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Volumn 288, Issue 22, 2013, Pages 15888-15899

Water-soluble LYNX1 residues important for interaction with muscle-type and/or neuronal nicotinic receptors

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINE-BINDING PROTEINS; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORS; IRREVERSIBLE INHIBITIONS; LIGAND BINDING DOMAIN; NICOTINIC ACETYLCHOLINE RECEPTORS; NICOTINIC ACETYLCHOLINE RECEPTORS (NACHR); PATCH CLAMP TECHNIQUE; TRANS-MEMBRANE DOMAINS;

EID: 84878423730     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.436576     Document Type: Article
Times cited : (45)

References (41)
  • 1
    • 0033136270 scopus 로고    scopus 로고
    • lynx1, an endogenous toxin-like modulator of nicotinic acetylcholine receptors in the mammalian CNS
    • DOI 10.1016/S0896-6273(00)80757-6
    • Miwa, J. M., Ibanez-Tallon, I., Crabtree, G. W., Sánchez, R., Sali, A., Role, L. W., and Heintz, N. (1999) lynx1, an endogenous toxin-like modulator of nicotinic acetylcholine receptors in the mammalian CNS. Neuron 23, 105-114 (Pubitemid 29262468)
    • (1999) Neuron , vol.23 , Issue.1 , pp. 105-114
    • Miwa, J.M.1    Ibanez-Tallon, I.2    Crabtree, G.W.3    Sanchez, R.4    Sali, A.5    Role, L.W.6    Heintz, N.7
  • 2
    • 79953805191 scopus 로고    scopus 로고
    • Neural systems governed by nicotinic acetylcholine receptors: Emerging hypotheses
    • Miwa, J. M., Freedman, R., and Lester, H. A. (2011) Neural systems governed by nicotinic acetylcholine receptors: emerging hypotheses. Neuron 70, 20-33
    • (2011) Neuron , vol.70 , pp. 20-33
    • Miwa, J.M.1    Freedman, R.2    Lester, H.A.3
  • 4
    • 0037075542 scopus 로고    scopus 로고
    • Novel modulation of neuronal nicotinic acetylcholine receptors by association with the endogenous prototoxin lynx1
    • DOI 10.1016/S0896-6273(02)00632-3
    • Ibañez-Tallon, I., Miwa, J. M., Wang, H. L., Adams, N. C., Crabtree, G. W., Sine, S. M., and Heintz, N. (2002) Novel modulation of neuronal nicotinic acetylcholine receptors by association with the endogenous prototoxin lynx1. Neuron 33, 893-903 (Pubitemid 34246355)
    • (2002) Neuron , vol.33 , Issue.6 , pp. 893-903
    • Ibanez-Tallon, I.1    Miwa, J.M.2    Wang, H.-L.3    Adams, N.C.4    Crabtree, G.W.5    Sine, S.M.6    Heintz, N.7
  • 7
    • 78649442213 scopus 로고    scopus 로고
    • Lynx1, a cholinergic brake, limits plasticity in adult visual cortex
    • Morishita, H., Miwa, J. M., Heintz, N., and Hensch, T. K. (2010) Lynx1, a cholinergic brake, limits plasticity in adult visual cortex. Science 330, 1238-1240
    • (2010) Science , vol.330 , pp. 1238-1240
    • Morishita, H.1    Miwa, J.M.2    Heintz, N.3    Hensch, T.K.4
  • 9
    • 72449189587 scopus 로고    scopus 로고
    • Prostate stem cell antigen is an endogenous lynx1-like prototoxin that antagonizes α7-containing nicotinic receptors and prevents programmed cell death of parasympathetic neurons
    • Hruska, M., Keefe, J., Wert, D., Tekinay, A. B., Hulce, J. J., Ibañez-Tallon, I., and Nishi, R. (2009) Prostate stem cell antigen is an endogenous lynx1-like prototoxin that antagonizes α7-containing nicotinic receptors and prevents programmed cell death of parasympathetic neurons. J. Neurosci. 29, 14847-14854
    • (2009) J. Neurosci. , vol.29 , pp. 14847-14854
    • Hruska, M.1    Keefe, J.2    Wert, D.3    Tekinay, A.B.4    Hulce, J.J.5    Ibañez-Tallon, I.6    Nishi, R.7
  • 10
    • 84867711270 scopus 로고    scopus 로고
    • The ly-6 protein, lynx1, is an endogenous inhibitor of nicotinic signaling in airway epithelium
    • Fu, X. W., Rekow, S. S., and Spindel, E. R. (2012) The ly-6 protein, lynx1, is an endogenous inhibitor of nicotinic signaling in airway epithelium. Am. J. Physiol. Lung Cell. Mol. Physiol. 303, L661-668
    • (2012) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.303
    • Fu, X.W.1    Rekow, S.S.2    Spindel, E.R.3
  • 11
    • 1642450641 scopus 로고    scopus 로고
    • Snake and snail toxins acting on nicotinic acetylcholine receptors: Fundamental aspects and medical applications
    • DOI 10.1016/S0014-5793(03)01454-6
    • Tsetlin, V. I., and Hucho, F. (2004) Snake and snail toxins acting on nicotinic acetylcholine receptors: fundamental aspects and medical applications. FEBS Lett. 557, 9-13 (Pubitemid 38115861)
    • (2004) FEBS Letters , vol.557 , Issue.1-3 , pp. 9-13
    • Tsetlin, V.I.1    Hucho, F.2
  • 12
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • Karlin, A. (2002) Emerging structure of the nicotinic acetylcholine receptors. Nat. Rev. Neurosci. 3, 102-114
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 102-114
    • Karlin, A.1
  • 13
    • 68349133608 scopus 로고    scopus 로고
    • Polypeptide and peptide toxins, magnifying lenses for binding sites in nicotinic acetylcholine receptors
    • Tsetlin, V., Utkin, Y., and Kasheverov, I. (2009) Polypeptide and peptide toxins, magnifying lenses for binding sites in nicotinic acetylcholine receptors. Biochem. Pharmacol. 78, 720-731
    • (2009) Biochem. Pharmacol. , vol.78 , pp. 720-731
    • Tsetlin, V.1    Utkin, Y.2    Kasheverov, I.3
  • 14
    • 18444411922 scopus 로고    scopus 로고
    • Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake α-neurotoxins and nicotinic receptors
    • DOI 10.1038/sj.emboj.7600620
    • Bourne, Y., Talley, T. T., Hansen, S. B., Taylor, P., and Marchot, P. (2005) Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake α-neurotoxins and nicotinic receptors. EMBO J. 24, 1512-1522 (Pubitemid 40646442)
    • (2005) EMBO Journal , vol.24 , Issue.8 , pp. 1512-1522
    • Bourne, Y.1    Talley, T.T.2    Hansen, S.B.3    Taylor, P.4    Marchot, P.5
  • 15
    • 34547520128 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain of nAChR α1 bound to α-bungarotoxin at 1.94 A resolution
    • DOI 10.1038/nn1942, PII NN1942
    • Dellisanti, C. D., Yao, Y., Stroud, J. C., Wang, Z. Z., and Chen, L. (2007) Crystal structure of the extracellular domain of nAChR α1 bound to α-bungarotoxin at 1.94 A resolution. Nat. Neurosci. 10, 953-962 (Pubitemid 47185209)
    • (2007) Nature Neuroscience , vol.10 , Issue.8 , pp. 953-962
    • Dellisanti, C.D.1    Yao, Y.2    Stroud, J.C.3    Wang, Z.-Z.4    Chen, L.5
  • 16
    • 14844323974 scopus 로고    scopus 로고
    • A chimera encoding the fusion of an acetylcholine-binding protein to an ion channel is stabilized in a state close to the desensitized form of ligand-gated ion channels
    • DOI 10.1016/j.crvi.2004.11.004, PII S1631069104002665
    • Grutter, T., Prado de Carvalho, L., Virginie, D., Taly, A., Fischer, M., and Changeux, J. P. (2005) A chimera encoding the fusion of an acetylcholine-binding protein to an ion channel is stabilized in a state close to the desensitized form of ligand-gated ion channels. C. R. Biol. 328, 223-234 (Pubitemid 40347868)
    • (2005) Comptes Rendus - Biologies , vol.328 , Issue.3 , pp. 223-234
    • Grutter, T.1    De Carvalho, L.P.2    Dufresne, V.3    Taly, A.4    Fischer, M.5    Changeux, J.-P.6
  • 18
    • 77957688441 scopus 로고    scopus 로고
    • Genetically encoded Cl-Sensor as a tool for monitoring of Cl-dependent processes in small neuronal compartments
    • Waseem, T., Mukhtarov, M., Buldakova, S., Medina, I., and Bregestovski, P. (2010) Genetically encoded Cl-Sensor as a tool for monitoring of Cl-dependent processes in small neuronal compartments. J. Neurosci. Methods 193, 14-23
    • (2010) J. Neurosci. Methods , vol.193 , pp. 14-23
    • Waseem, T.1    Mukhtarov, M.2    Buldakova, S.3    Medina, I.4    Bregestovski, P.5
  • 20
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • Unwin, N. (2005) Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J. Mol. Biol. 346, 967-989
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 21
    • 82755162931 scopus 로고    scopus 로고
    • Creating an α7 nicotinic acetylcholine recognition domain from the acetylcholine-binding protein: Crystallographic and ligand selectivity analyses
    • Nemecz, A., and Taylor, P. (2011) Creating an α7 nicotinic acetylcholine recognition domain from the acetylcholine-binding protein: crystallographic and ligand selectivity analyses. J. Biol. Chem. 286, 42555-42565
    • (2011) J. Biol. Chem. , vol.286 , pp. 42555-42565
    • Nemecz, A.1    Taylor, P.2
  • 22
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali, A., and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 24
    • 0036729768 scopus 로고    scopus 로고
    • Comparative pharmacology of rat and human α7 nAChR conducted with net charge analysis
    • DOI 10.1038/sj.bjp.0704833
    • Papke, R. L., and Porter Papke, J. K. (2002) Comparative pharmacology of rat and human α7 nAChR conducted with net charge analysis. Br. J. Pharmacol. 137, 49-61 (Pubitemid 34983463)
    • (2002) British Journal of Pharmacology , vol.137 , Issue.1 , pp. 49-61
    • Papke, R.L.1    Porter, P.J.K.2
  • 25
    • 57849127303 scopus 로고    scopus 로고
    • Characterization of compounds on nicotinic acetylcholine receptor α7 channels using higher throughput electrophysiology
    • Friis, S., Mathes, C., Sunesen, M., Bowlby, M. R., and Dunlop, J. (2009) Characterization of compounds on nicotinic acetylcholine receptor α7 channels using higher throughput electrophysiology. J. Neurosci. Methods 177, 142-148
    • (2009) J. Neurosci. Methods , vol.177 , pp. 142-148
    • Friis, S.1    Mathes, C.2    Sunesen, M.3    Bowlby, M.R.4    Dunlop, J.5
  • 26
    • 0027772476 scopus 로고
    • Chimaeric nicotinic-serotonergic receptor combines distinct ligand binding and channel specificities
    • Eiselé, J. L., Bertrand, S., Galzi, J. L., Devillers- Thiéry, A., Changeux, J. P., and Bertrand, D. (1993) Chimaeric nicotinic-serotonergic receptor combines distinct ligand binding and channel specificities. Nature 366, 479-483
    • (1993) Nature , vol.366 , pp. 479-483
    • Eiselé, J.L.1    Bertrand, S.2    Galzi, J.L.3    Devillers-Thiéry, A.4    Changeux, J.P.5    Bertrand, D.6
  • 27
    • 27544485478 scopus 로고    scopus 로고
    • 3A receptors
    • DOI 10.1124/mol.105.015438
    • Rayes, D., Spitzmaul, G., Sine, S. M., and Bouzat, C. (2005) Single-channel kinetic analysis of chimeric α7-5HT3A receptors. Mol. Pharmacol. 68, 1475-1483 (Pubitemid 41540003)
    • (2005) Molecular Pharmacology , vol.68 , Issue.5 , pp. 1475-1483
    • Rayes, D.1    Spitzmaul, G.2    Sine, S.M.3    Bouzat, C.4
  • 30
    • 84868347589 scopus 로고    scopus 로고
    • Enhancement in motor learning through genetic manipulation of the Lynx1 gene
    • Miwa, J. M., and Walz, A. (2012) Enhancement in motor learning through genetic manipulation of the Lynx1 gene. PLoS One 7, e43302
    • (2012) PLoS One , vol.7
    • Miwa, J.M.1    Walz, A.2
  • 32
    • 0028934293 scopus 로고
    • Genetic engineering of snake toxins. The functional site of Erabutoxin a, as delineated by site-directed mutagenesis, includes variant residues
    • Trémeau, O., Lemaire, C., Drevet, P., Pinkasfeld, S., Ducancel, F., Boulain, J. C., and Ménez, A. (1995) Genetic engineering of snake toxins. The functional site of Erabutoxin a, as delineated by site-directed mutagenesis, includes variant residues. .J. Biol. Chem. 270, 9362-9369
    • (1995) J. Biol. Chem. , vol.270 , pp. 9362-9369
    • Trémeau, O.1    Lemaire, C.2    Drevet, P.3    Pinkasfeld, S.4    Ducancel, F.5    Boulain, J.C.6    Ménez, A.7
  • 33
    • 77956063164 scopus 로고    scopus 로고
    • Structure, function and evolution of three-finger toxins: Mini proteins with multiple targets
    • Kini, R. M., and Doley, R. (2010) Structure, function and evolution of three-finger toxins: mini proteins with multiple targets. Toxicon 56, 855-867
    • (2010) Toxicon , vol.56 , pp. 855-867
    • Kini, R.M.1    Doley, R.2
  • 34
    • 67649365444 scopus 로고    scopus 로고
    • Loop 3 of short neurotoxin II is an additional interaction site with membrane-bound nicotinic acetylcholine receptor as detected by solid-state NMR spectroscopy
    • Krabben, L., van Rossum, B. J., Jehle, S., Bocharov, E., Lyukmanova, E. N., Schulga, A. A., Arseniev, A., Hucho, F., and Oschkinat, H. (2009) Loop 3 of short neurotoxin II is an additional interaction site with membrane-bound nicotinic acetylcholine receptor as detected by solid-state NMR spectroscopy. J. Mol. Biol. 390, 662-671
    • (2009) J. Mol. Biol. , vol.390 , pp. 662-671
    • Krabben, L.1    Van Rossum, B.J.2    Jehle, S.3    Bocharov, E.4    Lyukmanova, E.N.5    Schulga, A.A.6    Arseniev, A.7    Hucho, F.8    Oschkinat, H.9
  • 35
    • 0037124025 scopus 로고    scopus 로고
    • Candoxin, a novel toxin from Bungarus candidus, is a reversible antagonist of muscle (αβγδ) but a poorly reversible antagonist of neuronal α7 nicotinic acetylcholine receptors
    • DOI 10.1074/jbc.M111152200
    • Nirthanan, S., Charpantier, E., Gopalakrishnakone, P., Gwee, M. C., Khoo, H. E., Cheah, L. S., Bertrand, D., and Kini, R. M. (2002) Candoxin, a novel toxin from Bungarus candidus, is a reversible antagonist of muscle (αβγδ) but a poorly reversible antagonist of neuronal α7 nicotinic acetylcholine receptors. J. Biol. Chem. 277, 17811-17820 (Pubitemid 34967589)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.20 , pp. 17811-17820
    • Nirthanan, S.1    Charpantier, E.2    Gopalakrishnakone, P.3    Gwee, M.C.E.4    Khoo, H.-E.5    Cheah, L.-S.6    Bertrand, D.7    Manjunatha, K.R.8
  • 36
    • 0035844124 scopus 로고    scopus 로고
    • "Weak toxin" from Naja kaouthia is a nontoxic antagonist of α7 and muscle-type nicotinic acetylcholine receptors
    • Utkin, Y. N., Kukhtina, V. V., Kryukova, E. V., Chiodini, F., Bertrand, D., Methfessel, C., and Tsetlin, V. I. (2001) "Weak toxin" from Naja kaouthia is a nontoxic antagonist of α7 and muscle-type nicotinic acetylcholine receptors. J. Biol. Chem. 276, 15810-15815
    • (2001) J. Biol. Chem. , vol.276 , pp. 15810-15815
    • Utkin, Y.N.1    Kukhtina, V.V.2    Kryukova, E.V.3    Chiodini, F.4    Bertrand, D.5    Methfessel, C.6    Tsetlin, V.I.7
  • 37
    • 69449092043 scopus 로고    scopus 로고
    • Weak toxin WTX from Naja kaouthia cobra venom interacts with both nicotinic and muscarinic acetylcholine receptors
    • Mordvintsev, D. Y., Polyak, Y. L., Rodionov, D. I., Jakubik, J., Dolezal, V., Karlsson, E., Tsetlin, V. I., and Utkin, Y. N. (2009) Weak toxin WTX from Naja kaouthia cobra venom interacts with both nicotinic and muscarinic acetylcholine receptors. FEBS J. 276, 5065-5075
    • (2009) FEBS J. , vol.276 , pp. 5065-5075
    • Mordvintsev, D.Y.1    Polyak, Y.L.2    Rodionov, D.I.3    Jakubik, J.4    Dolezal, V.5    Karlsson, E.6    Tsetlin, V.I.7    Utkin, Y.N.8
  • 38
    • 79960164372 scopus 로고    scopus 로고
    • Protein-protein complex structure predictions by multimeric threading and template recombination
    • Mukherjee, S., and Zhang, Y. (2011) Protein-protein complex structure predictions by multimeric threading and template recombination. Structure 19, 955-966
    • (2011) Structure , vol.19 , pp. 955-966
    • Mukherjee, S.1    Zhang, Y.2
  • 40
    • 0041843714 scopus 로고    scopus 로고
    • α-Bungarotoxin binding to acetylcholine receptor membranes studied by low angle x-ray diffraction
    • Young, H. S., Herbette, L. G., and Skita, V. (2003) α-bungarotoxin binding to acetylcholine receptor membranes studied by low angle X-ray diffraction. Biophys. J. 85, 943-953 (Pubitemid 36909658)
    • (2003) Biophysical Journal , vol.85 , Issue.2 , pp. 943-953
    • Young, H.S.1    Herbette, L.G.2    Skita, V.3


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