamprey synucleins. The latter suggests that this region appeared at early stages of evolution. The obtained amino acid sequences of synucleins in the river lamprey brain will allow generating novel molecular tools for dissecting physiological functions of these proteins.


synuclein molecular cloning synapse lamprey evolution synucleinopathies 


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  1. 1.
    Toni M., Cioni C. 2015. Fish synucleins: An update. Mar. Drugs. 13 (11), 6665–6686.CrossRefPubMedPubMedCentralGoogle Scholar
  2. 2.
    Bendor J. T., Logan T. P., Edwards R. H. 2013. The function of alpha-synuclein. Neuron. 79 (6), 1044–1066.CrossRefPubMedGoogle Scholar
  3. 3.
    Maroteaux L., Campanelli J. T., Scheller R. H. 1988. Synuclein: A neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci. 8 (8), 2804–2815.CrossRefPubMedGoogle Scholar
  4. 4.
    Hasegawa, M. Nonaka, T., Masuda-Suzukake M. 2016. Alpha-synuclein: Experimental pathology. Cold Spring Harb. Perspect. Med. 6 (9), pii: a024273.Google Scholar
  5. 5.
    Sundborger A., Soderblom C., Vorontsova O., Evergren E., Hinshaw J. E., Shupliakov O. 2011. An endophilin-dynamin complex promotes budding of clathrin-coated vesicles during synaptic vesicle recycling. J. Cell Sci. 124 (1), 133–143.CrossRefPubMedGoogle Scholar
  6. 6.
    von Kleist L., Stahlschmidt W., Bulut H., Gromova K., Puchkov D., Robertson M. J., MacGregor K. A., Tomilin N., Pechstein A., Chau N., Chircop M., Sakoff J., von Kries J. P., Saenger W., Krausslich H. G., Shupliakov O., Robinson P. J., McCluskey A., Haucke V. 2011. Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition. Cell. 146 (9), 471–484.Google Scholar
  7. 7.
    Busch D. J., Oliphint P. A., Walsh R. B., Banks S. M., Woods W. S., George J. M., Morgan J. R. 2014. Acute increase of alpha-synuclein inhibits synaptic vesicle recycling evoked during intense stimulation. Mol. Biol. Cell. 25 (24), 3926–3941.CrossRefPubMedPubMedCentralGoogle Scholar
  8. 8.
    Xu J., Wu X. S., Sheng J., Zhang Z., Yue H. Y., Sun L., Sgobio C., Lin X., Peng S., Jin Y., Gan L., Cai H., Wu L. G. 2016. Alpha-synuclein mutation inhibits endocytosis at mammalian central nerve terminals. J. Neurosci. 36 (16), 4408–4414.CrossRefPubMedPubMedCentralGoogle Scholar
  9. 9.
    Sun Z., Gitler A. D. 2008. Discovery and characterization of three novel synuclein genes in zebrafish. Dev. Dyn. 237 (9), 2490–2495.CrossRefPubMedGoogle Scholar
  10. 10.
    Fusco G., De Simone A., Gopinath T., Vostrikov V., Vendruscolo M., Dobson C. M., Veglia G. 2014. Direct observation of the three regions in alpha-synuclein that determine its membrane-bound behaviour. Nat. Commun. 5, 3827.CrossRefPubMedPubMedCentralGoogle Scholar
  11. 11.
    Petrucci S., Ginevrino M., Valente E. M. 2016. Phenotypic spectrum of alpha-synuclein mutations: New insights from patients and cellular models. Parkinsonism Relat. Disord. 22 (Suppl. 1), 16–20.Google Scholar

Copyright information

© Pleiades Publishing, Ltd. 2018

Authors and Affiliations

  • O. V. Vorontsova
    • 1
  • E. E. Akkuratov
    • 2
  • O. M. Korenkova
    • 2
  • O. Shupliakov
    • 1
    • 2
    Email author
  1. 1.Department of NeuroscienceKarolinska InstitutetStockholmSweden
  2. 2.Institute of Translational BiomedicineSt.-Petersburg State UniversitySt. PetersburgRussia

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