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Volumn 2, Issue 3, 2005, Pages 209-223

Unraveling the dopamine receptor signalplex by DRIPs and DRAPs

Author keywords

Cell signaling; Dopamine receptor; G protein coupled receptor; Interacting proteins; Macromolecular complex; Neurodegenerative disease; Receptor protein interaction; Signaling complex; Signalplex

Indexed keywords


EID: 28844488474     PISSN: 15701646     EISSN: None     Source Type: Journal    
DOI: 10.2174/157016405774641174     Document Type: Review
Times cited : (6)

References (150)
  • 1
    • 24644507172 scopus 로고    scopus 로고
    • Existence and theoretical aspects of homomeric and heteromeric dopamine receptor complexes and their relevance for neurological diseases
    • Agnati, L. F., Ferre, S., Burioni, R., Woods, A., Genedani, S., Franco, R. and Fuxe, K. (2005). Existence and theoretical aspects of homomeric and heteromeric dopamine receptor complexes and their relevance for neurological diseases. Neuromol. Med. 7: 61-78.
    • (2005) Neuromol. Med. , vol.7 , pp. 61-78
    • Agnati, L.F.1    Ferre, S.2    Burioni, R.3    Woods, A.4    Genedani, S.5    Franco, R.6    Fuxe, K.7
  • 5
    • 4444368049 scopus 로고    scopus 로고
    • Abnormalities in the dopamine system in schizophrenia may lie in altered levels of dopamine receptor-interacting proteins
    • Bai, J., He, F., Novikova, S. I., Undie, A. S., Dracheva, S., Haroutunian, V. and Lidow, M. S. (2004). Abnormalities in the dopamine system in schizophrenia may lie in altered levels of dopamine receptor-interacting proteins. Biol. Psychiatry 56: 427-40.
    • (2004) Biol. Psychiatry , vol.56 , pp. 427-440
    • Bai, J.1    He, F.2    Novikova, S.I.3    Undie, A.S.4    Dracheva, S.5    Haroutunian, V.6    Lidow, M.S.7
  • 6
    • 0030045605 scopus 로고    scopus 로고
    • A protein linkage map of Escherichia coli bacteriophage T7
    • Bartel, P. L., Roecklein, J. A., Sengupta, D. and Fields, S. (1996). A protein linkage map of Escherichia coli bacteriophage T7. Nat. Genet. 12: 72-7.
    • (1996) Nat. Genet. , vol.12 , pp. 72-77
    • Bartel, P.L.1    Roecklein, J.A.2    Sengupta, D.3    Fields, S.4
  • 8
    • 22744449073 scopus 로고    scopus 로고
    • An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior
    • Beaulieu, J. M., Sotnikova, T. D., Marion, S., Lefkowitz, R. J., Gainetdinov, R. R. and Caron, M. G. (2005). An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior. Cell 122: 261-73.
    • (2005) Cell , vol.122 , pp. 261-273
    • Beaulieu, J.M.1    Sotnikova, T.D.2    Marion, S.3    Lefkowitz, R.J.4    Gainetdinov, R.R.5    Caron, M.G.6
  • 9
    • 0042880916 scopus 로고    scopus 로고
    • Dopamine receptor-interacting proteins: The Ca(2+) connection in dopamine signaling
    • Bergson, C., Levenson, R., Goldman-Rakic, P. S. and Lidow, M. S. (2003). Dopamine receptor-interacting proteins: the Ca(2+) connection in dopamine signaling. Trends Pharmacol. Sci. 24: 486-92.
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 486-492
    • Bergson, C.1    Levenson, R.2    Goldman-Rakic, P.S.3    Lidow, M.S.4
  • 10
    • 0025166071 scopus 로고
    • Inhibition by dopamine of (Na(+)+K+)ATPase activity in neostriatal neurons through D1 and D2 dopamine receptor synergism
    • Bertorello, A. M., Hopfield, J. F., Aperia, A. and Greengard, P. (1990). Inhibition by dopamine of (Na(+)+K+)ATPase activity in neostriatal neurons through D1 and D2 dopamine receptor synergism. Nature 347: 386-8.
    • (1990) Nature , vol.347 , pp. 386-388
    • Bertorello, A.M.1    Hopfield, J.F.2    Aperia, A.3    Greengard, P.4
  • 11
    • 0036765857 scopus 로고    scopus 로고
    • D2 and D3 dopamine receptor cell surface localization mediated by interaction with protein 4.1N
    • Binda, A. V., Kabbani, N., Lin, R. and Levenson, R. (2002). D2 and D3 dopamine receptor cell surface localization mediated by interaction with protein 4.1N. Mol. Pharmacol. 62: 507-13.
    • (2002) Mol. Pharmacol. , vol.62 , pp. 507-513
    • Binda, A.V.1    Kabbani, N.2    Lin, R.3    Levenson, R.4
  • 12
    • 18044377786 scopus 로고    scopus 로고
    • Regulation of dense core vesicle release from PC12 cells by interaction between the D2 dopamine receptor and calcium-dependent activator protein for secretion (CAPS)
    • Binda, A. V., Kabbani, N. and Levenson, R. (2005). Regulation of dense core vesicle release from PC12 cells by interaction between the D2 dopamine receptor and calcium-dependent activator protein for secretion (CAPS). Biochem. Pharmacol. 69: 1451-61.
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 1451-1461
    • Binda, A.V.1    Kabbani, N.2    Levenson, R.3
  • 15
    • 0034692687 scopus 로고    scopus 로고
    • Binding of calmodulin to the D2-dopamine receptor reduces receptor signaling by arresting the G protein activation switch
    • Bofill-Cardona, E., Kudlacek, O., Yang, Q., Ahorn, H., Freissmuth, M. and Nanoff, C. (2000). Binding of calmodulin to the D2-dopamine receptor reduces receptor signaling by arresting the G protein activation switch. J. Biol. Chem. 275: 32672-80.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32672-32680
    • Bofill-Cardona, E.1    Kudlacek, O.2    Yang, Q.3    Ahorn, H.4    Freissmuth, M.5    Nanoff, C.6
  • 16
    • 23044434010 scopus 로고    scopus 로고
    • The Dopamine D2 Receptor: New Surprises from an Old Friend
    • Bonci, A. and Hopf, F. W. (2005). The Dopamine D2 Receptor: New Surprises from an Old Friend. Neuron 47: 335-338.
    • (2005) Neuron , vol.47 , pp. 335-338
    • Bonci, A.1    Hopf, F.W.2
  • 17
    • 0035318509 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled transmitter receptors
    • Bouvier, M. (2001). Oligomerization of G-protein-coupled transmitter receptors. Nat. Rev. Neurosci. 2: 274-86.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 274-286
    • Bouvier, M.1
  • 18
    • 0034610353 scopus 로고    scopus 로고
    • Probing the three-dimensional structure of human calreticulin
    • Bouvier, M. and Stafford, W. F. (2000). Probing the three-dimensional structure of human calreticulin. Biochemistry 39: 14950-9.
    • (2000) Biochemistry , vol.39 , pp. 14950-14959
    • Bouvier, M.1    Stafford, W.F.2
  • 19
    • 0041355213 scopus 로고    scopus 로고
    • Spinophilin stabilizes cell surface expression of alpha 2B-adrenergic receptors
    • Brady, A. E., Wang, Q., Colbran, R. J., Allen, P. B., Greengard, P. and Limbird, L. E. (2003). Spinophilin stabilizes cell surface expression of alpha 2B-adrenergic receptors. J. Biol. Chem. 278: 32405-12.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32405-32412
    • Brady, A.E.1    Wang, Q.2    Colbran, R.J.3    Allen, P.B.4    Greengard, P.5    Limbird, L.E.6
  • 20
    • 17844410054 scopus 로고    scopus 로고
    • Alpha 2-adrenergic agonist enrichment of spinophilin at the cell surface involves beta gamma subunits of Gi proteins and is preferentially induced by the alpha 2A-subtype
    • Brady, A. E., Wang, Q., Allen, P. B., Rizzo, M., Greengard, P. and Limbird, L. E. (2005). Alpha 2-adrenergic agonist enrichment of spinophilin at the cell surface involves beta gamma subunits of Gi proteins and is preferentially induced by the alpha 2A-subtype. Mol. Pharmacol. 67: 1690-6.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1690-1696
    • Brady, A.E.1    Wang, Q.2    Allen, P.B.3    Rizzo, M.4    Greengard, P.5    Limbird, L.E.6
  • 22
    • 0031804503 scopus 로고    scopus 로고
    • Signaling complexes: Biophysical constraints on intracellular communication
    • Bray, D. (1998). Signaling complexes: biophysical constraints on intracellular communication. Annu. Rev. Biophys. Biomol. Struct. 27: 59-75.
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 59-75
    • Bray, D.1
  • 23
    • 0034814469 scopus 로고    scopus 로고
    • Effects of neuromodulation in a cortical network model of object working memory dominated by recurrent inhibition
    • Brunel, N. and Wang, X. J. (2001). Effects of neuromodulation in a cortical network model of object working memory dominated by recurrent inhibition. J. Comput. Neurosci. 11: 63-85.
    • (2001) J. Comput. Neurosci. , vol.11 , pp. 63-85
    • Brunel, N.1    Wang, X.J.2
  • 26
    • 0026611121 scopus 로고
    • Coactivation of D1 and D2 dopamine receptors is required for long-term synaptic depression in the striatum
    • Calabresi, P., Maj, R., Mercuri, N. B. and Bernardi, G. (1992a). Coactivation of D1 and D2 dopamine receptors is required for long-term synaptic depression in the striatum. Neurosci. Lett. 142: 95-9.
    • (1992) Neurosci. Lett. , vol.142 , pp. 95-99
    • Calabresi, P.1    Maj, R.2    Mercuri, N.B.3    Bernardi, G.4
  • 27
    • 0026526276 scopus 로고
    • Long-term synaptic depression in the striatum: Physiological and pharmacological characterization
    • Calabresi, P., Maj, R., Pisani, A., Mercuri, N. B. and Bernardi, G. (1992b). Long-term synaptic depression in the striatum: physiological and pharmacological characterization. J. Neurosci. 12: 4224-33.
    • (1992) J. Neurosci. , vol.12 , pp. 4224-4233
    • Calabresi, P.1    Maj, R.2    Pisani, A.3    Mercuri, N.B.4    Bernardi, G.5
  • 28
    • 0344875553 scopus 로고    scopus 로고
    • Adenosine A2A-dopamine D2 receptor-receptor heteromerization: Qualitative and quantitative assessment by fluorescence and bioluminescence energy transfer
    • Canals, M., Marcellino, D., Fanelli, F., Ciruela, F., De Benedetti, P., Goldberg, S. R., Neve, K., Fuxe, K., et al. (2003). Adenosine A2A-dopamine D2 receptor-receptor heteromerization: qualitative and quantitative assessment by fluorescence and bioluminescence energy transfer. J. Biol. Chem. 278: 46741-9.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46741-46749
    • Canals, M.1    Marcellino, D.2    Fanelli, F.3    Ciruela, F.4    De Benedetti, P.5    Goldberg, S.R.6    Neve, K.7    Fuxe, K.8
  • 29
    • 2142760058 scopus 로고    scopus 로고
    • Proteomics in postgenomic neuroscience: The end of the beginning
    • Choudhary, J. and Grant, S. G. (2004). Proteomics in postgenomic neuroscience: the end of the beginning. Nat. Neurosci. 7: 440-5.
    • (2004) Nat. Neurosci. , vol.7 , pp. 440-445
    • Choudhary, J.1    Grant, S.G.2
  • 30
    • 4544278502 scopus 로고    scopus 로고
    • Combining mass spectrometry and pull-down techniques for the study of receptor heteromerization. Direct epitope-epitope electrostatic interactions between adenosine A2A and dopamine D2 receptors
    • Ciruela, F., Burgueno, J., Casado, V., Canals, M., Marcellino, D., Goldberg, S. R., Bader, M., Fuxe, K., et al. (2004). Combining mass spectrometry and pull-down techniques for the study of receptor heteromerization. Direct epitope-epitope electrostatic interactions between adenosine A2A and dopamine D2 receptors. Anal. Chem. 76: 5354-63.
    • (2004) Anal. Chem. , vol.76 , pp. 5354-5363
    • Ciruela, F.1    Burgueno, J.2    Casado, V.3    Canals, M.4    Marcellino, D.5    Goldberg, S.R.6    Bader, M.7    Fuxe, K.8
  • 31
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • Clapham, D. E. (2003). TRP channels as cellular sensors. Nature 426: 517-24.
    • (2003) Nature , vol.426 , pp. 517-524
    • Clapham, D.E.1
  • 32
    • 0033811553 scopus 로고    scopus 로고
    • Synaptic mechanisms and network dynamics underlying spatial working memory in a cortical network model
    • Compte, A., Brunel, N., Goldman-Rakic, P. S. and Wang, X. J. (2000). Synaptic mechanisms and network dynamics underlying spatial working memory in a cortical network model. Cereb. Cortex 10: 910-23.
    • (2000) Cereb. Cortex , vol.10 , pp. 910-923
    • Compte, A.1    Brunel, N.2    Goldman-Rakic, P.S.3    Wang, X.J.4
  • 33
  • 35
    • 0033012932 scopus 로고    scopus 로고
    • Prostate apoptosis response-4 production in synaptic compartments following apoptotic and excitotoxic insults: Evidence for a pivotal role in mitochondrial dysfunction and neuronal degeneration
    • Duan, W., Rangnekar, V. M. and Mattson, M. P. (1999). Prostate apoptosis response-4 production in synaptic compartments following apoptotic and excitotoxic insults: evidence for a pivotal role in mitochondrial dysfunction and neuronal degeneration. J. Neurochem. 72: 2312-22.
    • (1999) J. Neurochem. , vol.72 , pp. 2312-2322
    • Duan, W.1    Rangnekar, V.M.2    Mattson, M.P.3
  • 37
    • 0037101776 scopus 로고    scopus 로고
    • G-protein-coupled receptors for neurotransmitter amino acids: C-terminal tails, crowded signalosomes
    • El Far, O. and Betz, H. (2002). G-protein-coupled receptors for neurotransmitter amino acids: C-terminal tails, crowded signalosomes. Biochem. J. 365: 329-36.
    • (2002) Biochem. J. , vol.365 , pp. 329-336
    • El Far, O.1    Betz, H.2
  • 38
    • 0034141207 scopus 로고    scopus 로고
    • Complex interactions between mGluRs, intracellular Ca2+ stores and ion channels in neurons
    • Fagni, L., Chavis, P., Ango, F. and Bockaert, J. (2000). Complex interactions between mGluRs, intracellular Ca2+ stores and ion channels in neurons. Trends Neurosci. 23: 80-8.
    • (2000) Trends Neurosci. , vol.23 , pp. 80-88
    • Fagni, L.1    Chavis, P.2    Ango, F.3    Bockaert, J.4
  • 39
  • 40
    • 0035101820 scopus 로고    scopus 로고
    • Evolving concepts in G protein-coupled receptor endocytosis: The role in receptor desensitization and signaling
    • Ferguson, S. S. (2001). Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling. Pharmacol. Rev. 53: 1-24.
    • (2001) Pharmacol. Rev. , vol.53 , pp. 1-24
    • Ferguson, S.S.1
  • 42
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S. and Song, O. (1989). A novel genetic system to detect protein-protein interactions. Nature 340: 245-6.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 43
    • 10644269916 scopus 로고    scopus 로고
    • Oligomeric assembly of dopamine D1 and glutamate NMDA receptors: Molecular mechanisms and functional implications
    • Fiorentini, C. and Missale, C. (2004). Oligomeric assembly of dopamine D1 and glutamate NMDA receptors: molecular mechanisms and functional implications. Biochem. Soc. Trans. 32: 1025-8.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 1025-1028
    • Fiorentini, C.1    Missale, C.2
  • 46
    • 3042670429 scopus 로고    scopus 로고
    • Molecular and functional characterization of proteins interacting with the C-terminal domains of 5-HT2 receptors: Emergence of 5-HT2 "receptosomes"
    • Gavarini, S., Becamel, C., Chanrion, B., Bockaert, J. and Marin, P. (2004). Molecular and functional characterization of proteins interacting with the C-terminal domains of 5-HT2 receptors: emergence of 5-HT2 "receptosomes". Biol. Cell 96: 373-81.
    • (2004) Biol. Cell , vol.96 , pp. 373-381
    • Gavarini, S.1    Becamel, C.2    Chanrion, B.3    Bockaert, J.4    Marin, P.5
  • 47
    • 1842861706 scopus 로고    scopus 로고
    • Differential effects of regulator of G protein signaling (RGS) proteins on serotonin 5-HT1A, 5-HT2A, and dopamine D2 receptor-mediated signaling and adenylyl cyclase activity
    • Ghavami, A., Hunt, R. A., Olsen, M. A., Zhang, J., Smith, D. L., Kalgaonkar, S., Rahman, Z. and Young, K. H. (2004). Differential effects of regulator of G protein signaling (RGS) proteins on serotonin 5-HT1A, 5-HT2A, and dopamine D2 receptor-mediated signaling and adenylyl cyclase activity. Cell Signal. 16: 711-21.
    • (2004) Cell Signal. , vol.16 , pp. 711-721
    • Ghavami, A.1    Hunt, R.A.2    Olsen, M.A.3    Zhang, J.4    Smith, D.L.5    Kalgaonkar, S.6    Rahman, Z.7    Young, K.H.8
  • 50
    • 2442467014 scopus 로고    scopus 로고
    • The neurobiology of dopamine signaling
    • Girault, J. A. and Greengard, P. (2004). The neurobiology of dopamine signaling. Arch. Neurol. 61: 641-4.
    • (2004) Arch. Neurol. , vol.61 , pp. 641-644
    • Girault, J.A.1    Greengard, P.2
  • 51
    • 77956751404 scopus 로고    scopus 로고
    • The cortical dopamine system: Role in memory and cognition
    • Goldman-Rakic, P. S. (1998). The cortical dopamine system: role in memory and cognition. Adv. Pharmacol. 42: 707-11.
    • (1998) Adv. Pharmacol. , vol.42 , pp. 707-711
    • Goldman-Rakic, P.S.1
  • 53
    • 1842455769 scopus 로고    scopus 로고
    • The X-linked mental retardation protein oligophrenin-1 is required for dendritic spine morphogenesis
    • Govek, E. E., Newey, S. E., Akerman, C. J., Cross, J. R., Van Der Veken, L. and Van Aelst, L. (2004). The X-linked mental retardation protein oligophrenin-1 is required for dendritic spine morphogenesis. Nat. Neurosci. 7: 364-72.
    • (2004) Nat. Neurosci. , vol.7 , pp. 364-372
    • Govek, E.E.1    Newey, S.E.2    Akerman, C.J.3    Cross, J.R.4    Van Der Veken, L.5    Van Aelst, L.6
  • 54
    • 0035503379 scopus 로고    scopus 로고
    • Proteomics in neuroscience: From protein to network
    • Grant, S. G. and Blackstock, W. P. (2001). Proteomics in neuroscience: from protein to network. J. Neurosci. 21: 8315-8.
    • (2001) J. Neurosci. , vol.21 , pp. 8315-8318
    • Grant, S.G.1    Blackstock, W.P.2
  • 55
    • 0035370012 scopus 로고    scopus 로고
    • Multiprotein complex signaling and the plasticity problem
    • Grant, S. G. and O'Dell, T. J. (2001). Multiprotein complex signaling and the plasticity problem. Curr. Opin. Neurobiol. 11: 363-8.
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 363-368
    • Grant, S.G.1    O'Dell, T.J.2
  • 57
    • 0141783682 scopus 로고    scopus 로고
    • CLIC6, a member of the intracellular chloride channel family, interacts with dopamine D(2)-like receptors
    • Griffon, N., Jeanneteau, F., Prieur, F., Diaz, J. and Sokoloff, P. (2003). CLIC6, a member of the intracellular chloride channel family, interacts with dopamine D(2)-like receptors. Brain Res. Mol. Brain Res. 117: 47-57.
    • (2003) Brain Res. Mol. Brain Res. , vol.117 , pp. 47-57
    • Griffon, N.1    Jeanneteau, F.2    Prieur, F.3    Diaz, J.4    Sokoloff, P.5
  • 58
    • 0037077255 scopus 로고    scopus 로고
    • Membrane association domains in Ca2+-dependent activator protein for secretion mediate plasma membrane and dense-core vesicle binding required for Ca2+-dependent exocytosis
    • Grishanin, R. N., Klenchin, V. A., Loyet, K. M., Kowalchyk, J. A., Ann, K. and Martin, T. F. (2002). Membrane association domains in Ca2+-dependent activator protein for secretion mediate plasma membrane and dense-core vesicle binding required for Ca2+-dependent exocytosis. J. Biol. Chem. 277: 22025-34.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22025-22034
    • Grishanin, R.N.1    Klenchin, V.A.2    Loyet, K.M.3    Kowalchyk, J.A.4    Ann, K.5    Martin, T.F.6
  • 60
    • 3142671973 scopus 로고    scopus 로고
    • Spinophilin is phosphorylated by Ca2+/calmodulin-dependent protein kinase II resulting in regulation of its binding to F-actin
    • Grossman, S. D., Futter, M., Snyder, G. L., Allen, P. B., Nairn, A. C., Greengard, P. and Hsieh-Wilson, L. C. (2004). Spinophilin is phosphorylated by Ca2+/calmodulin-dependent protein kinase II resulting in regulation of its binding to F-actin. J. Neurochem. 90: 317-24.
    • (2004) J. Neurochem. , vol.90 , pp. 317-324
    • Grossman, S.D.1    Futter, M.2    Snyder, G.L.3    Allen, P.B.4    Nairn, A.C.5    Greengard, P.6    Hsieh-Wilson, L.C.7
  • 61
    • 9744226444 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors and striatal synaptic plasticity: Implications for neurological diseases
    • Gubellini, P., Pisani, A., Centonze, D., Bernardi, G. and Calabresi, P. (2004). Metabotropic glutamate receptors and striatal synaptic plasticity: implications for neurological diseases. Prog. Neurobiol. 74: 271-300.
    • (2004) Prog. Neurobiol. , vol.74 , pp. 271-300
    • Gubellini, P.1    Pisani, A.2    Centonze, D.3    Bernardi, G.4    Calabresi, P.5
  • 62
    • 0029075363 scopus 로고
    • The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin
    • Hanson, P. I., Otto, H., Barton, N. and Jahn, R. (1995). The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin. J. Biol. Chem. 270: 16955-61.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16955-16961
    • Hanson, P.I.1    Otto, H.2    Barton, N.3    Jahn, R.4
  • 63
    • 0037124032 scopus 로고    scopus 로고
    • Coaggregation, cointernalization, and codesensitization of adenosine A2A receptors and dopamine D2 receptors
    • Hillion, J., Canals, M., Torvinen, M., Casado, V., Scott, R., Terasmaa, A., Hansson, A., Watson, S., et al. (2002). Coaggregation, cointernalization, and codesensitization of adenosine A2A receptors and dopamine D2 receptors. J. Biol. Chem. 277: 18091-7.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18091-18097
    • Hillion, J.1    Canals, M.2    Torvinen, M.3    Casado, V.4    Scott, R.5    Terasmaa, A.6    Hansson, A.7    Watson, S.8
  • 64
    • 0033946468 scopus 로고    scopus 로고
    • Proteomic analysis of NMDA receptor-adhesion protein signaling complexes
    • Husi, H., Ward, M. A., Choudhary, J. S., Blackstock, W. P. and Grant, S. G. (2000). Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. Nat. Neurosci. 3: 661-9.
    • (2000) Nat. Neurosci. , vol.3 , pp. 661-669
    • Husi, H.1    Ward, M.A.2    Choudhary, J.S.3    Blackstock, W.P.4    Grant, S.G.5
  • 65
    • 0742270638 scopus 로고    scopus 로고
    • Interactions of GIPC with dopamine D2, D3 but not D4 receptors define a novel mode of regulation of G protein-coupled receptors
    • Jeanneteau, F., Diaz, J., Sokoloff, P. and Griffon, N. (2004a). Interactions of GIPC with dopamine D2, D3 but not D4 receptors define a novel mode of regulation of G protein-coupled receptors. Mol. Biol. Cell 15: 696-705.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 696-705
    • Jeanneteau, F.1    Diaz, J.2    Sokoloff, P.3    Griffon, N.4
  • 66
    • 6344241436 scopus 로고    scopus 로고
    • GIPC recruits GAIP (RGS19) to attenuate dopamine D2 receptor signaling
    • Jeanneteau, F., Guillin, O., Diaz, J., Griffon, N. and Sokoloff, P. (2004b). GIPC recruits GAIP (RGS19) to attenuate dopamine D2 receptor signaling. Mol. Biol. Cell 15: 4926-37.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4926-4937
    • Jeanneteau, F.1    Guillin, O.2    Diaz, J.3    Griffon, N.4    Sokoloff, P.5
  • 67
    • 10544225383 scopus 로고    scopus 로고
    • A novel repressor, par-4, modulates transcription and growth suppression functions of the Wilms' tumor suppressor WT1
    • Johnstone, R. W., See, R. H., Sells, S. F., Wang, J., Muthukkumar, S., Englert, C., Haber, D. A., Licht, J. D., et al. (1996). A novel repressor, par-4, modulates transcription and growth suppression functions of the Wilms' tumor suppressor WT1. Mol. Cell Biol. 16: 6945-56.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 6945-6956
    • Johnstone, R.W.1    See, R.H.2    Sells, S.F.3    Wang, J.4    Muthukkumar, S.5    Englert, C.6    Haber, D.A.7    Licht, J.D.8
  • 68
    • 28844452141 scopus 로고    scopus 로고
    • A role for the neuronal calcium sensor NCS-1 in modulating GRK-mediated desensitization of the D2 receptor
    • Program No. 542.2 Society for Neuroscience 2002
    • Kabbani, N., and Levenson, R. (2002). A role for the neuronal calcium sensor NCS-1 in modulating GRK-mediated desensitization of the D2 receptor. Program No. 542.2 Abstract Viewer/ Itinerary Planner, Society for Neuroscience 2002.
    • (2002) Abstract Viewer/ Itinerary Planner
    • Kabbani, N.1    Levenson, R.2
  • 69
    • 0036813090 scopus 로고    scopus 로고
    • Interaction with neuronal calcium sensor NCS-1 mediates desensitization of the D2 dopamine receptor
    • Kabbani, N., Negyessy, L., Lin, R., Goldman-Rakic, P. and Levenson, R. (2002). Interaction with neuronal calcium sensor NCS-1 mediates desensitization of the D2 dopamine receptor. J. Neurosci. 22: 8476-86.
    • (2002) J. Neurosci. , vol.22 , pp. 8476-8486
    • Kabbani, N.1    Negyessy, L.2    Lin, R.3    Goldman-Rakic, P.4    Levenson, R.5
  • 70
    • 0346725001 scopus 로고    scopus 로고
    • Dynamin-2 associates with the dopamine receptor signalplex and regulates internalization of activated D2 receptors
    • Kabbani, N., Jeromin, A. and Levenson, R. (2004). Dynamin-2 associates with the dopamine receptor signalplex and regulates internalization of activated D2 receptors. Cell Signal. 16: 497-503.
    • (2004) Cell Signal. , vol.16 , pp. 497-503
    • Kabbani, N.1    Jeromin, A.2    Levenson, R.3
  • 71
    • 0037870163 scopus 로고    scopus 로고
    • Oligomerization of adenosine A2A and dopamine D2 receptors in living cells
    • Kamiya, T., Saitoh, O., Yoshioka, K. and Nakata, H. (2003). Oligomerization of adenosine A2A and dopamine D2 receptors in living cells. Biochem. Biophys. Res. Commun. 306: 544-9.
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 544-549
    • Kamiya, T.1    Saitoh, O.2    Yoshioka, K.3    Nakata, H.4
  • 72
    • 17844410926 scopus 로고    scopus 로고
    • Concurrent stimulation of cannabinoid CB1 and dopamine D2 receptors enhances heterodimer formation: A mechanism for receptor cross-talk?
    • Kearn, C. S., Blake-Palmer, K., Daniel, E., Mackie, K. and Glass, M. (2005). Concurrent stimulation of cannabinoid CB1 and dopamine D2 receptors enhances heterodimer formation: a mechanism for receptor cross-talk? Mol. Pharmacol. 67: 1697-704.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1697-1704
    • Kearn, C.S.1    Blake-Palmer, K.2    Daniel, E.3    Mackie, K.4    Glass, M.5
  • 73
    • 0030756892 scopus 로고    scopus 로고
    • Endocytosis and recycling of G protein-coupled receptors
    • Koenig, J. A. and Edwardson, J. M. (1997). Endocytosis and recycling of G protein-coupled receptors. Trends Pharmacol. Sci. 18: 276-87.
    • (1997) Trends Pharmacol. Sci. , vol.18 , pp. 276-287
    • Koenig, J.A.1    Edwardson, J.M.2
  • 74
    • 0037422584 scopus 로고    scopus 로고
    • Up-regulation of neuronal calcium sensor-1 (NCS-1) in the prefrontal cortex of schizophrenic and bipolar patients
    • Koh, P. O., Undie, A. S., Kabbani, N., Levenson, R., Goldman-Rakic, P. S. and Lidow, M. S. (2003). Up-regulation of neuronal calcium sensor-1 (NCS-1) in the prefrontal cortex of schizophrenic and bipolar patients. Proc. Natl. Acad. Sci. USA 100: 313-7.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 313-317
    • Koh, P.O.1    Undie, A.S.2    Kabbani, N.3    Levenson, R.4    Goldman-Rakic, P.S.5    Lidow, M.S.6
  • 75
    • 0036783234 scopus 로고    scopus 로고
    • Organisation of G-protein-coupled receptor signalling complexes by scaffolding proteins
    • Kreienkamp, H. J. (2002). Organisation of G-protein-coupled receptor signalling complexes by scaffolding proteins. Curr. Opin. Pharmacol. 2: 581-6.
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 581-586
    • Kreienkamp, H.J.1
  • 76
    • 0031747997 scopus 로고    scopus 로고
    • The role of receptor kinases and arrestins in G protein-coupled receptor regulation
    • Krupnick, J. G. and Benovic, J. L. (1998). The role of receptor kinases and arrestins in G protein-coupled receptor regulation. Annu. Rev. Pharmacol. Toxicol. 38: 289-319.
    • (1998) Annu. Rev. Pharmacol. Toxicol. , vol.38 , pp. 289-319
    • Krupnick, J.G.1    Benovic, J.L.2
  • 77
    • 0037195909 scopus 로고    scopus 로고
    • G protein-coupled receptors form stable complexes with inwardly rectifying potassium channels and adenylyl cyclase
    • Lavine, N., Ethier, N., Oak, J. N., Pei, L., Liu, F., Trieu, P., Rebois, R. V., Bouvier, M., et al. (2002). G protein-coupled receptors form stable complexes with inwardly rectifying potassium channels and adenylyl cyclase. J. Biol. Chem. 277: 46010-9.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46010-46019
    • Lavine, N.1    Ethier, N.2    Oak, J.N.3    Pei, L.4    Liu, F.5    Trieu, P.6    Rebois, R.V.7    Bouvier, M.8
  • 79
    • 18644386370 scopus 로고    scopus 로고
    • Dual regulation of NMDA receptor functions by direct protein-protein interactions with the dopamine D1 receptor
    • Lee, F. J., Xue, S., Pei, L., Vukusic, B., Chery, N., Wang, Y., Wang, Y. T., Niznik, H. B., et al. (2002). Dual regulation of NMDA receptor functions by direct protein-protein interactions with the dopamine D1 receptor. Cell 111: 219-30.
    • (2002) Cell , vol.111 , pp. 219-230
    • Lee, F.J.1    Xue, S.2    Pei, L.3    Vukusic, B.4    Chery, N.5    Wang, Y.6    Wang, Y.T.7    Niznik, H.B.8
  • 80
    • 25844469660 scopus 로고    scopus 로고
    • Direct receptor cross-talk can mediate the modulation of excitatory and inhibitory neurotransmission by dopamine
    • Lee, F. J., Wang, Y. T. and Liu, F. (2005). Direct receptor cross-talk can mediate the modulation of excitatory and inhibitory neurotransmission by dopamine. J. Mol. Neurosci. 26: 245-52.
    • (2005) J. Mol. Neurosci. , vol.26 , pp. 245-252
    • Lee, F.J.1    Wang, Y.T.2    Liu, F.3
  • 81
    • 0033924207 scopus 로고    scopus 로고
    • Inhibition of cell surface expression by mutant receptors demonstrates that D2 dopamine receptors exist as oligomers in the cell
    • Lee, S. P., O'dowd, B. F., Ng, G. Y., Varghese, G., Akil, H., Mansour, A., Nguyen, T. and George, S. R. (2000). Inhibition of cell surface expression by mutant receptors demonstrates that D2 dopamine receptors exist as oligomers in the cell. Mol. Pharmacol. 58: 120-8.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 120-128
    • Lee, S.P.1    O'Dowd, B.F.2    Ng, G.Y.3    Varghese, G.4    Akil, H.5    Mansour, A.6    Nguyen, T.7    George, S.R.8
  • 82
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by beta-arrestins
    • Lefkowitz, R. J. and Shenoy, S. K. (2005). Transduction of receptor signals by beta-arrestins. Science 308: 512-7.
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 83
    • 0034089048 scopus 로고    scopus 로고
    • Modulation of dopamine D(2) receptor signaling by actin-binding protein (ABP-280)
    • Li, M., Bermak, J. C., Wang, Z. W. and Zhou, Q. Y. (2000). Modulation of dopamine D(2) receptor signaling by actin-binding protein (ABP-280). Mol. Pharmacol. 57: 446-52.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 446-452
    • Li, M.1    Bermak, J.C.2    Wang, Z.W.3    Zhou, Q.Y.4
  • 85
    • 0035942279 scopus 로고    scopus 로고
    • Dopamine D2 and D3 receptors are linked to the actin cytoskeleton via interaction with filamin A
    • Lin, R., Karpa, K., Kabbani, N., Goldman-Rakic, P. and Levenson, R. (2001). Dopamine D2 and D3 receptors are linked to the actin cytoskeleton via interaction with filamin A. Proc. Natl. Acad. Sci. USA 98: 5258-63.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5258-5263
    • Lin, R.1    Karpa, K.2    Kabbani, N.3    Goldman-Rakic, P.4    Levenson, R.5
  • 86
    • 0036966954 scopus 로고    scopus 로고
    • Dominant negative mutants of filamin A block cell surface expression of the D2 dopamine receptor
    • Lin, R., Canfield, V. and Levenson, R. (2002). Dominant negative mutants of filamin A block cell surface expression of the D2 dopamine receptor. Pharmacology 66: 173-81.
    • (2002) Pharmacology , vol.66 , pp. 173-181
    • Lin, R.1    Canfield, V.2    Levenson, R.3
  • 87
    • 0037386738 scopus 로고    scopus 로고
    • Distinct roles of dopamine D2L and D2S receptor isoforms in the regulation of protein phosphorylation at presynaptic and postsynaptic sites
    • Lindgren, N., Usiello, A., Goiny, M., Haycock, J., Erbs, E., Greengard, P., Hokfelt, T., Borrelli, E., et al. (2003). Distinct roles of dopamine D2L and D2S receptor isoforms in the regulation of protein phosphorylation at presynaptic and postsynaptic sites. Proc. Natl. Acad. Sci. USA 100: 4305-9.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4305-4309
    • Lindgren, N.1    Usiello, A.2    Goiny, M.3    Haycock, J.4    Erbs, E.5    Greengard, P.6    Hokfelt, T.7    Borrelli, E.8
  • 88
    • 0034688225 scopus 로고    scopus 로고
    • Direct protein-protein coupling enables cross-talk between dopamine D5 and gamma-aminobutyric acid A receptors
    • Liu, F., Wan, Q., Pristupa, Z. B., Yu, X. M., Wang, Y. T. and Niznik, H. B. (2000). Direct protein-protein coupling enables cross-talk between dopamine D5 and gamma-aminobutyric acid A receptors. Nature 403: 274-80.
    • (2000) Nature , vol.403 , pp. 274-280
    • Liu, F.1    Wan, Q.2    Pristupa, Z.B.3    Yu, X.M.4    Wang, Y.T.5    Niznik, H.B.6
  • 90
    • 9444280897 scopus 로고    scopus 로고
    • Preferential Interaction between the dopamine D2 receptor and Arrestin2 in neostriatal neurons
    • Macey, T. A., Gurevich, V. V. and Neve, K. A. (2004). Preferential Interaction between the dopamine D2 receptor and Arrestin2 in neostriatal neurons. Mol. Pharmacol. 66: 1635-42.
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1635-1642
    • Macey, T.A.1    Gurevich, V.V.2    Neve, K.A.3
  • 91
    • 0035034203 scopus 로고    scopus 로고
    • The cellular neurobiology of depression
    • Manji, H. K., Drevets, W. C. and Charney, D. S. (2001). The cellular neurobiology of depression. Nat. Med. 7: 541-7.
    • (2001) Nat. Med. , vol.7 , pp. 541-547
    • Manji, H.K.1    Drevets, W.C.2    Charney, D.S.3
  • 92
    • 9244264418 scopus 로고    scopus 로고
    • D2 dopamine receptor-mediated modulation of voltage-dependent Na+ channels reduces autonomous activity in striatal cholinergic interneurons
    • Maurice, N., Mercer, J., Chan, C. S., Hernandez-Lopez, S., Held, J., Tkatch, T. and Surmeier, D. J. (2004). D2 dopamine receptor-mediated modulation of voltage-dependent Na+ channels reduces autonomous activity in striatal cholinergic interneurons. J. Neurosci. 24: 10289-301.
    • (2004) J. Neurosci. , vol.24 , pp. 10289-10301
    • Maurice, N.1    Mercer, J.2    Chan, C.S.3    Hernandez-Lopez, S.4    Held, J.5    Tkatch, T.6    Surmeier, D.J.7
  • 93
    • 0036157172 scopus 로고    scopus 로고
    • The developing relationship between receptor-operated and store-operated calcium channels in smooth muscle
    • Mcfadzean, I. and Gibson, A. (2002). The developing relationship between receptor-operated and store-operated calcium channels in smooth muscle. Br. J. Pharmacol. 135: 1-13.
    • (2002) Br. J. Pharmacol. , vol.135 , pp. 1-13
    • Mcfadzean, I.1    Gibson, A.2
  • 94
    • 0035478746 scopus 로고    scopus 로고
    • Protein-protein interactions at G-protein-coupled receptors
    • Milligan, G. and White, J. H. (2001). Protein-protein interactions at G-protein-coupled receptors. Trends Pharmacol. Sci. 22: 513-8.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 513-518
    • Milligan, G.1    White, J.H.2
  • 97
    • 12344326514 scopus 로고    scopus 로고
    • Treatments for schizophrenia: A critical review of pharmacology and mechanisms of action of antipsychotic drugs
    • Miyamoto, S., Duncan, G. E., Marx, C. E. and Lieberman, J. A. (2005). Treatments for schizophrenia: a critical review of pharmacology and mechanisms of action of antipsychotic drugs. Mol. Psychiatry 10: 79-104.
    • (2005) Mol. Psychiatry , vol.10 , pp. 79-104
    • Miyamoto, S.1    Duncan, G.E.2    Marx, C.E.3    Lieberman, J.A.4
  • 98
    • 0033280228 scopus 로고    scopus 로고
    • Visual transduction in Drosophila
    • Montell, C. (1999). Visual transduction in Drosophila. Annu. Rev. Cell Dev. Biol. 15: 231-68.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 231-268
    • Montell, C.1
  • 99
    • 0037636295 scopus 로고    scopus 로고
    • The venerable inveterate invertebrate TRP channels
    • Montell, C. (2003). The venerable inveterate invertebrate TRP channels. Cell Calcium 33: 409-17.
    • (2003) Cell Calcium , vol.33 , pp. 409-417
    • Montell, C.1
  • 101
    • 17544368654 scopus 로고    scopus 로고
    • Dopaminergic modulation of neuronal excitability in the striatum and nucleus accumbens
    • Nicola, S. M., Surmeier, J. and Malenka, R. C. (2000). Dopaminergic modulation of neuronal excitability in the striatum and nucleus accumbens. Annu. Rev. Neurosci. 23: 185-215.
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 185-215
    • Nicola, S.M.1    Surmeier, J.2    Malenka, R.C.3
  • 102
    • 0030831116 scopus 로고    scopus 로고
    • Bidirectional regulation of DARPP-32 phosphorylation by dopamine
    • Nishi, A., Snyder, G. L. and Greengard, P. (1997). Bidirectional regulation of DARPP-32 phosphorylation by dopamine. J. Neurosci. 17: 8147-55.
    • (1997) J. Neurosci. , vol.17 , pp. 8147-8155
    • Nishi, A.1    Snyder, G.L.2    Greengard, P.3
  • 104
    • 7544225524 scopus 로고    scopus 로고
    • Cellular and subcellular distribution of spinophilin, a PP1 regulatory protein that bundles F-actin in dendritic spines
    • Ouimet, C. C., Katona, I., Allen, P., Freund, T. F. and Greengard, P. (2004). Cellular and subcellular distribution of spinophilin, a PP1 regulatory protein that bundles F-actin in dendritic spines. J. Comp. Neurol. 479: 374-88.
    • (2004) J. Comp. Neurol. , vol.479 , pp. 374-388
    • Ouimet, C.C.1    Katona, I.2    Allen, P.3    Freund, T.F.4    Greengard, P.5
  • 106
    • 13944252008 scopus 로고    scopus 로고
    • Presynaptic D1 dopamine receptors in primate prefrontal cortex: Target-specific expression in the glutamatergic synapse
    • Paspalas, C. D. and Goldman-Rakic, P. S. (2005). Presynaptic D1 dopamine receptors in primate prefrontal cortex: target-specific expression in the glutamatergic synapse. J. Neurosci. 25: 1260-7.
    • (2005) J. Neurosci. , vol.25 , pp. 1260-1267
    • Paspalas, C.D.1    Goldman-Rakic, P.S.2
  • 107
    • 0032780823 scopus 로고    scopus 로고
    • Somatostatin and its receptor family
    • Patel, Y. C. (1999). Somatostatin and its receptor family. Front. Neuroendocrinol. 20: 157-98.
    • (1999) Front. Neuroendocrinol. , vol.20 , pp. 157-198
    • Patel, Y.C.1
  • 109
    • 0035487327 scopus 로고    scopus 로고
    • Classical and new roles of beta-arrestins in the regulation of G-protein-coupled receptors
    • Pierce, K. L. and Lefkowitz, R. J. (2001). Classical and new roles of beta-arrestins in the regulation of G-protein-coupled receptors. Nat. Rev. Neurosci. 2: 727-33.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 727-733
    • Pierce, K.L.1    Lefkowitz, R.J.2
  • 110
    • 7444255626 scopus 로고    scopus 로고
    • Membrane targeting of lipid modified signal transduction proteins
    • Resh, M. D. (2004). Membrane targeting of lipid modified signal transduction proteins. Subcell. Biochem. 37: 217-32.
    • (2004) Subcell. Biochem. , vol.37 , pp. 217-232
    • Resh, M.D.1
  • 111
    • 0034616021 scopus 로고    scopus 로고
    • Receptors for dopamine and somatostatin: Formation of hetero-oligomers with enhanced functional activity
    • Rocheville, M., Lange, D. C., Kumar, U., Patel, S. C., Patel, R. C. and Patel, Y. C. (2000). Receptors for dopamine and somatostatin: formation of hetero-oligomers with enhanced functional activity. Science 288: 154-7.
    • (2000) Science , vol.288 , pp. 154-157
    • Rocheville, M.1    Lange, D.C.2    Kumar, U.3    Patel, S.C.4    Patel, R.C.5    Patel, Y.C.6
  • 112
    • 0029011541 scopus 로고
    • The endogenous cannabinoid receptor ligand, anandamide, inhibits the motor behavior: Role of nigrostriatal dopaminergic neurons
    • Romero, J., Garcia, L., Cebeira, M., Zadrozny, D., Fernandez-Ruiz, J. J. and Ramos, J. A. (1995). The endogenous cannabinoid receptor ligand, anandamide, inhibits the motor behavior: role of nigrostriatal dopaminergic neurons. Life Sci. 56: 2033-40.
    • (1995) Life Sci. , vol.56 , pp. 2033-2040
    • Romero, J.1    Garcia, L.2    Cebeira, M.3    Zadrozny, D.4    Fernandez-Ruiz, J.J.5    Ramos, J.A.6
  • 113
    • 0242353156 scopus 로고    scopus 로고
    • PI3 kinase enhancer-Homer complex couples mGluRI to PI3 kinase, preventing neuronal apoptosis
    • Rong, R., Ahn, J. Y., Huang, H., Nagata, E., Kalman, D., Kapp, J. A., Tu, J., Worley, P. F., et al. (2003). PI3 kinase enhancer-Homer complex couples mGluRI to PI3 kinase, preventing neuronal apoptosis. Nat. Neurosci. 6: 1153-61.
    • (2003) Nat. Neurosci. , vol.6 , pp. 1153-1161
    • Rong, R.1    Ahn, J.Y.2    Huang, H.3    Nagata, E.4    Kalman, D.5    Kapp, J.A.6    Tu, J.7    Worley, P.F.8
  • 114
    • 0034879863 scopus 로고    scopus 로고
    • Regulation of dendritic spine morphology and synaptic function by Shank and Homer
    • Sala, C., Piech, V., Wilson, N. R., Passafaro, M., Liu, G. and Sheng, M. (2001). Regulation of dendritic spine morphology and synaptic function by Shank and Homer. Neuron 31: 115-30.
    • (2001) Neuron , vol.31 , pp. 115-130
    • Sala, C.1    Piech, V.2    Wilson, N.R.3    Passafaro, M.4    Liu, G.5    Sheng, M.6
  • 115
    • 0031946369 scopus 로고    scopus 로고
    • Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62
    • Sanchez, P., De Carcer, G., Sandoval, I. V., Moscat, J. and Diaz-Meco, M. T. (1998). Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62. Mol. Cell Biol. 18: 3069-80.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 3069-3080
    • Sanchez, P.1    De Carcer, G.2    Sandoval, I.V.3    Moscat, J.4    Diaz-Meco, M.T.5
  • 117
    • 0037057755 scopus 로고    scopus 로고
    • Getting formal with dopamine and reward
    • Schultz, W. (2002). Getting formal with dopamine and reward. Neuron 36: 241-63.
    • (2002) Neuron , vol.36 , pp. 241-263
    • Schultz, W.1
  • 118
    • 0033669189 scopus 로고    scopus 로고
    • A network of protein-protein interactions in yeast
    • Schwikowski, B., Uetz, P. and Fields, S. (2000). A network of protein-protein interactions in yeast. Nat. Biotechnol. 18: 1257-61.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1257-1261
    • Schwikowski, B.1    Uetz, P.2    Fields, S.3
  • 119
    • 0742304657 scopus 로고    scopus 로고
    • The principal features and mechanisms of dopamine modulation in the prefrontal cortex
    • Seamans, J. K. and Yang, C. R. (2004). The principal features and mechanisms of dopamine modulation in the prefrontal cortex. Prog. Neurobiol. 74: 1-58.
    • (2004) Prog. Neurobiol. , vol.74 , pp. 1-58
    • Seamans, J.K.1    Yang, C.R.2
  • 120
    • 0028128734 scopus 로고
    • The D2 dopamine receptor isoforms signal through distinct Gi alpha proteins to inhibit adenylyl cyclase. A study with site-directed mutant Gi alpha proteins
    • Senogles, S. E. (1994). The D2 dopamine receptor isoforms signal through distinct Gi alpha proteins to inhibit adenylyl cyclase. A study with site-directed mutant Gi alpha proteins. J. Biol. Chem. 269: 23120-7.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23120-23127
    • Senogles, S.E.1
  • 121
    • 0345826180 scopus 로고    scopus 로고
    • A region of the third intracellular loop of the short form of the D2 dopamine receptor dictates Gi coupling specificity
    • Senogles, S. E., Heimert, T. L., Odife, E. R. and Quasney, M. W. (2004). A region of the third intracellular loop of the short form of the D2 dopamine receptor dictates Gi coupling specificity. J. Biol. Chem. 279: 1601-6.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1601-1606
    • Senogles, S.E.1    Heimert, T.L.2    Odife, E.R.3    Quasney, M.W.4
  • 122
    • 0033848928 scopus 로고    scopus 로고
    • Coupling of dopamine receptor subtypes to multiple and diverse G proteins
    • Sidhu, A. and Niznik, H. B. (2000). Coupling of dopamine receptor subtypes to multiple and diverse G proteins. Int. J. Dev. Neurosci. 18: 669-77.
    • (2000) Int. J. Dev. Neurosci. , vol.18 , pp. 669-677
    • Sidhu, A.1    Niznik, H.B.2
  • 123
    • 0033538487 scopus 로고    scopus 로고
    • Association of the D2 dopamine receptor third cytoplasmic loop with spinophilin, a protein phosphatase-1 -interacting protein
    • Smith, F. D., Oxford, G. S. and Milgram, S. L. (1999). Association of the D2 dopamine receptor third cytoplasmic loop with spinophilin, a protein phosphatase-1 -interacting protein. J. Biol. Chem. 274: 19894-900.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19894-19900
    • Smith, F.D.1    Oxford, G.S.2    Milgram, S.L.3
  • 124
    • 14644442259 scopus 로고    scopus 로고
    • Dopaminergic stimulation of local protein synthesis enhances surface expression of GluR1 and synaptic transmission in hippocampal neurons
    • Smith, W. B., Starck, S. R., Roberts, R. W. and Schuman, E. M. (2005). Dopaminergic stimulation of local protein synthesis enhances surface expression of GluR1 and synaptic transmission in hippocampal neurons. Neuron 45: 765-79.
    • (2005) Neuron , vol.45 , pp. 765-779
    • Smith, W.B.1    Starck, S.R.2    Roberts, R.W.3    Schuman, E.M.4
  • 125
    • 23944467820 scopus 로고    scopus 로고
    • D1 and D2 Dopamine Receptors Form Heterooligomers and Co-internalize Following Selective Activation of Either Receptor
    • So, C. H., Varghese, G., Curley, K. J., Kong, M. M., Alijaniaram, M., Ji, X., Nguyen, T., O'dowd B, F., et al. (2005). D1 and D2 Dopamine Receptors Form Heterooligomers and Co-internalize Following Selective Activation of Either Receptor. Mol. Pharmacol. 68: 568-78.
    • (2005) Mol. Pharmacol. , vol.68 , pp. 568-578
    • So, C.H.1    Varghese, G.2    Curley, K.J.3    Kong, M.M.4    Alijaniaram, M.5    Ji, X.6    Nguyen, T.7    O'Dowd, B.F.8
  • 126
    • 0035101404 scopus 로고    scopus 로고
    • Antipsychotic drugs: Importance of dopamine receptors for mechanisms of therapeutic actions and side effects
    • Strange, P. G. (2001). Antipsychotic drugs: importance of dopamine receptors for mechanisms of therapeutic actions and side effects. Pharmacol. Rev. 53: 119-33.
    • (2001) Pharmacol. Rev. , vol.53 , pp. 119-133
    • Strange, P.G.1
  • 127
    • 0141755156 scopus 로고    scopus 로고
    • Formation of novel TRPC channels by complex subunit interactions in embryonic brain
    • Strubing, C., Krapivinsky, G., Krapivinsky, L. and Clapham, D. E. (2003). Formation of novel TRPC channels by complex subunit interactions in embryonic brain. J. Biol. Chem. 278: 39014-9.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39014-39019
    • Strubing, C.1    Krapivinsky, G.2    Krapivinsky, L.3    Clapham, D.E.4
  • 128
    • 0344199383 scopus 로고    scopus 로고
    • Effects of cannabinoids on dopamine release in the corpus striatum and the nucleus accumbens in vitro
    • Szabo, B., Muller, T. and Koch, H. (1999). Effects of cannabinoids on dopamine release in the corpus striatum and the nucleus accumbens in vitro. J. Neurochem. 73: 1084-9.
    • (1999) J. Neurochem. , vol.73 , pp. 1084-1089
    • Szabo, B.1    Muller, T.2    Koch, H.3
  • 129
    • 4444307002 scopus 로고    scopus 로고
    • Calcium dependence of native metabotropic glutamate receptor signaling in central neurons
    • Tabata, T. and Kano, M. (2004). Calcium dependence of native metabotropic glutamate receptor signaling in central neurons. Mol. Neurobiol. 29: 261-70.
    • (2004) Mol. Neurobiol. , vol.29 , pp. 261-270
    • Tabata, T.1    Kano, M.2
  • 130
    • 0037573440 scopus 로고    scopus 로고
    • Differential subcellular localization of two dopamine D2 receptor isoforms in transfected NG108-15 cells
    • Takeuchi, Y. and Fukunaga, K. (2003). Differential subcellular localization of two dopamine D2 receptor isoforms in transfected NG108-15 cells. J. Neurochem. 85: 1064-74.
    • (2003) J. Neurochem. , vol.85 , pp. 1064-1074
    • Takeuchi, Y.1    Fukunaga, K.2
  • 131
    • 0035252096 scopus 로고    scopus 로고
    • Role of endocytosis in mediating downregulation of G-protein-coupled receptors
    • Tsao, P., Cao, T. and Von Zastrow, M. (2001). Role of endocytosis in mediating downregulation of G-protein-coupled receptors. Trends Pharmacol. Sci. 22: 91-6.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 91-96
    • Tsao, P.1    Cao, T.2    Von Zastrow, M.3
  • 132
    • 0035279936 scopus 로고    scopus 로고
    • Towards an understanding of complex protein networks
    • Tucker, C. L., Gera, J. F. and Uetz, P. (2001). Towards an understanding of complex protein networks. Trends Cell. Biol. 11: 102-6.
    • (2001) Trends Cell. Biol. , vol.11 , pp. 102-106
    • Tucker, C.L.1    Gera, J.F.2    Uetz, P.3
  • 135
    • 14844311241 scopus 로고    scopus 로고
    • Interactome modeling
    • Vidal, M. (2005). Interactome modeling. FEBS Lett. 579: 1834-8.
    • (2005) FEBS Lett. , vol.579 , pp. 1834-1838
    • Vidal, M.1
  • 136
    • 0242384217 scopus 로고    scopus 로고
    • Mechanisms regulating membrane trafficking of G protein-coupled receptors in the endocytic pathway
    • Von Zastrow, M. (2003). Mechanisms regulating membrane trafficking of G protein-coupled receptors in the endocytic pathway. Life Sci. 74: 217-24.
    • (2003) Life Sci. , vol.74 , pp. 217-224
    • Von Zastrow, M.1
  • 138
    • 0037147758 scopus 로고    scopus 로고
    • Dopamine D2 receptors are present in prefrontal cortical afferents and their targets in patches of the rat caudate-putamen nucleus
    • Wang, H. and Pickel, V. M. (2002). Dopamine D2 receptors are present in prefrontal cortical afferents and their targets in patches of the rat caudate-putamen nucleus. J. Comp. Neurol. 442: 392-404.
    • (2002) J. Comp. Neurol. , vol.442 , pp. 392-404
    • Wang, H.1    Pickel, V.M.2
  • 140
    • 17344367802 scopus 로고    scopus 로고
    • Spinophilin regulates Ca2+ signalling by binding the N-terminal domain of RGS2 and the third intracellular loop of G-protein-coupled receptors
    • Wang, X., Zeng, W., Soyombo, A. A., Tang, W., Ross, E. M., Barnes, A. P., Milgram, S. L., Penninger, J. M., et al. (2005). Spinophilin regulates Ca2+ signalling by binding the N-terminal domain of RGS2 and the third intracellular loop of G-protein-coupled receptors. Nat. Cell Biol. 7: 405-11.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 405-411
    • Wang, X.1    Zeng, W.2    Soyombo, A.A.3    Tang, W.4    Ross, E.M.5    Barnes, A.P.6    Milgram, S.L.7    Penninger, J.M.8
  • 141
    • 15244351924 scopus 로고    scopus 로고
    • D2 dopamine receptor activation of potassium channels is selectively decoupled by Galpha-specific GoLoco motif peptides
    • Webb, C. K., Mccudden, C. R., Willard, F. S., Kimple, R. J., Siderovski, D. P. and Oxford, G. S. (2005). D2 dopamine receptor activation of potassium channels is selectively decoupled by Galpha-specific GoLoco motif peptides. J. Neurochem. 92: 1408-18.
    • (2005) J. Neurochem. , vol.92 , pp. 1408-1418
    • Webb, C.K.1    Mccudden, C.R.2    Willard, F.S.3    Kimple, R.J.4    Siderovski, D.P.5    Oxford, G.S.6
  • 143
    • 0029188187 scopus 로고
    • Animal models of depression: Validity and applications
    • Willner, P. (1995). Animal models of depression: validity and applications. Adv. Biochem. Psychopharmacol. 49: 19-41.
    • (1995) Adv. Biochem. Psychopharmacol. , vol.49 , pp. 19-41
    • Willner, P.1
  • 144
    • 0032589998 scopus 로고    scopus 로고
    • Dopamine D2 receptor isoforms expressed in AtT20 cells differentially couple to G proteins to acutely inhibit high voltage-activated calcium channels
    • Wolfe, S. E. and Morris, S. J. (1999). Dopamine D2 receptor isoforms expressed in AtT20 cells differentially couple to G proteins to acutely inhibit high voltage-activated calcium channels. J. Neurochem. 73: 2375-82.
    • (1999) J. Neurochem. , vol.73 , pp. 2375-2382
    • Wolfe, S.E.1    Morris, S.J.2
  • 145
    • 0035913955 scopus 로고    scopus 로고
    • Agonist-independent and -dependent oligomerization of dopamine D(2) receptors by fusion to fluorescent proteins
    • Wurch, T., Matsumoto, A. and Pauwels, P. J. (2001). Agonist-independent and -dependent oligomerization of dopamine D(2) receptors by fusion to fluorescent proteins. FEBS Lett. 507: 109-13.
    • (2001) FEBS Lett. , vol.507 , pp. 109-113
    • Wurch, T.1    Matsumoto, A.2    Pauwels, P.J.3
  • 146
    • 12244262773 scopus 로고    scopus 로고
    • Dopamine D2S and D2L receptors may differentially contribute to the actions of antipsychotic and psychotic agents in mice
    • Xu, R., Hranilovic, D., Fetsko, L. A., Bucan, M. and Wang, Y. (2002). Dopamine D2S and D2L receptors may differentially contribute to the actions of antipsychotic and psychotic agents in mice. Mol. Psychiatry 7: 1075-82.
    • (2002) Mol. Psychiatry , vol.7 , pp. 1075-1082
    • Xu, R.1    Hranilovic, D.2    Fetsko, L.A.3    Bucan, M.4    Wang, Y.5
  • 147
    • 12944324246 scopus 로고    scopus 로고
    • Dopamine receptor 2 regulates L-type voltage-gated calcium channel in primary cultured mouse midbrain neural network
    • Yasumoto, F., Negishi, T., Ishii, Y., Kyuwa, S., Kuroda, Y. and Yoshikawa, Y. (2004). Dopamine receptor 2 regulates L-type voltage-gated calcium channel in primary cultured mouse midbrain neural network. Cell Mol. Neurobiol. 24: 877-82.
    • (2004) Cell Mol. Neurobiol. , vol.24 , pp. 877-882
    • Yasumoto, F.1    Negishi, T.2    Ishii, Y.3    Kyuwa, S.4    Kuroda, Y.5    Yoshikawa, Y.6
  • 149
    • 27644520813 scopus 로고    scopus 로고
    • Carbachol induces burst firing of dopamine cells in the ventral tegmental area by promoting calcium entry through L-type channels
    • Zhang, L., Liu, Y. and Chen, X. (2005). Carbachol induces burst firing of dopamine cells in the ventral tegmental area by promoting calcium entry through L-type channels. J. Physiol. 568: 469-81.
    • (2005) J. Physiol. , vol.568 , pp. 469-481
    • Zhang, L.1    Liu, Y.2    Chen, X.3
  • 150
    • 18244388958 scopus 로고    scopus 로고
    • Protein-protein coupling/uncoupling enables dopamine D2 receptor regulation of AMPA receptor-mediated excitotoxicity
    • Zou, S., Li, L., Pei, L., Vukusic, B., Van Tol, H. H., Lee, F. J., Wan, Q. and Liu, F. (2005). Protein-protein coupling/uncoupling enables dopamine D2 receptor regulation of AMPA receptor-mediated excitotoxicity. J. Neurosci. 25: 4385-95.
    • (2005) J. Neurosci. , vol.25 , pp. 4385-4395
    • Zou, S.1    Li, L.2    Pei, L.3    Vukusic, B.4    Van Tol, H.H.5    Lee, F.J.6    Wan, Q.7    Liu, F.8


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