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Prof Yuri Ushkaryov

Professor of Biological Sciences

Medway School of Pharmacy

 

Yuri Ushkaryov obtained BSc and MSc degrees with Distinction in Biochemistry from the Biology Department of the Moscow State University in 1979. He then joined the Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences, Moscow, where he began studying the mechanisms of neurotransmitter release using α-latrotoxin from black widow spider venom and participated in the isolation of the first α-latrotoxin receptor 1990.

In parallel, Yuri Ushkaryov learned molecular biology and in 1988 wrote a PhD thesis on the identification and sequencing of human genes encoding different isoforms of the Na+,K+-ATPase.

At the Shemyakin Institute, Yuri progressed to become research scientist, senior research scientist and leading scientist, serving also as the Head of Genetic Engineering Unit with a P3 Containment Facility.

In 1990 Yuri moved to the lab of Prof Thomas Südhof at the Howard Hughes Medical Institute, University of Texas Southwestern Medical Center in Dallas, Texas, where he cloned the first α-latrotoxin receptor, neurexin.

After winning a prestigious Wellcome Senior European Research Fellowship in 1993, Yuri set up his laboratory in the Department of Biochemistry at Imperial College London. Soon, the team discovered the Ca2+-independent α-latrotoxin receptor, a novel G-protein-coupled receptors (GPCRs), which they termed latrophilin. This successful work led to the award of a second Wellcome Senior European Research Fellowship in 1998.

In 2003, Yuri became a Reader in Molecular Neurobiology at the Division of Cell and Molecular Biology, Imperial College London, where he continued his studies of α-latrotoxin, latrophilin and its novel ligand, Lasso. He also took on a substantial teaching load, serving for many years as Convenor of the final year Molecular Neurobiology course and Director of the Masters by Research (MRes) in Biochemical Research postgraduate course. In 2008, he became Professor of Molecular Neurobiology, before moving to the Medway School of Pharmacy, University of Kent, in October 2011.

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Exocytosis of neurotransmitters is the main means of communication between neurons. Yuri Ushkaryov and his laboratory investigate how presynaptic receptors and trans-synaptic interactions regulate cytosolic Ca2+ and neurotransmitter secretion. The team has discovered latrophilin, an unusual adhesion G-protein-coupled receptor, which localises in the presynaptic terminals and controls neurotransmitter release. Recently, they also discovered an endogenous ligand of latrophilin, a large postsynaptic receptor, Lasso/teneurin-2. Lasso interacts with latrophilin across the synaptic cleft, and this link is important for functional maturation of synapses. Both proteins have been implicated in anxiety, attention deficit/hyperactivity disorder and bipolar disorder. Yuri's group is currently conducting an in-depth analysis of Lasso-latrophilin interaction and its role in synaptogenesis.

Current Projects

Unusual molecular architecture of latrophilins

Yuri’s laboratory continues studying latrophilins, novel G-protein-coupled receptors (GPCRs). Latrophilins belong to the family of "adhesion GPCRs", which have an unusual architecture: these proteins are natural chimeras of cell adhesion receptors and canonical GPCRs. Immediately after their synthesis - and in order to be transported to the cell surface - adhesion GPCRs are cleaved into the N-terminal fragment (NTF) and the C-terminal fragment (CTF), which correspond to the two structural domains. These fragments were initially thought to be inseparable. With this idea, came the misconception that adhesion GPCRs bind agonists, and signal, like the ordinary GPCRs.

However, Yuri's group has discovered a novel mechanism by which the adhesion GPCRs act (see Figure). NTF and CTF of latrophilin are not always found together. Both fragments are separately anchored in the membrane and can function as independent receptors in the plasma membrane. They are transported to distinct cell-surface compartments and can be separated by Ab patching. The two fragments are endocytosed separately. NTF localises in cell-adhesion protrusions and is probably engaged in interactions with neighbouring cells. Interestingly, NTF and CTF can also bind each other with high affinity. This interaction is induced when agonists (e.g. LTXN4C and antibodies) bind the NTF. This triggers CTF-mediated signalling, which leads to intracellular Ca2+ release.

current project fig 1.

A model of latrophilin structure and separate functioning of its fragments. Latrophilin is synthesised as a single protein, which is then proteolytically cleaved into two fragments in the endoplasmic reticulum (ER) or the Golgi complex (GC). Thereafter, the N-terminal fragment (NTF) and C-terminal fragment (CTF) behave largely independently on the cell membrane. However, they can also reassociate. Complex formation is induced by LTXN4C binding to NTF. This triggers signal transduction from CTF to intracellular Ca2+ stores.

Role of latrophilin in brain development

In their quest of the functions of this unusual receptor, Yuri's laboratory, in collaboration with Serguei Kozlov, USA, has generated a latrophilin 1 knockout mouse. Latrophilin knockout is embryonically lethal (1st Figure, left). However, during the breeding of heterozygous mice, a permissive haplotype (most likely lphn2P) was serendipitously selected that efficiently compensated for the lack of latrophilin 1 (1st Figure, right). Yet, even on the compensatory background, the lack of latrophilin 1 leads to a substantial decrease in transmitter release induced by the wild type α α-latrotoxin and complete loss of secretion stimulated by the non-pore-forming mutant LTXN4C (2nd Figure). These mice also demonstrate gene dose-dependent anxiety-like behaviour manifested in postnatal infanticide by the knockout mothers (Figure 3). Yuri's group is trying to genetically separate the two strains of lphn1-/- mice, homozygous for the permissive and non-permissive compensatory haplotype with the purpose of unequivocally identifying the compensatory gene and the pathways of brain development that are affected by latrophilin gene deletion.

current project fig 2.

Latrophilin controls release of neurotransmitters

The important role of latrophilin 1 in neurotransmitter release has been remarkably confirmed by the recent finding by Ushkaryov's group that a recombinant single-chain antibody, scFvA1, against latrophilin 1 can cause burst-like neurotransmitter exocytosis in mouse neuromuscular junctions, similar to that induced by LTXN4C (Figure). This ultimately proves that stimulation of latrophilin 1 can control or modulate presynaptic machinery for exocytosis. The team is working to improve the affinity of scFvA1 for latrophilin and uses mouse neuromuscular junctions and neuronal cultures to study its effect on exocytosis of different transmitters.

current project fig 3.

Latrophilin-Lasso interaction and its role in synapse formation and maturation

Latrophilin, a G-protein-coupled receptor, has an unusually long N-terminal domain containing cell-adhesion modules. It may be able of converting cell-cell contacts into intracellular signalling. Its structure also suggests that it may be involved in binding cell-surface receptors on adjacent cells. Indeed, we have recently identified a postsynaptic brain protein, Lasso, which binds latrophilin specifically. We currently study the consequences of disrupting this complex in subsequent synapse formation and functional maturation. For this purpose, we use primary cultures of hippocampal neurons. The expressed of either of these receptors on the cell surface is inhibited by respective RNAi, or their interaction is blocked by incubation with antibodies. Any alterations in synapse formation are assessed by immunostaining and electron microscopy. In addition, we measure the exocytotic activity of such modified synapses by monitoring the release of fluorescent dyes.

Acknowledgements:- Funding from: Wellcome Trust, Biotechnology and Biological Sciences Research Council, Royal Society.

current project fig 4.



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Selected earlier publications

  • Y.A. Ushkaryov, A.G. Petrenko, M. Geppert, T.C. Sudhof (1992) Neurexins: synaptic cell surface proteins related to the &alpha-latrotoxin receptor and laminin. Science, 257, 50-56
  • B.A. Davletov, O.G. Shamotienko, V.G. Lelianova, E.V. Grishin, Y.A. Ushkaryov (1996) Isolation and biochemical characterization of a Ca2+-independent α-latrotoxin-binding protein. J. Biol. Chem., 271, 23239-23245
  • V.G. Lelianova, B.A. Davletov, A. Sterling, M.A. Rahman, E.V. Grishin, N.F. Totty, Y.A. Ushkaryov (1997) α-Latrotoxin receptor, latrophilin, is a novel member of the secretin family of G protein-coupled receptors. J. Biol. Chem., 272, 21504-21508
  • B.A. Davletov, F.A. Meunier, A.C. Ashton, H. Matsushita, W.D. Hirst, V.G. Lelianova, G.P. Wilkin, J.O. Dolly, Y.A. Ushkaryov (1998) Vesicle exocytosis stimulated by α-latrotoxin is mediated by latrophilin and requires both external and stored Ca2+. EMBO J., 17, 3909-3920
  • E.V. Orlova, M.A. Rahman, B. Gowen, K.E. Volynski, A.C. Ashton, C. Manser, H.M. van, Y.A. Ushkaryov (2000) Structure of α-latrotoxin oligomers reveals that divalent cation-dependent tetramers form membrane pores. Nat. Struct. Biol., 7, 48-53
  • M. Capogna, K.E. Volynski, N.J. Emptage, Y.A. Ushkaryov (2003) The α-latrotoxin mutant LTXN4C enhances spontaneous and evoked transmitter release in CA3 pyramidal neurons. J. Neurosci., 23, 4044-4053
  • K.E. Volynski, M. Capogna, A.C. Ashton, D. Thomson, E.V. Orlova, C.F. Manser, R.R. Ribchester, Y.A. Ushkaryov (2003) Mutant a-latrotoxin (LTXN4C) does not form pores and causes secretion by receptor stimulation: this action does not require neurexins. J. Biol. Chem., 278, 31058-31066
  • Y.A. Ushkaryov, K.E. Volynski, A.C. Ashton (2004) The multiple actions of black widow spider toxins and their selective use in neurosecretion studies. Toxicon, 43, 527-542
  • K.E. Volynski, J.P. Silva, V.G. Lelianova, R.M. Atiqur, C. Hopkins, Y.A. Ushkaryov (2004) Latrophilin fragments behave as independent proteins that associate and signal on binding of LTXN4C. EMBO J., 23, 4423-4433
  • A.C. Ashton, Y.A. Ushkaryov (2005) Properties of synaptic vesicle pools in mature central nerve terminals. J. Biol. Chem., 280, 37278-37288
  • O. Berninghausen, M.A. Rahman, J.P. Silva, B. Davletov, C. Hopkins, Y.A. Ushkaryov (2007) Neurexin Ib and neuroligin are localized on opposite membranes in mature central synapses. J. Neurochem., 103, 1855-1863

Recent publications

  • J.P. Silva, V. Lelianova, C. Hopkins, K.E. Volynski, Y. Ushkaryov (2009) Functional cross-interaction of the fragments produced by the cleavage of distinct adhesion G-protein-coupled receptors. J. Biol. Chem., 284, 6495-6506
  • F. Darios, D. Niranjan, E. Ferrari, F. Zhang, M. Soloviev, A. Rummel, H. Bigalke, J. Suckling, Y. Ushkaryov, N. Naumenko, A. Shakirzyanova, R. Giniatullin, E. Maywood, M. Hastings, T. Binz, B. Davletov (2010) SNARE tagging allows stepwise assembly of a multimodular medicinal toxin. Proc. Natl. Acad. Sci. U.S.A., 107, 18197-18201
  • J.P. Silva, V.G. Lelianova, Y.S. Ermolyuk, N. Vysokov, P.G. Hitchen, O. Berninghausen, M.A. Rahman, A. Zangrandi, S. Fidalgo, A.G. Tonevitsky, A. Dell, K.E. Volynski, Y.A. Ushkaryov (2011) Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities. Proc. Natl. Acad. Sci. U.S.A., 108, 12113-12118
  • B. Davletov, E. Ferrari, Y.A. Ushkaryov (2012) Presynaptic neurotoxins: an expanding array of natural and modified molecules. Cell Calcium, In press
  • K. Volynski, J. Suckling, D. Thomson, R.R. Ribchester, Y.A. Ushkaryov (2012) High frequency kiss-and-run exocytosis at mammalian neuromuscular junctions: stimulus dependence. In preparation

Book chapters

  • Secretagogue activity of trachynilysin, a neurotoxic protein isolated from stonefish (Synanceia trachynis) venom (F.A. Meunier, G. Ouanounou, C. Mattei, P. Chameau, C. Colasante, Y.A. Ushkaryov, J.O. Dolly, A.S. Kreger, J. Molgó). In Handb. Neurotoxicol. vol. I, Edited by E.J. Massaro, Human Press, Totowa, NJ, 595-616 (2001)
  • α-Latrotoxin and its receptors (Y.A. Ushkaryov, A. Rohou, S. Sugita). In Pharmacology of neurotransmitter release: Handb. Exp. Pharmacol. 184, Edited by T.C. Südhof, K. Starke, Springer, Berlin, 171-206 (2008)
  • The latrophilins, "split-personality" receptors (J.P. Silva, Y.A. Ushkaryov). In Adhesion-GPCRs: Structure to Function, Edited by S. Iona, M. Stacey, Landes Bioscience - Springer, Austin, TX, 59-75 (2010).

Full list of publications

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  • Sokolov, I. Ushkarev, A. Grasso, E.V. Grishin, V.K. Lishko (1983) [Interaction of black widow spider toxin with bilayer phospholipid membranes]. Ukr. Biokhim. Zh., 55, 179-184
  • Ovchinnikov, G.S. Monastyrskaia, N.E. Broude, I. Ushkarev, G.M. Dolganov (1986) [Human Na+,K+-ATPase genes. Nucleotide sequence encoding the C-terminal region of the α-subunit]. Dokl. Akad. Nauk SSSR, 287, 1251-1254
  • Ushkarev, E.V. Grishin (1986) [Neurotoxin of the black widow spider and its interaction with receptors from the rat brain]. Bioorg. Khim., 12, 71-80
  • Y. Ovchinnikov, G.S. Monastyrskaya, N.E. Broude, R.L. Allikmets, Y. Ushkaryov, A.M. Melkov, Y. Smirnov, I.V. Malyshev, I.E. Dulubova, K.E. Petrukhin (1987) The family of human Na+,K+-ATPase genes. A partial nucleotide sequence related to the α-subunit. FEBS Lett., 213, 73-80
  • E.D. Sverdlov, G.S. Monastyrskaia, N.E. Broude, I. Ushkarev, R.L. Allikmets (1987) [The family of human Na+,K+-ATPase genes. At least 5 genes and/or pseudogenes homologous to α-subunit]. Dokl. Akad. Nauk SSSR, 294, 734-738
  • E.D. Sverdlov, G.S. Monastyrskaia, N.E. Broude, I. Ushkarev, A.M. Melkov (1987) [The family of human Na+,K+-ATPase genes. Structure of the gene for isozyme αIII]. Dokl. Akad. Nauk SSSR, 297, 1488-1494
  • E.D. Sverdlov, G.S. Monastyrskaya, N.E. Broude, Y. Ushkaryov, R.L. Allikmets, A.M. Melkov, Y. Smirnov, I.V. Malyshev, I.E. Dulobova, K.E. Petrukhin (1987) The family of human Na+,K+-ATPase genes. II. No less than five genes and/or pseudogenes related to the a-subunit. FEBS Lett., 217, 275-278
  • V.E. Sverdlov, N.E. Broude, E.D. Sverdlov, A.V. Grishin, K.E. Petrukhin, Y. Ushkaryov, N.N. Modyanov, Y. Ovchinnikov (1987) [Genomic DNAs from various human organs give different restriction fragments hybridizing with cDNA of Na+,K+-ATPase α-subunit]. Dokl. Akad. Nauk SSSR, 296, 236-238
  • Y. Ovchinnikov, G.S. Monastyrskaya, N.E. Broude, Y. Ushkaryov, A.M. Melkov, Y. Smirnov, I.V. Malyshev, R.L. Allikmets, M.B. Kostina, I.E. Dulubova (1988) Family of human Na+, K+-ATPase genes. Structure of the gene for the catalytic subunit (αIII-form) and its relationship with structural features of the protein. FEBS Lett., 233, 87-94
  • E.D. Sverdlov, D.A. Bessarab, I.V. Malyshev, K.E. Petrukhin, Y. Smirnov, Y. Ushkaryov, G.S. Monastyrskaya, N.E. Broude, N.N. Modyanov (1989) Family of human Na+,K+-ATPase genes. Structure of the putative regulatory region of the α+-gene. FEBS Lett., 244, 481-483
  • Y. Ushkaryov, G.S. Monastyrskaya, N.E. Broude, N.N. Nikiforova, D.A. Bessarab, M.Y. Orlova, K.E. Petrukhin, N.N. Modyanov, E.D. Sverdlov (1989) Human Na+,K+-ATPase genes. β-Subunit gene family contains at least one gene and one pseudogene. FEBS Lett., 257, 439-442
  • A.G. Petrenko, V.A. Kovalenko, O.G. Shamotienko, I.N. Surkova, T.A. Tarasyuk, Y. Ushkaryov, E.V. Grishin (1990) Isolation and properties of the α-latrotoxin receptor. EMBO J., 9, 2023-2027
  • A.G. Petrenko, I.N. Surkova, O.G. Shamotienko, V.A. Kovalenko, V.N. Krasnoperov, L.A. Tret'iakov, I. Ushkarev, E.V. Grishin (1990) [Study of the receptor for black widow spider neurotoxin. II. Isolation and characteristics of the receptor from bovine brain membranes]. Bioorg. Khim., 16, 158-165
  • Ushkarev, G.S. Monastyrskaia, N.E. Broude, N.N. Nikiforova, D.A. Bessarab, M.I. Orlova, K.E. Petrukhin, N.N. Modianov, E.D. Sverdlov (1990) [Human Na+,K+-ATPase genes. Gene family and pseudogene for β-subunit]. Dokl. Akad. Nauk SSSR, 312, 495-499
  • A.G. Petrenko, M.S. Perin, B.A. Davletov, Y.A. Ushkaryov, M. Geppert, T.C. Sudhof (1991) Binding of synaptotagmin to the α-latrotoxin receptor implicates both in synaptic vesicle exocytosis. Nature, 353, 65-68
  • T.C. Sudhof, C.L. Newton, B.T. Archer, III, Y.A. Ushkaryov, G.A. Mignery (1991) Structure of a novel InsP3 receptor. EMBO J., 10, 3199-3206
  • M. Geppert, Y.A. Ushkaryov, Y. Hata, B. Davletov, A.G. Petrenko, T.C. Sudhof (1992) Neurexins. Cold Spring Harb. Symp. Quant. Biol., 57, 483-490
  • Y.A. Ushkaryov, A.G. Petrenko, M. Geppert, T.C. Sudhof (1992) Neurexins: synaptic cell surface proteins related to the α-latrotoxin receptor and laminin. Science, 257, 50-56
  • H.T. McMahon, Y.A. Ushkaryov, L. Edelmann, E. Link, T. Binz, H. Niemann, R. Jahn, T.C. Sudhof (1993) Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein. Nature, 364, 346-349
  • A.G. Petrenko, V.D. Lazaryeva, M. Geppert, T.A. Tarasyuk, C. Moomaw, A.V. Khokhlatchev, Y.A. Ushkaryov, C. Slaughter, I.V. Nasimov, T.C. Sudhof (1993) Polypeptide composition of the α-latrotoxin receptor. High affinity binding protein consists of a family of related high molecular weight polypeptides complexed to a low molecular weight protein. J. Biol. Chem., 268, 1860-1867
  • Y.A. Ushkaryov, T.C. Sudhof (1993) Neurexin IIIa: extensive alternative splicing generates membrane-bound and soluble forms. Proc. Natl. Acad. Sci. U. S. A., 90, 6410-6414
  • J.M. Sontag, E.M. Fykse, Y. Ushkaryov, J.P. Liu, P.J. Robinson, T.C. Sudhof (1994) Differential expression and regulation of multiple dynamins. J. Biol. Chem., 269, 4547-4554
  • Y.A. Ushkaryov, Y. Hata, K. Ichtchenko, C. Moomaw, S. Afendis, C.A. Slaughter, T.C. Sudhof (1994) Conserved domain structure of β-neurexins. Unusual cleaved signal sequences in receptor-like neuronal cell-surface proteins. J. Biol. Chem., 269, 11987-11992
  • B. Ullrich, Y.A. Ushkaryov, T.C. Sudhof (1995) Cartography of neurexins: more than 1000 isoforms generated by alternative splicing and expressed in distinct subsets of neurons. Neuron, 14, 497-507
  • B.A. Davletov, O.G. Shamotienko, V.G. Lelianova, E.V. Grishin, Y.A. Ushkaryov (1996) Isolation and biochemical characterization of a Ca2+-independent α-latrotoxin-binding protein. J. Biol. Chem., 271, 23239-23245
  • V.G. Lelianova, B.A. Davletov, A. Sterling, M.A. Rahman, E.V. Grishin, N.F. Totty, Y.A. Ushkaryov (1997) α-Latrotoxin receptor, latrophilin, is a novel member of the secretin family of G protein-coupled receptors. J. Biol. Chem., 272, 21504-21508
  • P. McIntosh, A.P. Southan, S. Akhtar, C. Sidera, Y. Ushkaryov, J.O. Dolly, B. Robertson (1997) Modification of rat brain Kv1.4 channel gating by association with accessory Kvβ1.1 and β2.1 subunits. Pflugers Arch., 435, 43-54
  • B.A. Davletov, F.A. Meunier, A.C. Ashton, H. Matsushita, W.D. Hirst, V.G. Lelianova, G.P. Wilkin, J.O. Dolly, Y.A. Ushkaryov (1998) Vesicle exocytosis stimulated by α-latrotoxin is mediated by latrophilin and requires both external and stored Ca2+. EMBO J., 17, 3909-3920
  • J. Lang, Y. Ushkaryov, A. Grasso, C.B. Wollheim (1998) Ca2+-independent insulin exocytosis induced by α-latrotoxin requires latrophilin, a G protein-coupled receptor. EMBO J., 17, 648-657
  • R.R. Ribchester, D. Thomson, L.J. Haddow, Y.A. Ushkaryov (1998) Enhancement of spontaneous transmitter release at neonatal mouse neuromuscular junctions by the glial cell line-derived neurotrophic factor (GDNF). J. Physiol., 512 ( Pt 3), 635-641
  • H. Matsushita, V.G. Lelianova, Y.A. Ushkaryov (1999) The latrophilin family: multiply spliced G protein-coupled receptors with differential tissue distribution. FEBS Lett., 443, 348-352
  • M.A. Rahman, A.C. Ashton, F.A. Meunier, B.A. Davletov, J.O. Dolly, Y.A. Ushkaryov (1999) Norepinephrine exocytosis stimulated by α-latrotoxin requires both external and stored Ca2+ and is mediated by latrophilin, G proteins and phospholipase C. Philos. Trans. R. Soc. Lond. B Biol. Sci., 354, 379-386
  • K.E. Volynski, E.D. Nosyreva, Y.A. Ushkaryov, E.V. Grishin (1999) Functional expression of α-latrotoxin in baculovirus system. FEBS Lett., 442, 25-28
  • A.C. Ashton, M.A. Rahman, K.E. Volynski, C. Manser, E.V. Orlova, H. Matsushita, B.A. Davletov, H.M. van, E.V. Grishin, Y.A. Ushkaryov (2000) Tetramerisation of α-latrotoxin by divalent cations is responsible for toxin-induced non-vesicular release and contributes to the Ca2+-dependent vesicular exocytosis from synaptosomes. Biochimie, 82, 453-468
  • E.V. Orlova, M.A. Rahman, B. Gowen, K.E. Volynski, A.C. Ashton, C. Manser, H.M. van, Y.A. Ushkaryov (2000) Structure of α-latrotoxin oligomers reveals that divalent cation-dependent tetramers form membrane pores. Nat. Struct. Biol., 7, 48-53
  • C. Van Renterghem, C. Iborra, N. Martin-Moutot, V. Lelianova, Y. Ushkaryov, M. Seagar (2000) α-Latrotoxin forms Ca2+-permeable membrane pores via interactions with latrophilin or neurexin. Eur. J. Neurosci., 12, 3953-3962
  • K.E. Volynski, F.A. Meunier, V.G. Lelianova, E.E. Dudina, T.M. Volkova, M.A. Rahman, C. Manser, E.V. Grishin, J.O. Dolly, R.H. Ashley, Y.A. Ushkaryov (2000) Latrophilin, neurexin, and their signaling-deficient mutants facilitate α-latrotoxin insertion into membranes but are not involved in pore formation. J. Biol. Chem., 275, 41175-41183
  • A.C. Ashton, K.E. Volynski, V.G. Lelianova, E.V. Orlova, R.C. Van, M. Canepari, M. Seagar, Y.A. Ushkaryov (2001) α-Latrotoxin, acting via two Ca2+-dependent pathways, triggers exocytosis of two pools of synaptic vesicles. J. Biol. Chem., 276, 44695-44703
  • F.A. Meunier, G. Ouanounou, C. Mattei, P. Chameau, C. Colasante, Y.A. Ushkaryov, J.O. Dolly, A.S. Kreger, J. Molgó (2001) Secretagogue activity of trachynilysin, a neurotoxic protein isolated from stonefish (Synanceia trachynis) venom. In Handb. Neurotoxicol. vol. I, Edited by E.J. Massaro, Human Press, Totowa, NJ, 595-616
  • Y. Ushkaryov (2002) α-Latrotoxin: from structure to some functions. Toxicon, 40, 1-5
  • M. Capogna, K.E. Volynski, N.J. Emptage, Y.A. Ushkaryov (2003) The α-latrotoxin mutant LTXN4C enhances spontaneous and evoked transmitter release in CA3 pyramidal neurons. J. Neurosci., 23, 4044-4053
  • G.M. O'Hanlon, P.D. Humphreys, R.S. Goldman, S.K. Halstead, R.W. Bullens, J.J. Plomp, Y. Ushkaryov, H.J. Willison (2003) Calpain inhibitors protect against axonal degeneration in a model of anti-ganglioside antibody-mediated motor nerve terminal injury. Brain, 126, 2497-2509
  • K.E. Volynski, M. Capogna, A.C. Ashton, D. Thomson, E.V. Orlova, C.F. Manser, R.R. Ribchester, Y.A. Ushkaryov (2003) Mutant α-latrotoxin (LTXN4C) does not form pores and causes secretion by receptor stimulation: this action does not require neurexins. J. Biol. Chem., 278, 31058-31066
  • Y.A. Ushkaryov, K.E. Volynski, A.C. Ashton (2004) The multiple actions of black widow spider toxins and their selective use in neurosecretion studies. Toxicon, 43, 527-542
  • K.E. Volynski, J.P. Silva, V.G. Lelianova, R.M. Atiqur, C. Hopkins, Y.A. Ushkaryov (2004) Latrophilin fragments behave as independent proteins that associate and signal on binding of LTXN4C. EMBO J., 23, 4423-4433
  • A.C. Ashton, Y.A. Ushkaryov (2005) Properties of synaptic vesicle pools in mature central nerve terminals. J. Biol. Chem., 280, 37278-37288
  • J. Liu, Q. Wan, X. Lin, H. Zhu, K. Volynski, Y. Ushkaryov, T. Xu (2005) α-Latrotoxin modulates the secretory machinery via receptor-mediated activation of protein kinase C. Traffic, 6, 756-765
  • S. Lajus, P. Vacher, D. Huber, M. Dubois, M.N. Benassy, Y. Ushkaryov, J. Lang (2006) a-Latrotoxin induces exocytosis by inhibition of voltage-dependent K+ channels and by stimulation of L-type Ca2+ channels via latrophilin in b-cells. J. Biol. Chem., 281, 5522-5531
  • O. Berninghausen, M.A. Rahman, J.P. Silva, B. Davletov, C. Hopkins, Y.A. Ushkaryov (2007) Neurexin Ib and neuroligin are localized on opposite membranes in mature central synapses. J. Neurochem., 103, 1855-1863
  • Rohou, J. Nield, Y.A. Ushkaryov (2007) Insecticidal toxins from black widow spider venom. Toxicon, 49, 531-549
  • Y.A. Ushkaryov, A. Rohou, S. Sugita (2008) α-Latrotoxin and its receptors. In Handb. Exp. Pharmacol, Edited byT.C. Südhof, K. Starke, Springer, Berlin, 171-206
  • I.I. Davydov, S. Fidalgo, S.A. Khaustova, V.G. Lelyanova, E.S. Grebenyuk, Y.A. Ushkaryov, A.G. Tonevitsky (2009) Prediction of epitopes in closely related proteins using a new algorithm. Bull. Exp. Biol. Med., 148, 869-873
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