메뉴 건너뛰기




Volumn 29, Issue 4, 2009, Pages 907-917

Modulation of the dimer interface at ionotropic glutamate-like receptor δ2 by D-serine and extracellular calcium

Author keywords

Delta2; Disulfide bond; Electrophysiological recordings; Pharmacology; Structure function relationship; Xenopus oocytes

Indexed keywords

CALCIUM; DEXTRO SERINE; DIMER; IONOTROPIC GLUTAMATE LIKE RECEPTOR DELTA2; IONOTROPIC RECEPTOR; UNCLASSIFIED DRUG;

EID: 59649125327     PISSN: 02706474     EISSN: 02706474     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.4081-08.2009     Document Type: Article
Times cited : (52)

References (51)
  • 1
    • 0032566513 scopus 로고    scopus 로고
    • Disulfide bonding and cysteine accessibility in the alpha-amino-3-hydroxy-5-methylisoxazole-4- propionic acid receptor subunit GluRD. Implications for redox modulation of glutamate receptors
    • Abele R, Lampinen M, Keinänen K, Madden DR (1998) Disulfide bonding and cysteine accessibility in the alpha-amino-3-hydroxy-5-methylisoxazole-4- propionic acid receptor subunit GluRD. Implications for redox modulation of glutamate receptors. J Biol Chem 273:25132-25138.
    • (1998) J Biol Chem , vol.273 , pp. 25132-25138
    • Abele, R.1    Lampinen, M.2    Keinänen, K.3    Madden, D.R.4
  • 2
    • 0027724656 scopus 로고
    • Selective expression of the glutamate receptor channel delta 2 subunit in cerebellar Purkinje cells
    • Araki K, Meguro H, Kushiya E, Takayama C, Inoue Y, Mishina M (1993) Selective expression of the glutamate receptor channel delta 2 subunit in cerebellar Purkinje cells. Biochem Biophys Res Commun 197:1267-1276.
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 1267-1276
    • Araki, K.1    Meguro, H.2    Kushiya, E.3    Takayama, C.4    Inoue, Y.5    Mishina, M.6
  • 3
    • 0033636314 scopus 로고    scopus 로고
    • Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: Crystal structures of the GluR2 ligand binding core
    • Armstrong N, Gouaux E (2000) Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 28:165-181.
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 4
    • 33749059766 scopus 로고    scopus 로고
    • Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor
    • Armstrong N, Jasti J, Beich-Frandsen M, Gouaux E (2006) Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor. Cell 127:85-97.
    • (2006) Cell , vol.127 , pp. 85-97
    • Armstrong, N.1    Jasti, J.2    Beich-Frandsen, M.3    Gouaux, E.4
  • 5
    • 0037088834 scopus 로고    scopus 로고
    • External anions and cations distinguish between AMPA and kainate receptor gating mechanisms
    • Bowie D (2002) External anions and cations distinguish between AMPA and kainate receptor gating mechanisms. J Physiol 539:725-733.
    • (2002) J Physiol , vol.539 , pp. 725-733
    • Bowie, D.1
  • 9
    • 34249951037 scopus 로고    scopus 로고
    • Structural aspects of AMPA receptor activation, desensitization and deactivation
    • Hansen KB, Yuan H, Traynelis SF (2007) Structural aspects of AMPA receptor activation, desensitization and deactivation. Curr Opin Neurobiol 17:281-288.
    • (2007) Curr Opin Neurobiol , vol.17 , pp. 281-288
    • Hansen, K.B.1    Yuan, H.2    Traynelis, S.F.3
  • 10
    • 44249093505 scopus 로고    scopus 로고
    • Pharmacological characterization of ligands at recombinant NMDA receptor subtypes by electrophysiological recordings and intracellular calcium measurements
    • Hansen KB, Bräuner-Osborne H, Egebjerg J (2008) Pharmacological characterization of ligands at recombinant NMDA receptor subtypes by electrophysiological recordings and intracellular calcium measurements. Comb Chem High Throughput Screen 11:304-315.
    • (2008) Comb Chem High Throughput Screen , vol.11 , pp. 304-315
    • Hansen, K.B.1    Bräuner-Osborne, H.2    Egebjerg, J.3
  • 11
    • 0029893942 scopus 로고    scopus 로고
    • The glycine binding site of the N-methyl-D-aspartate receptor subunit NR1: Identification of novel determinants of co-agonist potentiation in the extracellular M3-M4 loop region
    • Hirai H, Kirsch J, Laube B, Betz H, Kuhse J (1996) The glycine binding site of the N-methyl-D-aspartate receptor subunit NR1: identification of novel determinants of co-agonist potentiation in the extracellular M3-M4 loop region. Proc Natl Acad Sci U S A 93:6031-6036.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6031-6036
    • Hirai, H.1    Kirsch, J.2    Laube, B.3    Betz, H.4    Kuhse, J.5
  • 12
    • 1242293631 scopus 로고    scopus 로고
    • Regulation of AMPA receptor gating by ligand binding core dimers
    • Horning MS, Mayer ML (2004) Regulation of AMPA receptor gating by ligand binding core dimers. Neuron 41:379-388.
    • (2004) Neuron , vol.41 , pp. 379-388
    • Horning, M.S.1    Mayer, M.L.2
  • 13
    • 0043033172 scopus 로고    scopus 로고
    • Structural basis for partial agonist action at ionotropic glutamate receptors
    • Jin R, Banke TG, Mayer ML, Traynelis SF, Gouaux E (2003) Structural basis for partial agonist action at ionotropic glutamate receptors. Nat Neurosci 6:803-810.
    • (2003) Nat Neurosci , vol.6 , pp. 803-810
    • Jin, R.1    Banke, T.G.2    Mayer, M.L.3    Traynelis, S.F.4    Gouaux, E.5
  • 15
    • 29144505981 scopus 로고    scopus 로고
    • A mechanism underlying AMPA receptor trafficking during cerebellar long-term potentiation
    • Kakegawa W, Yuzaki M (2005) A mechanism underlying AMPA receptor trafficking during cerebellar long-term potentiation. Proc Natl Acad Sci U S A 102:17846-17851.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 17846-17851
    • Kakegawa, W.1    Yuzaki, M.2
  • 16
    • 33947161018 scopus 로고    scopus 로고
    • Ca2+ permeability of the channel pore is not essential for the delta2 glutamate receptor to regulate synaptic plasticity and motor coordination
    • Kakegawa W, Miyazaki T, Hirai H, Motohashi J, Mishina M, Watanabe M, Yuzaki M (2007) Ca2+ permeability of the channel pore is not essential for the delta2 glutamate receptor to regulate synaptic plasticity and motor coordination. J Physiol 579:729-735.
    • (2007) J Physiol , vol.579 , pp. 729-735
    • Kakegawa, W.1    Miyazaki, T.2    Hirai, H.3    Motohashi, J.4    Mishina, M.5    Watanabe, M.6    Yuzaki, M.7
  • 18
    • 33847654251 scopus 로고    scopus 로고
    • In silico mutation of cysteine residues in the ligand-binding domain of an N-methyl-D-aspartate receptor
    • Kaye SL, Sansom MS, Biggin PC (2007) In silico mutation of cysteine residues in the ligand-binding domain of an N-methyl-D-aspartate receptor. Biochemistry 46:2136-2145.
    • (2007) Biochemistry , vol.46 , pp. 2136-2145
    • Kaye, S.L.1    Sansom, M.S.2    Biggin, P.C.3
  • 19
    • 2542553538 scopus 로고    scopus 로고
    • Effects of the lurcher mutation on GluR1 desensitization and activation kinetics
    • Klein RM, Howe JR (2004) Effects of the lurcher mutation on GluR1 desensitization and activation kinetics. J Neurosci 24:4941-4951.
    • (2004) J Neurosci , vol.24 , pp. 4941-4951
    • Klein, R.M.1    Howe, J.R.2
  • 20
    • 0034114521 scopus 로고    scopus 로고
    • Mutation of a glutamate receptor motif reveals its role in gating and delta2 receptor channel properties
    • Kohda K, Wang Y, Yuzaki M (2000) Mutation of a glutamate receptor motif reveals its role in gating and delta2 receptor channel properties. Nat Neurosci 3:315-322.
    • (2000) Nat Neurosci , vol.3 , pp. 315-322
    • Kohda, K.1    Wang, Y.2    Yuzaki, M.3
  • 21
    • 0031012268 scopus 로고    scopus 로고
    • Differential localization of delta glutamate receptors in the rat cerebellum: Coexpression with AMPA receptors in parallel fiber-spine synapses and absence from climbing fiberspine synapses
    • Landsend AS, Amiry-Moghaddam M, Matsubara A, Bergersen L, Usami S, Wenthold RJ, Ottersen OP (1997) Differential localization of delta glutamate receptors in the rat cerebellum: coexpression with AMPA receptors in parallel fiber-spine synapses and absence from climbing fiberspine synapses. J Neurosci 17:834-842.
    • (1997) J Neurosci , vol.17 , pp. 834-842
    • Landsend, A.S.1    Amiry-Moghaddam, M.2    Matsubara, A.3    Bergersen, L.4    Usami, S.5    Wenthold, R.J.6    Ottersen, O.P.7
  • 23
    • 0036430258 scopus 로고    scopus 로고
    • Mutation in hotfoot-4J mice results in retention of delta2 glutamate receptors in ER
    • Matsuda S, Yuzaki M (2002) Mutation in hotfoot-4J mice results in retention of delta2 glutamate receptors in ER. Eur J Neurosci 16:1507-1516.
    • (2002) Eur J Neurosci , vol.16 , pp. 1507-1516
    • Matsuda, S.1    Yuzaki, M.2
  • 24
    • 0028927274 scopus 로고
    • Immunoprecipitation, immunoblotting, and immunocytochemistry studies suggest that glutamate receptor delta subunits form novel postsynaptic receptor complexes
    • Mayat E, Petralia RS, Wang YX, Wenthold RJ (1995) Immunoprecipitation, immunoblotting, and immunocytochemistry studies suggest that glutamate receptor delta subunits form novel postsynaptic receptor complexes. J Neurosci 15:2533-2546.
    • (1995) J Neurosci , vol.15 , pp. 2533-2546
    • Mayat, E.1    Petralia, R.S.2    Wang, Y.X.3    Wenthold, R.J.4
  • 25
    • 33645321641 scopus 로고    scopus 로고
    • Glutamate receptors at atomic resolution
    • Mayer ML (2006) Glutamate receptors at atomic resolution. Nature 440:456-462.
    • (2006) Nature , vol.440 , pp. 456-462
    • Mayer, M.L.1
  • 27
    • 0017356990 scopus 로고
    • Calcium modulation in brain extracellular microenvironment demonstrated with ion-selective micropipette
    • Nicholson C, Bruggencate GT, Steinberg R, Stöckle H (1977) Calcium modulation in brain extracellular microenvironment demonstrated with ion-selective micropipette. Proc Natl Acad Sci U S A 74:1287-1290.
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 1287-1290
    • Nicholson, C.1    Bruggencate, G.T.2    Steinberg, R.3    Stöckle, H.4
  • 28
    • 0018096724 scopus 로고
    • Calcium and potassium changes in extracellular microenvironment of cat cerebellar cortex
    • Nicholson C, ten Bruggencate G, Stöckle H, Steinberg R (1978) Calcium and potassium changes in extracellular microenvironment of cat cerebellar cortex. J Neurophysiol 41:1026-1039.
    • (1978) J Neurophysiol , vol.41 , pp. 1026-1039
    • Nicholson, C.1    ten Bruggencate, G.2    Stöckle, H.3    Steinberg, R.4
  • 30
    • 0027235488 scopus 로고
    • Three-dimensional structures of the periplasmic lysine/arginine/ornithine- binding protein with and without a ligand
    • Oh BH, Pandit J, Kang CH, Nikaido K, Gokcen S, Ames GF, Kim SH (1993) Three-dimensional structures of the periplasmic lysine/arginine/ornithine- binding protein with and without a ligand. J Biol Chem 268:11348-11355.
    • (1993) J Biol Chem , vol.268 , pp. 11348-11355
    • Oh, B.H.1    Pandit, J.2    Kang, C.H.3    Nikaido, K.4    Gokcen, S.5    Ames, G.F.6    Kim, S.H.7
  • 31
    • 33847769253 scopus 로고    scopus 로고
    • Structure and mechanism of kainate receptor modulation by anions
    • Plested AJ, Mayer ML (2007) Structure and mechanism of kainate receptor modulation by anions. Neuron 53:829-841.
    • (2007) Neuron , vol.53 , pp. 829-841
    • Plested, A.J.1    Mayer, M.L.2
  • 32
    • 44649169115 scopus 로고    scopus 로고
    • Molecular basis of kainate receptor modulation by sodium
    • Plested AJ, Vijayan R, Biggin PC, Mayer ML (2008) Molecular basis of kainate receptor modulation by sodium. Neuron 58:720-735.
    • (2008) Neuron , vol.58 , pp. 720-735
    • Plested, A.J.1    Vijayan, R.2    Biggin, P.C.3    Mayer, M.L.4
  • 33
    • 0032102482 scopus 로고    scopus 로고
    • Kainate receptor modulation of GABA release involves a metabotropic function
    • Rodríguez-Moreno A, Lerma J (1998) Kainate receptor modulation of GABA release involves a metabotropic function. Neuron 20:1211-1218.
    • (1998) Neuron , vol.20 , pp. 1211-1218
    • Rodríguez-Moreno, A.1    Lerma, J.2
  • 34
    • 0034815622 scopus 로고    scopus 로고
    • The role of perisynaptic glial sheaths in glutamate spill-over and extracellular Ca(2+) depletion
    • Rusakov DA (2001) The role of perisynaptic glial sheaths in glutamate spill-over and extracellular Ca(2+) depletion. Biophys J 81:1947-1959.
    • (2001) Biophys J , vol.81 , pp. 1947-1959
    • Rusakov, D.A.1
  • 35
    • 53749096977 scopus 로고    scopus 로고
    • To gate or not to gate: Are the delta subunits in the glutamate receptor family functional ion channels?
    • Schmid SM, Hollmann M (2008) To gate or not to gate: are the delta subunits in the glutamate receptor family functional ion channels? Mol Neurobiol 37:126-141.
    • (2008) Mol Neurobiol , vol.37 , pp. 126-141
    • Schmid, S.M.1    Hollmann, M.2
  • 36
    • 84944648082 scopus 로고
    • Revised effective ionic radii and systematic studies of interatomie distances in halides and chaleogenides
    • Shannon RD (1976) Revised effective ionic radii and systematic studies of interatomie distances in halides and chaleogenides. Acta Crystallogr A 32:751-767.
    • (1976) Acta Crystallogr A , vol.32 , pp. 751-767
    • Shannon, R.D.1
  • 37
    • 0028034803 scopus 로고
    • Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor
    • Sullivan JM, Traynelis SF, Chen HS, Escobar W, Heinemann SF, Lipton SA (1994) Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor. Neuron 13:929-936.
    • (1994) Neuron , vol.13 , pp. 929-936
    • Sullivan, J.M.1    Traynelis, S.F.2    Chen, H.S.3    Escobar, W.4    Heinemann, S.F.5    Lipton, S.A.6
  • 39
    • 0032529588 scopus 로고    scopus 로고
    • Control of voltage-independent zinc inhibition of NMDA receptors by the NR1 subunit
    • Traynelis SF, Burgess MF, Zheng F, Lyuboslavsky P, Powers JL (1998) Control of voltage-independent zinc inhibition of NMDA receptors by the NR1 subunit. J Neurosci 18:6163-6175.
    • (1998) J Neurosci , vol.18 , pp. 6163-6175
    • Traynelis, S.F.1    Burgess, M.F.2    Zheng, F.3    Lyuboslavsky, P.4    Powers, J.L.5
  • 40
    • 0026686125 scopus 로고
    • Mutations in a putative agonist binding region of the AMPA-selective glutamate receptor channel
    • Uchino S, Sakimura K, Nagahari K, Mishina M (1992) Mutations in a putative agonist binding region of the AMPA-selective glutamate receptor channel. FEBS Lett 308:253-257.
    • (1992) FEBS Lett , vol.308 , pp. 253-257
    • Uchino, S.1    Sakimura, K.2    Nagahari, K.3    Mishina, M.4
  • 41
    • 0030893070 scopus 로고    scopus 로고
    • Assessment of frequency-dependent alterations in the level of extracellular Ca2+ in the synaptic cleft
    • Vassilev PM, Mitchel J, Vassilev M, Kanazirska M, Brown EM (1997) Assessment of frequency-dependent alterations in the level of extracellular Ca2+ in the synaptic cleft. Biophys J 72:2103-2116.
    • (1997) Biophys J , vol.72 , pp. 2103-2116
    • Vassilev, P.M.1    Mitchel, J.2    Vassilev, M.3    Kanazirska, M.4    Brown, E.M.5
  • 42
    • 0034986665 scopus 로고    scopus 로고
    • A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux
    • Vissel B, Krupp JJ, Heinemann SF, Westbrook GL (2001) A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux. Nat Neurosci 4:587-596.
    • (2001) Nat Neurosci , vol.4 , pp. 587-596
    • Vissel, B.1    Krupp, J.J.2    Heinemann, S.F.3    Westbrook, G.L.4
  • 43
    • 33847641082 scopus 로고    scopus 로고
    • The Lurcher mouse: Fresh insights from an old mutant
    • Vogel MW, Caston J, Yuzaki M, Mariani J (2007) The Lurcher mouse: fresh insights from an old mutant. Brain Res 1140:4-18.
    • (2007) Brain Res , vol.1140 , pp. 4-18
    • Vogel, M.W.1    Caston, J.2    Yuzaki, M.3    Mariani, J.4
  • 44
    • 0031049768 scopus 로고    scopus 로고
    • Dominant negative mutant of ionotropic glutamate receptor subunit GluR3: Implications for the role of a cysteine residue for its channel activity and pharmacological properties
    • Watase K, Sekiguchi M, Matsui TA, Tagawa Y, Wada K (1997) Dominant negative mutant of ionotropic glutamate receptor subunit GluR3: implications for the role of a cysteine residue for its channel activity and pharmacological properties. Biochem J 322:385-391.
    • (1997) Biochem J , vol.322 , pp. 385-391
    • Watase, K.1    Sekiguchi, M.2    Matsui, T.A.3    Tagawa, Y.4    Wada, K.5
  • 46
    • 0029921964 scopus 로고    scopus 로고
    • Activation of N-methyl-D-aspartate receptors by glycine: Role of an aspartate residue in the M3-M4 loop of the NR1 subunit
    • Williams K, Chao J, Kashiwagi K, Masuko T, Igarashi K (1996) Activation of N-methyl-D-aspartate receptors by glycine: role of an aspartate residue in the M3-M4 loop of the NR1 subunit. Mol Pharmacol 50:701-708.
    • (1996) Mol Pharmacol , vol.50 , pp. 701-708
    • Williams, K.1    Chao, J.2    Kashiwagi, K.3    Masuko, T.4    Igarashi, K.5
  • 48
    • 33744973079 scopus 로고    scopus 로고
    • External ions are coactivators of kainate receptors
    • Wong AY, Fay AM, Bowie D (2006) External ions are coactivators of kainate receptors. J Neurosci 26:5750-5755.
    • (2006) J Neurosci , vol.26 , pp. 5750-5755
    • Wong, A.Y.1    Fay, A.M.2    Bowie, D.3
  • 49
    • 34250806504 scopus 로고    scopus 로고
    • - dipole couples agonist binding to kainate receptor activation
    • - dipole couples agonist binding to kainate receptor activation. J Neurosci 27:6800-6809.
    • (2007) J Neurosci , vol.27 , pp. 6800-6809
    • Wong, A.Y.1    MacLean, D.M.2    Bowie, D.3
  • 50
    • 0032528151 scopus 로고    scopus 로고
    • Glutamate receptor targeting to synaptic populations on Purkinje cells is developmentally regulated
    • Zhao HM, Wenthold RJ, Petralia RS (1998) Glutamate receptor targeting to synaptic populations on Purkinje cells is developmentally regulated. J Neurosci 18:5517-5528.
    • (1998) J Neurosci , vol.18 , pp. 5517-5528
    • Zhao, H.M.1    Wenthold, R.J.2    Petralia, R.S.3
  • 51
    • 0030800468 scopus 로고    scopus 로고
    • Neurodegeneration in Lurcher mice caused by mutation in delta2 glutamate receptor gene
    • Zuo J, De Jager PL, Takahashi KA, Jiang W, Linden DJ, Heintz N (1997) Neurodegeneration in Lurcher mice caused by mutation in delta2 glutamate receptor gene. Nature 388:769-773.
    • (1997) Nature , vol.388 , pp. 769-773
    • Zuo, J.1    De Jager, P.L.2    Takahashi, K.A.3    Jiang, W.4    Linden, D.J.5    Heintz, N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.