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Volumn 104, Issue 4, 2008, Pages 1020-1031

The C-terminus of the metabotropic glutamate receptor 1b regulates dimerization of the receptor

Author keywords

C terminus; Dimerization; Endoplasmic reticulum; Metabotropic glutamate receptor 1b; Retention; Trafficking

Indexed keywords

CD2 ANTIGEN; ENDOPLASMIC RETICULUM GOLGI INTERMEDIATE COMPARTMENT PROTEIN; GLUTAMATE RECEPTOR; LYMPHOCYTE ANTIGEN; METABOTROPIC GLUTAMATE RECEPTOR 1A; METABOTROPIC GLUTAMATE RECEPTOR 1B; METABOTROPIC RECEPTOR; PROTEIN; UNCLASSIFIED DRUG;

EID: 38449093046     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2007.05034.x     Document Type: Article
Times cited : (16)

References (64)
  • 1
    • 0035927783 scopus 로고    scopus 로고
    • Agonist-independent activation of metabotropic glutamate receptors by the intracellular protein Homer
    • Ango F., Prezeau L., Muller T., Tu J. C., Xiao B., Worley P. F., Pin J. P., Bockaert J. Fagni L. (2001) Agonist-independent activation of metabotropic glutamate receptors by the intracellular protein Homer. Nature 411, 962 965.
    • (2001) Nature , vol.411 , pp. 962-965
    • Ango, F.1    Prezeau, L.2    Muller, T.3    Tu, J.C.4    Xiao, B.5    Worley, P.F.6    Pin, J.P.7    Bockaert, J.8    Fagni, L.9
  • 2
    • 2442529839 scopus 로고    scopus 로고
    • Hetero-oligomerization between GABAA and GABAB receptors regulates GABAB receptor trafficking
    • Balasubramanian S., Teissere J. A., Raju D. V. Hall R. A. (2004) Hetero-oligomerization between GABAA and GABAB receptors regulates GABAB receptor trafficking. J. Biol. Chem. 279, 18840 18850.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18840-18850
    • Balasubramanian, S.1    Teissere, J.A.2    Raju, D.V.3    Hall, R.A.4
  • 3
    • 0037143619 scopus 로고    scopus 로고
    • Closure of the Venus flytrap module of mGlu8 receptor and the activation process: Insights from mutations converting antagonists into agonists
    • Bessis A. S., Rondard P., Gaven F., Brabet I., Triballeau N., Prezeau L., Acher F. Pin J. P. (2002) Closure of the Venus flytrap module of mGlu8 receptor and the activation process: insights from mutations converting antagonists into agonists. Proc. Natl Acad. Sci. U. S. A. 99, 11097 11102.
    • (2002) Proc. Natl Acad. Sci. U. S. A. , vol.99 , pp. 11097-11102
    • Bessis, A.S.1    Rondard, P.2    Gaven, F.3    Brabet, I.4    Triballeau, N.5    Prezeau, L.6    Acher, F.7    Pin, J.P.8
  • 6
    • 28644432057 scopus 로고    scopus 로고
    • Assembly-dependent surface targeting of the heterodimeric GABAB receptor is controlled by COPI but not 14-3-3
    • Brock C., Boudier L., Maurel D., Blahos J. Pin J. P. (2005) Assembly-dependent surface targeting of the heterodimeric GABAB receptor is controlled by COPI but not 14-3-3. Mol. Biol. Cell 16, 5572 5578.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5572-5578
    • Brock, C.1    Boudier, L.2    Maurel, D.3    Blahos, J.4    Pin, J.P.5
  • 8
    • 0033179032 scopus 로고    scopus 로고
    • Co-expression of metabotropic glutamate receptor type 1 alpha with Homer-1a/Vesl-1S increases the cell surface expression of the receptor
    • Ciruela F., Soloviev M. M. McIlhinney R. A. J. (1999a) Co-expression of metabotropic glutamate receptor type 1 alpha with Homer-1a/Vesl-1S increases the cell surface expression of the receptor. Biochem. J. 341, 795 803.
    • (1999) Biochem. J. , vol.341 , pp. 795-803
    • Ciruela, F.1    Soloviev, M.M.2    McIlhinney, R.A.J.3
  • 9
    • 0032994233 scopus 로고    scopus 로고
    • Cell surface expression of the metabotropic glutamate receptor type 1α is regulated by the C-terminal tail
    • Ciruela F., Soloviev M. M. McIlhinney R. A. J. (1999b) Cell surface expression of the metabotropic glutamate receptor type 1α is regulated by the C-terminal tail. FEBS Lett. 448, 91 94.
    • (1999) FEBS Lett. , vol.448 , pp. 91-94
    • Ciruela, F.1    Soloviev, M.M.2    McIlhinney, R.A.J.3
  • 10
    • 0033964384 scopus 로고    scopus 로고
    • Homer-1c/Vesl-1L modulates the cell surface targeting of metabotropic glutamate receptor type 1 alpha: Evidence for an anchoring function
    • Ciruela F., Soloviev M. M., Chan W. Y. McIlhinney R. A. J. (2000) Homer-1c/Vesl-1L modulates the cell surface targeting of metabotropic glutamate receptor type 1 alpha: evidence for an anchoring function. Mol. Cell. Neurosci. 15, 36 50.
    • (2000) Mol. Cell. Neurosci. , vol.15 , pp. 36-50
    • Ciruela, F.1    Soloviev, M.M.2    Chan, W.Y.3    McIlhinney, R.A.J.4
  • 11
    • 0030995878 scopus 로고    scopus 로고
    • Pharmacology and functions of metabotropic glutamate receptors
    • Conn P. J. Pin J. P. (1997) Pharmacology and functions of metabotropic glutamate receptors. Ann. Rev. Pharmacol. Toxicol. 37, 205 237.
    • (1997) Ann. Rev. Pharmacol. Toxicol. , vol.37 , pp. 205-237
    • Conn, P.J.1    Pin, J.P.2
  • 12
    • 0037088919 scopus 로고    scopus 로고
    • Alternative splicing unmasks dendritic and axonal targeting signals in metabotropic glutamate receptor 1
    • Francesconi A. Duvoisin R. M. (2002) Alternative splicing unmasks dendritic and axonal targeting signals in metabotropic glutamate receptor 1. J. Neurosci. 22, 2196 2205.
    • (2002) J. Neurosci. , vol.22 , pp. 2196-2205
    • Francesconi, A.1    Duvoisin, R.M.2
  • 13
    • 0035914405 scopus 로고    scopus 로고
    • Heterodimerization of calcium sensing receptors with metabotropic glutamate receptors in neurons
    • Gama L., Wilt S. G. Breitwieser G. E. (2001) Heterodimerization of calcium sensing receptors with metabotropic glutamate receptors in neurons. J. Biol. Chem. 276, 39053 39059.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39053-39059
    • Gama, L.1    Wilt, S.G.2    Breitwieser, G.E.3
  • 14
    • 0033538058 scopus 로고    scopus 로고
    • Ligand binding to the amino-terminal domain of the mGluR4 subtype of metabotropic glutamate receptor
    • Han G. Hampson D. R. (1999) Ligand binding to the amino-terminal domain of the mGluR4 subtype of metabotropic glutamate receptor. J. Biol. Chem. 274, 10008 10013.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10008-10013
    • Han, G.1    Hampson, D.R.2
  • 16
    • 0029043591 scopus 로고
    • Molecular, functional, and pharmacological characterization of the metabotropic glutamate receptor type 5 splice variants: Comparison with mGluR1
    • Joly C., Gomeza J., Brabet I., Curry K., Bockaert J. Pin J. P. (1995) Molecular, functional, and pharmacological characterization of the metabotropic glutamate receptor type 5 splice variants: comparison with mGluR1. J. Neurosci. 15, 3970 3981.
    • (1995) J. Neurosci. , vol.15 , pp. 3970-3981
    • Joly, C.1    Gomeza, J.2    Brabet, I.3    Curry, K.4    Bockaert, J.5    Pin, J.P.6
  • 17
    • 0033578005 scopus 로고    scopus 로고
    • G-protein heterodimerization modulates receptor function
    • Jordan B. A. Devi L. A. (1999) G-protein heterodimerization modulates receptor function. Nature 399, 697 700.
    • (1999) Nature , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 18
    • 0029991350 scopus 로고    scopus 로고
    • Transfecting mammalian cells: Optimization of critical parameters affecting calcium phosphate precipitate formation
    • Jordan M., Schallhorn A. Wurm F. M. (1996) Transfecting mammalian cells: optimization of critical parameters affecting calcium phosphate precipitate formation. Nucleic Acids Res. 24, 596 601.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 596-601
    • Jordan, M.1    Schallhorn, A.2    Wurm, F.M.3
  • 19
    • 0037083370 scopus 로고    scopus 로고
    • Tamalin, a PDZ domain-containing protein, links a protein complex formation of group 1 metabotropic glutamate receptors and the guanine nucleotide exchange factor cytohesins
    • Kitano J., Kimura K., Yamazaki Y., Soda T., Shigemoto R., Nakajima Y. Nakanishi S. (2002) Tamalin, a PDZ domain-containing protein, links a protein complex formation of group 1 metabotropic glutamate receptors and the guanine nucleotide exchange factor cytohesins. J. Neurosci. 22, 1280 1289.
    • (2002) J. Neurosci. , vol.22 , pp. 1280-1289
    • Kitano, J.1    Kimura, K.2    Yamazaki, Y.3    Soda, T.4    Shigemoto, R.5    Nakajima, Y.6    Nakanishi, S.7
  • 20
    • 3543036363 scopus 로고    scopus 로고
    • Closed state of both binding domains of homodimeric mGlu receptors is required for full activity
    • Kniazeff J., Bessis A. S., Maurel D., Ansanay H., Prezeau L. Pin J. P. (2004a) Closed state of both binding domains of homodimeric mGlu receptors is required for full activity. Nat. Struct. Mol. Biol. 11, 706 713.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 706-713
    • Kniazeff, J.1    Bessis, A.S.2    Maurel, D.3    Ansanay, H.4    Prezeau, L.5    Pin, J.P.6
  • 23
    • 1942469528 scopus 로고    scopus 로고
    • Molecular determinants involved in the allosteric control of agonist affinity in the GABAB receptor by the GABAB2 subunit
    • Liu J., Maurel D., Etzol S., Brabet I., Ansanay H., Pin J. P. Rondard P. (2004a) Molecular determinants involved in the allosteric control of agonist affinity in the GABAB receptor by the GABAB2 subunit. J. Biol. Chem. 279, 15824 15830.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15824-15830
    • Liu, J.1    Maurel, D.2    Etzol, S.3    Brabet, I.4    Ansanay, H.5    Pin, J.P.6    Rondard, P.7
  • 24
    • 11244251776 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer reports properties of syntaxin1a interaction with Munc18-1 in vivo
    • Liu J., Ernst S. A., Gladycheva S. E., Lee Y. Y., Lentz S. I., Ho C. S., Li Q. Stuenkel E. L. (2004b) Fluorescence resonance energy transfer reports properties of syntaxin1a interaction with Munc18-1 in vivo. J. Biol. Chem. 279, 55924 55936.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55924-55936
    • Liu, J.1    Ernst, S.A.2    Gladycheva, S.E.3    Lee, Y.Y.4    Lentz, S.I.5    Ho, C.S.6    Li, Q.7    Stuenkel, E.L.8
  • 25
    • 0027485836 scopus 로고
    • NMDA-receptor-dependent synaptic plasticity: Multiple forms and mechanisms
    • Malenka R. C. Nicoll R. A. (1993) NMDA-receptor-dependent synaptic plasticity: multiple forms and mechanisms. Trends Neurosci. 16, 521 527.
    • (1993) Trends Neurosci. , vol.16 , pp. 521-527
    • Malenka, R.C.1    Nicoll, R.A.2
  • 26
    • 0036382829 scopus 로고    scopus 로고
    • Assembly-dependent trafficking assays in the detection of receptor-receptor interactions
    • Margeta-Mitrovic M. (2002) Assembly-dependent trafficking assays in the detection of receptor-receptor interactions. Methods 27, 311 317.
    • (2002) Methods , vol.27 , pp. 311-317
    • Margeta-Mitrovic, M.1
  • 27
    • 0030609103 scopus 로고    scopus 로고
    • The rat mGlu1d receptor splice variant shares functional properties with the other short isoforms of mGlu1 receptor
    • Mary S., Stephan D., Gomeza J., Bockaert J., Pruss R. M. Pin J. P. (1997) The rat mGlu1d receptor splice variant shares functional properties with the other short isoforms of mGlu1 receptor. Eur. J. Pharmacol. 335, 65 72.
    • (1997) Eur. J. Pharmacol. , vol.335 , pp. 65-72
    • Mary, S.1    Stephan, D.2    Gomeza, J.3    Bockaert, J.4    Pruss, R.M.5    Pin, J.P.6
  • 28
    • 0031983457 scopus 로고    scopus 로고
    • A cluster of basic residues in the carboxyl-terminal tail of the short metabotropic glutamate receptor 1 variants impairs their coupling to phospholipase C
    • Mary S., Gomeza J., Prezeau L., Bockaert J. Pin J. P. (1998) A cluster of basic residues in the carboxyl-terminal tail of the short metabotropic glutamate receptor 1 variants impairs their coupling to phospholipase C. J. Biol. Chem. 273, 425 432.
    • (1998) J. Biol. Chem. , vol.273 , pp. 425-432
    • Mary, S.1    Gomeza, J.2    Prezeau, L.3    Bockaert, J.4    Pin, J.P.5
  • 30
    • 0343852212 scopus 로고    scopus 로고
    • Immunolocalization of the mGluR1b splice variant of the metabotropic glutamate receptor 1 at parallel fiber-Purkinje cell synapses in the rat cerebellar cortex
    • Mateos J. M., Benitez R., Elezgarai I. et al. (2000) Immunolocalization of the mGluR1b splice variant of the metabotropic glutamate receptor 1 at parallel fiber-Purkinje cell synapses in the rat cerebellar cortex. J. Neurochem. 74, 1301 1309.
    • (2000) J. Neurochem. , vol.74 , pp. 1301-1309
    • Mateos, J.M.1    Benitez, R.2    Elezgarai, I.3
  • 31
    • 0023125256 scopus 로고
    • The physiology of excitatory amino acids in the vertebrate central nervous system
    • Mayer M. L. Westbrook G. L. (1987) The physiology of excitatory amino acids in the vertebrate central nervous system. Prog. Neurobiol. 28, 197 276.
    • (1987) Prog. Neurobiol. , vol.28 , pp. 197-276
    • Mayer, M.L.1    Westbrook, G.L.2
  • 32
    • 30944461855 scopus 로고    scopus 로고
    • Hide and run. Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins
    • Michelsen K., Yuan H. Schwappach B. (2005) Hide and run. Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins. EMBO Rep 6, 717 722.
    • (2005) EMBO Rep , vol.6 , pp. 717-722
    • Michelsen, K.1    Yuan, H.2    Schwappach, B.3
  • 33
    • 0037353568 scopus 로고    scopus 로고
    • Long-term potentiation of mGluR1 activity by depolarization-induced Homer1a in mouse cerebellar Purkinje neurons
    • Minami I., Kengaku M., Smitt P. S., Shigemoto R. Hirano T. (2003) Long-term potentiation of mGluR1 activity by depolarization-induced Homer1a in mouse cerebellar Purkinje neurons. Eur. J. Neurosci. 17, 1023 1032.
    • (2003) Eur. J. Neurosci. , vol.17 , pp. 1023-1032
    • Minami, I.1    Kengaku, M.2    Smitt, P.S.3    Shigemoto, R.4    Hirano, T.5
  • 34
    • 0034948422 scopus 로고    scopus 로고
    • Bidirectional regulation of neurite elaboration by alternatively spliced metabotropic glutamate receptor 5 (mGluR5) isoforms
    • Mion S., Corti C., Neki A., Shigemoto R., Corsi M., Fumagalli G. Ferraguti F. (2001) Bidirectional regulation of neurite elaboration by alternatively spliced metabotropic glutamate receptor 5 (mGluR5) isoforms. Mol. Cell. Neurosci. 17, 957 972.
    • (2001) Mol. Cell. Neurosci. , vol.17 , pp. 957-972
    • Mion, S.1    Corti, C.2    Neki, A.3    Shigemoto, R.4    Corsi, M.5    Fumagalli, G.6    Ferraguti, F.7
  • 35
    • 0347064158 scopus 로고    scopus 로고
    • Assembly of alpha4beta2 nicotinic acetylcholine receptors assessed with functional fluorescently labeled subunits: Effects of localization, trafficking, and nicotine-induced upregulation in clonal mammalian cells and in cultured midbrain neurons
    • Nashmi R., Dickinson M. E., McKinney S., Jareb M., Labarca C., Fraser S. E. Lester H. A. (2003) Assembly of alpha4beta2 nicotinic acetylcholine receptors assessed with functional fluorescently labeled subunits: effects of localization, trafficking, and nicotine-induced upregulation in clonal mammalian cells and in cultured midbrain neurons. J. Neurosci. 23, 11554 11567.
    • (2003) J. Neurosci. , vol.23 , pp. 11554-11567
    • Nashmi, R.1    Dickinson, M.E.2    McKinney, S.3    Jareb, M.4    Labarca, C.5    Fraser, S.E.6    Lester, H.A.7
  • 36
    • 0037112329 scopus 로고    scopus 로고
    • Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals
    • O'Kelly I., Butler M. H., Zilberberg N. Goldstein S. A. (2002) Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell 111, 577 588.
    • (2002) Cell , vol.111 , pp. 577-588
    • O'Kelly, I.1    Butler, M.H.2    Zilberberg, N.3    Goldstein, S.A.4
  • 37
    • 0035958027 scopus 로고    scopus 로고
    • Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A)
    • Pfeiffer M., Koch T., Schroder H., Klutzny M., Kirscht S., Kreienkamp H. J., Hollt V. Schulz S. (2001) Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A). J. Biol. Chem. 276, 14027 14036.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14027-14036
    • Pfeiffer, M.1    Koch, T.2    Schroder, H.3    Klutzny, M.4    Kirscht, S.5    Kreienkamp, H.J.6    Hollt, V.7    Schulz, S.8
  • 38
    • 0001050066 scopus 로고    scopus 로고
    • The metabotropic glutamate receptors: Structure, activation mechanism and pharmacology
    • Pin J. P. Acher F. (2002) The metabotropic glutamate receptors: structure, activation mechanism and pharmacology. Curr. Drug Targets CNS Neurol. Disord. 1, 297 317.
    • (2002) Curr. Drug Targets CNS Neurol. Disord. , vol.1 , pp. 297-317
    • Pin, J.P.1    Acher, F.2
  • 39
    • 0029187946 scopus 로고
    • The metabotropic glutamate receptors: Structure and functions
    • Pin J. P. Duvoisin R. (1995) The metabotropic glutamate receptors: structure and functions. Neuropharmacology 34, 1 26.
    • (1995) Neuropharmacology , vol.34 , pp. 1-26
    • Pin, J.P.1    Duvoisin, R.2
  • 40
    • 0026476478 scopus 로고
    • Alternative splicing generates metabotropic glutamate receptors inducing different patterns of calcium release in Xenopus oocytes
    • Pin J. P., Waeber C., Prezeau L., Bockaert J. Heinemann S. F. (1992) Alternative splicing generates metabotropic glutamate receptors inducing different patterns of calcium release in Xenopus oocytes. Proc. Natl Acad. Sci. USA 89, 10331 10335.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10331-10335
    • Pin, J.P.1    Waeber, C.2    Prezeau, L.3    Bockaert, J.4    Heinemann, S.F.5
  • 42
    • 0034602293 scopus 로고    scopus 로고
    • Cys-140 is critical for metabotropic glutamate receptor-1 dimerization
    • Ray K. Hauschild B. C. (2000) Cys-140 is critical for metabotropic glutamate receptor-1 dimerization. J. Biol. Chem. 275, 34245 34251.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34245-34251
    • Ray, K.1    Hauschild, B.C.2
  • 43
    • 0033600911 scopus 로고    scopus 로고
    • Identification of the cysteine residues in the amino-terminal extracellular domain of the human Ca(2+) receptor critical for dimerization. Implications for function of monomeric Ca(2+) receptor
    • Ray K., Hauschild B. C., Steinbach P. J., Goldsmith P. K., Hauache O. Spiegel A. M. (1999) Identification of the cysteine residues in the amino-terminal extracellular domain of the human Ca(2+) receptor critical for dimerization. Implications for function of monomeric Ca(2+) receptor. J. Biol. Chem. 274, 27642 27650.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27642-27650
    • Ray, K.1    Hauschild, B.C.2    Steinbach, P.J.3    Goldsmith, P.K.4    Hauache, O.5    Spiegel, A.M.6
  • 44
    • 0346101760 scopus 로고    scopus 로고
    • Cell surface expression of GluR5 kainate receptors is regulated by an endoplasmic reticulum retention signal
    • Ren Z., Riley N. J., Needleman L. A., Sanders J. M., Swanson G. T. Marshall J. (2003) Cell surface expression of GluR5 kainate receptors is regulated by an endoplasmic reticulum retention signal. J. Biol. Chem. 278, 52700 52709.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52700-52709
    • Ren, Z.1    Riley, N.J.2    Needleman, L.A.3    Sanders, J.M.4    Swanson, G.T.5    Marshall, J.6
  • 45
    • 0032973978 scopus 로고    scopus 로고
    • Characterization of the dimerization of metabotropic glutamate receptors using an N-terminal truncation of mGluR1alpha
    • Robbins M. J., Ciruela F., Rhodes A. McIlhinney R. A. (1999) Characterization of the dimerization of metabotropic glutamate receptors using an N-terminal truncation of mGluR1alpha. J. Neurochem. 72, 2539 2547.
    • (1999) J. Neurochem. , vol.72 , pp. 2539-2547
    • Robbins, M.J.1    Ciruela, F.2    Rhodes, A.3    McIlhinney, R.A.4
  • 47
    • 0029903640 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a disulfide-linked dimer
    • Romano C., Yang W. L. Omalley K. L. (1996) Metabotropic glutamate receptor 5 is a disulfide-linked dimer. J. Biol. Chem. 271, 28612 28616.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28612-28616
    • Romano, C.1    Yang, W.L.2    Omalley, K.L.3
  • 49
  • 50
    • 1542614144 scopus 로고    scopus 로고
    • Coordinated PKA and PKC phosphorylation suppresses RXR-mediated ER retention and regulates the surface delivery of NMDA receptors
    • Scott D. B., Blanpied T. A. Ehlers M. D. (2003) Coordinated PKA and PKC phosphorylation suppresses RXR-mediated ER retention and regulates the surface delivery of NMDA receptors. Neuropharmacology 45, 755 767.
    • (2003) Neuropharmacology , vol.45 , pp. 755-767
    • Scott, D.B.1    Blanpied, T.A.2    Ehlers, M.D.3
  • 51
    • 0036328482 scopus 로고    scopus 로고
    • Characterization of an N-terminal secreted domain of the type-1 human metabotropic glutamate receptor produced by a mammalian cell line
    • Selkirk J. V., Challiss R. A., Rhodes A. McIlhinney R. A. (2002) Characterization of an N-terminal secreted domain of the type-1 human metabotropic glutamate receptor produced by a mammalian cell line. J. Neurochem. 80, 346 353.
    • (2002) J. Neurochem. , vol.80 , pp. 346-353
    • Selkirk, J.V.1    Challiss, R.A.2    Rhodes, A.3    McIlhinney, R.A.4
  • 52
    • 0034520590 scopus 로고    scopus 로고
    • PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants
    • Standley S., Roche K. W., McCallum J., Sans N. Wenthold R. J. (2000) PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants. Neuron 28, 887 898.
    • (2000) Neuron , vol.28 , pp. 887-898
    • Standley, S.1    Roche, K.W.2    McCallum, J.3    Sans, N.4    Wenthold, R.J.5
  • 54
    • 3042551375 scopus 로고    scopus 로고
    • Ligand-induced rearrangement of the dimeric metabotropic glutamate receptor 1alpha
    • Tateyama M., Abe H., Nakata H., Saito O. Kubo Y. (2004) Ligand-induced rearrangement of the dimeric metabotropic glutamate receptor 1alpha. Nat. Struct. Mol. Biol. 11, 637 642.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 637-642
    • Tateyama, M.1    Abe, H.2    Nakata, H.3    Saito, O.4    Kubo, Y.5
  • 55
    • 0037022586 scopus 로고    scopus 로고
    • Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+
    • Tsuchiya D., Kunishima N., Kamiya N., Jingami H. Morikawa K. (2002) Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+. Proc. Natl Acad. Sci. USA 99, 2660 2665.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 2660-2665
    • Tsuchiya, D.1    Kunishima, N.2    Kamiya, N.3    Jingami, H.4    Morikawa, K.5
  • 57
    • 0032192487 scopus 로고    scopus 로고
    • Homer binds a novel proline rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors
    • Tu J. C., Xiao B., Yuan J. P., Lanahan A. A., Leoffert K., Li M., Linden D. J. Worley P. F. (1998) Homer binds a novel proline rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors. Neuron 21, 717 726.
    • (1998) Neuron , vol.21 , pp. 717-726
    • Tu, J.C.1    Xiao, B.2    Yuan, J.P.3    Lanahan, A.A.4    Leoffert, K.5    Li, M.6    Linden, D.J.7    Worley, P.F.8
  • 58
    • 0033166537 scopus 로고    scopus 로고
    • Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins
    • Tu J. C., Xiao B., Naisbitt S. et al. (1999) Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins. Neuron 23, 583 592.
    • (1999) Neuron , vol.23 , pp. 583-592
    • Tu, J.C.1    Xiao, B.2    Naisbitt, S.3
  • 60
    • 0034788270 scopus 로고    scopus 로고
    • An ER retention signal explains differences in surface expression of NMDA and AMPA receptor subunits
    • Xia H., Hornby Z. D. Malenka R. C. (2001) An ER retention signal explains differences in surface expression of NMDA and AMPA receptor subunits. Neuropharmacology 41, 714 723.
    • (2001) Neuropharmacology , vol.41 , pp. 714-723
    • Xia, H.1    Hornby, Z.D.2    Malenka, R.C.3
  • 61
    • 0037447231 scopus 로고    scopus 로고
    • 14-3-3 dimers probe the assembly status of multimeric membrane proteins
    • Yuan H., Michelsen K. Schwappach B. (2003) 14-3-3 dimers probe the assembly status of multimeric membrane proteins. Curr. Biol. 13, 638 646.
    • (2003) Curr. Biol. , vol.13 , pp. 638-646
    • Yuan, H.1    Michelsen, K.2    Schwappach, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.