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Volumn 365, Issue 2, 2002, Pages 329-336

G-protein-coupled receptors for neurotransmitter amino acids: C-terminal tails, crowded signalosomes

Author keywords

14 3 3 Protein; Activating transcription factor 4; Calmodulin; GABAB receptor; Metabotropic glutamate receptor; PICK1; Protein kinase C

Indexed keywords

MEMBRANES; PLASTICITY; PROTEINS;

EID: 0037101776     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020481     Document Type: Review
Times cited : (61)

References (63)
  • 1
    • 0035793059 scopus 로고    scopus 로고
    • Constitutive arrestin-mediated desensitization of a human vasopressin receptor mutant associated with nephrogenic diabetes insipidus
    • Barak, L. S., Oakley, R. H., Laporte, S. A. and Caron, M. G. (2001) Constitutive arrestin-mediated desensitization of a human vasopressin receptor mutant associated with nephrogenic diabetes insipidus. Proc. Natl. Acad. Sci. U.S.A. 98, 93-98
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 93-98
    • Barak, L.S.1    Oakley, R.H.2    Laporte, S.A.3    Caron, M.G.4
  • 4
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering of G protein-coupled receptors: An evolutionary success
    • Bockaert, J. and Pin, J. P. (1999) Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J. 7, 1723-1729
    • (1999) EMBO J. , vol.7 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 6
    • 0030995878 scopus 로고    scopus 로고
    • Pharmacology and functions of metabotropic glutamate receptors
    • Conn, P. J. and Pin, J.-P. (1997) Pharmacology and functions of metabotropic glutamate receptors. Annu. Rev. Pharmacol. Toxicol. 37, 205-237
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 205-237
    • Conn, P.J.1    Pin, J.-P.2
  • 7
    • 0026321096 scopus 로고
    • Crystal structure for the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7-Å resolution
    • Kang, C.-H., Shin, W.-C., Yamagata, Y., Gokcen, S., Ames, G. F.-L. and Kim, S.-H. (1991) Crystal structure for the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7-Å resolution. J. Biol. Chem. 266, 23893-23899
    • (1991) J. Biol. Chem. , vol.266 , pp. 23893-23899
    • Kang, C.-H.1    Shin, W.-C.2    Yamagata, Y.3    Gokcen, S.4    Ames, G.F.-L.5    Kim, S.-H.6
  • 8
    • 0027235488 scopus 로고
    • Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand
    • Oh, B. H., Pandit, J., Kang, C. H., Nikaido, K., Gokcen, S., Ames, G. F.-L. and Kim, S. H. (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.-L.6    Kim, S.H.7
  • 9
    • 0025716317 scopus 로고
    • Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria
    • Quiocho, F. A. (1990) Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria. Phil. Trans. R. Soc. London, Ser. B 326, 341-351
    • (1990) Phil. Trans. R. Soc. London, Ser. B , vol.326 , pp. 341-351
    • Quiocho, F.A.1
  • 15
    • 0031569809 scopus 로고    scopus 로고
    • Palmitoylation of muscarinic acetylcholine receptor m2 subtypes: Reduction in their ability to activate G proteins by mutation of a putative palmitoylation site, cysteine 457, in the carboxyl-terminal tail
    • Hayashi, M. K. and Haga, T. (1997) Palmitoylation of muscarinic acetylcholine receptor m2 subtypes: reduction in their ability to activate G proteins by mutation of a putative palmitoylation site, cysteine 457, in the carboxyl-terminal tail. Arch. Biochem. Biophys. 15, 376-382
    • (1997) Arch. Biochem. Biophys. , vol.15 , pp. 376-382
    • Hayashi, M.K.1    Haga, T.2
  • 16
    • 0028104820 scopus 로고
    • Phosphorylation and palmitoylation of the human D2L dopamine receptor in Sf9 cells
    • Ng, G. Y., O'Dowd, B. F., Caron, M., Dennis, M., Brann, M. R. and George, S. R. (1994) Phosphorylation and palmitoylation of the human D2L dopamine receptor in Sf9 cells. J. Neurochem. 63, 1589-1595
    • (1994) J. Neurochem. , vol.63 , pp. 1589-1595
    • Ng, G.Y.1    O'Dowd, B.F.2    Caron, M.3    Dennis, M.4    Brann, M.R.5    George, S.R.6
  • 17
    • 0028172976 scopus 로고
    • Palmitoylation of the α2A-adrenergic receptor. Analysis of the sequence requirements for and the dynamic properties of α2A-adrenergic receptor palmitoylation
    • Kennedy, M. E. and Limbird, L. E. (1994) Palmitoylation of the α2A-adrenergic receptor. Analysis of the sequence requirements for and the dynamic properties of α2A-adrenergic receptor palmitoylation. J. Biol. Chem. 269, 31915-31922
    • (1994) J. Biol. Chem. , vol.269 , pp. 31915-31922
    • Kennedy, M.E.1    Limbird, L.E.2
  • 18
    • 0026806492 scopus 로고
    • Agonist-modulated palmitoylation of α2-adrenergic receptor in Sf9 cells
    • Mouillac, B., Caron, M., Bonin, H., Dennis, M. and Bouvier, M. (1992) Agonist-modulated palmitoylation of α2-adrenergic receptor in Sf9 cells. J. Biol. Chem. 267, 21733-21737
    • (1992) J. Biol. Chem. , vol.267 , pp. 21733-21737
    • Mouillac, B.1    Caron, M.2    Bonin, H.3    Dennis, M.4    Bouvier, M.5
  • 20
    • 0035824541 scopus 로고    scopus 로고
    • The C terminus of the metabotropic glutamate receptor subtypes 2 and 7 specifies the receptor signaling pathways
    • Perroy, J., Gutierrez, G. J., Coulon, V., Bockaert, J., Pin, J.-P. and Fagni, L. (2001) The C terminus of the metabotropic glutamate receptor subtypes 2 and 7 specifies the receptor signaling pathways. J. Biol. Chem. 276, 45800-45805
    • (2001) J. Biol. Chem. , vol.276 , pp. 45800-45805
    • Perroy, J.1    Gutierrez, G.J.2    Coulon, V.3    Bockaert, J.4    Pin, J.-P.5    Fagni, L.6
  • 21
    • 0028912822 scopus 로고
    • Neurotransmitter receptors. I. The metabotropic glutamate receptors: Structure and functions
    • Pin, J.-P. and Duvoisin, R. (1995) Neurotransmitter receptors. I. The metabotropic glutamate receptors: structure and functions. Neuropharmacol. 34, 1-26
    • (1995) Neuropharmacol. , vol.34 , pp. 1-26
    • Pin, J.-P.1    Duvoisin, R.2
  • 22
    • 0029973079 scopus 로고    scopus 로고
    • Target-cell-specific concentration of a metabotropic glutamate receptor in the presynaptic active zone
    • Shigemoto, R., Kuli, A., Roberts, J. D. B., Ohishi, H., Nusser, Z., Kaneko, T. and Somogyi, P. (1996) Target-cell-specific concentration of a metabotropic glutamate receptor in the presynaptic active zone. Nature (London) 381, 523-525
    • (1996) Nature (London) , vol.381 , pp. 523-525
    • Shigemoto, R.1    Kuli, A.2    Roberts, J.D.B.3    Ohishi, H.4    Nusser, Z.5    Kaneko, T.6    Somogyi, P.7
  • 24
  • 25
    • 0031020814 scopus 로고    scopus 로고
    • Molecular determinants of inactivation and G protein modulation in the intracellular loop connecting domains I and II of the calcium channel α1A subunit
    • Herlitze, S., Hockerman, G. H., Scheuer, T. and Catterall, W. A. (1997) Molecular determinants of inactivation and G protein modulation in the intracellular loop connecting domains I and II of the calcium channel α1A subunit. Proc. Natl. Acad. Sci. U.S.A. 94, 1512-1516
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 1512-1516
    • Herlitze, S.1    Hockerman, G.H.2    Scheuer, T.3    Catterall, W.A.4
  • 26
    • 0029921401 scopus 로고    scopus 로고
    • Voltage-dependent modulation or N-type calcium channels by G-protein βγ subunits
    • Ikeda, S. R. (1996) Voltage-dependent modulation or N-type calcium channels by G-protein βγ subunits. Nature (London) 380, 255-258
    • (1996) Nature (London) , vol.380 , pp. 255-258
    • Ikeda, S.R.1
  • 27
    • 0034330981 scopus 로고    scopus 로고
    • Selective blockade of P/Q-type calcium channels by the metabotropic glutamate receptor type 7 involves a phospholipase C pathway in neurons
    • Perroy, J., Prezeau, L., De Waard, M., Shigemoto, R., Bockaert, J. and Fagni, L. (2000) Selective blockade of P/Q-type calcium channels by the metabotropic glutamate receptor type 7 involves a phospholipase C pathway in neurons. J. Neurosci. 20, 7896-7904
    • (2000) J. Neurosci. , vol.20 , pp. 7896-7904
    • Perroy, J.1    Prezeau, L.2    De Waard, M.3    Shigemoto, R.4    Bockaert, J.5    Fagni, L.6
  • 32
    • 0029656267 scopus 로고    scopus 로고
    • B receptors negatively regulate transcription in cerebellar granular neurons through cyclic AMP responsive element binding protein-dependent mechanisms
    • B receptors negatively regulate transcription in cerebellar granular neurons through cyclic AMP responsive element binding protein-dependent mechanisms. Neuroscience 70, 417-427
    • (1996) Neuroscience , vol.70 , pp. 417-427
    • Barthel, F.1    Kienlen Campard, P.2    Demeneix, B.A.3    Feltz, P.4    Loeffler, J.P.5
  • 34
    • 0033600833 scopus 로고    scopus 로고
    • Relationship between protein kinase C phosphorylation and calmodulin binding to the metabotropic glutamate receptor subtype 7
    • Nakajima, Y., Yamamoto, T., Nakayama, T. and Nakanishi, S. A. (1999) Relationship between protein kinase C phosphorylation and calmodulin binding to the metabotropic glutamate receptor subtype 7. J. Biol. Chem. 274, 27573-27577
    • (1999) J. Biol. Chem. , vol.274 , pp. 27573-27577
    • Nakajima, Y.1    Yamamoto, T.2    Nakayama, T.3    Nakanishi, S.A.4
  • 35
    • 0030806935 scopus 로고    scopus 로고
    • Phosphorylation and calmodulin binding of the metabotropic glutamate receptor subtype 5 (mGluR5) are antagonistic in vitro
    • Minakami, R., Jinnai, N. and Sugiyama, H. (1997) Phosphorylation and calmodulin binding of the metabotropic glutamate receptor subtype 5 (mGluR5) are antagonistic in vitro. J. Biol. Chem. 272, 20291-20298
    • (1997) J. Biol. Chem. , vol.272 , pp. 20291-20298
    • Minakami, R.1    Jinnai, N.2    Sugiyama, H.3
  • 36
    • 0035903123 scopus 로고    scopus 로고
    • Mapping of calmodulin and Gβγ binding domains within the C-terminal region of the metabotropic glutamate receptor 7A
    • El Far, O., Bofill-Cardona, E., Airas, J. M., O'Connor, V., Boehm, S., Freissmuth, M., Nanoff, C. and Betz, H. (2001) Mapping of calmodulin and Gβγ binding domains within the C-terminal region of the metabotropic glutamate receptor 7A. J. Biol. Chem. 276, 30662-30669
    • (2001) J. Biol. Chem. , vol.276 , pp. 30662-30669
    • El Far, O.1    Bofill-Cardona, E.2    Airas, J.M.3    O'Connor, V.4    Boehm, S.5    Freissmuth, M.6    Nanoff, C.7    Betz, H.8
  • 37
    • 0032529355 scopus 로고    scopus 로고
    • 3 adenosine receptor activation inhibit presynaptic metabotropic glutamate receptor (mGluR) function and uncouple mGluRs from GTP-binding proteins
    • 3 adenosine receptor activation inhibit presynaptic metabotropic glutamate receptor (mGluR) function and uncouple mGluRs from GTP-binding proteins. J. Neurosci. 18, 6138-6146
    • (1998) J. Neurosci. , vol.18 , pp. 6138-6146
    • Macek, T.A.1    Schaffhausen, H.2    Conn, P.J.3
  • 38
    • 0035815417 scopus 로고    scopus 로고
    • PKC phosphorylation of a conserved serine residue in the C-terminus of group III metabotropic glutamate receptors inhibits calmodulin binding
    • Airas, J. M., Betz, H. and El Far, O. (2001) PKC phosphorylation of a conserved serine residue in the C-terminus of group III metabotropic glutamate receptors inhibits calmodulin binding. FEBS Lett. 494, 60-63
    • (2001) FEBS Lett. , vol.494 , pp. 60-63
    • Airas, J.M.1    Betz, H.2    El Far, O.3
  • 39
    • 0033639031 scopus 로고    scopus 로고
    • Presynaptic clustering of mGluR7A requires the PICK1 PDZ domain binding site
    • Boudin, H., Doan, A., Xia, J., Shigemoto, R., Huganir, R. L., Worley, P. and Craig, A. M. (2000) Presynaptic clustering of mGluR7A requires the PICK1 PDZ domain binding site. Neuron 28, 485-497
    • (2000) Neuron , vol.28 , pp. 485-497
    • Boudin, H.1    Doan, A.2    Xia, J.3    Shigemoto, R.4    Huganir, R.L.5    Worley, P.6    Craig, A.M.7
  • 40
    • 0034517551 scopus 로고    scopus 로고
    • Interaction of the C-terminal tail region of the metabotropic glutamate receptor 7 with the protein kinase C substrate PICK1
    • El Far, O., Airas, J., Wischmeyer, E., Nehring, R. B., Karschin, A. and Betz, H. (2000) Interaction of the C-terminal tail region of the metabotropic glutamate receptor 7 with the protein kinase C substrate PICK1. Eur. J. Neurosci. 12, 4215-4221
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 4215-4221
    • El Far, O.1    Airas, J.2    Wischmeyer, E.3    Nehring, R.B.4    Karschin, A.5    Betz, H.6
  • 41
    • 0028898641 scopus 로고
    • PICK1: A perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system
    • Staudinger, J., Zhou, J., Burgess, R., Elledge, S. J. and Olson, E. N. (1995) PICK1: a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system. J. Cell. Biol. 128, 263-271
    • (1995) J. Cell. Biol. , vol.128 , pp. 263-271
    • Staudinger, J.1    Zhou, J.2    Burgess, R.3    Elledge, S.J.4    Olson, E.N.5
  • 42
    • 0031465589 scopus 로고    scopus 로고
    • Specific interaction of the PDZ domain protein PICK1 with the COOH terminus of protein kinase C-α
    • Staudinger, J., Lu, J. and Olson, E. N. (1997) Specific interaction of the PDZ domain protein PICK1 with the COOH terminus of protein kinase C-α. J. Biol. Chem. 272, 32019-32024
    • (1997) J. Biol. Chem. , vol.272 , pp. 32019-32024
    • Staudinger, J.1    Lu, J.2    Olson, E.N.3
  • 44
    • 0035839423 scopus 로고    scopus 로고
    • Molecular determinants for PICK1 synaptic aggregation and mGluR7A receptor co-clustering
    • Boudin, H. and Craig, A. M. (2001) Molecular determinants for PICK1 synaptic aggregation and mGluR7A receptor co-clustering. J. Biol. Chem. 276, 30270-30276
    • (2001) J. Biol. Chem. , vol.276 , pp. 30270-30276
    • Boudin, H.1    Craig, A.M.2
  • 46
    • 0032752399 scopus 로고    scopus 로고
    • Dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae
    • Roth, D., Birkenfeld, J. and Betz, H. (1999) Dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae. FEBS Lett. 460, 411-416
    • (1999) FEBS Lett. , vol.460 , pp. 411-416
    • Roth, D.1    Birkenfeld, J.2    Betz, H.3
  • 49
    • 0033531936 scopus 로고    scopus 로고
    • The zeta isoform of 14-3-3 proteins interacts with the third intracellular loop of different α2-adrenergic receptor subtypes
    • Prezeau, L., Richman, J. G., Edwards, S. W. and Limbird, L. E. (1999) The zeta isoform of 14-3-3 proteins interacts with the third intracellular loop of different α2-adrenergic receptor subtypes. J. Biol. Chem. 274, 13462-13469
    • (1999) J. Biol. Chem. , vol.274 , pp. 13462-13469
    • Prezeau, L.1    Richman, J.G.2    Edwards, S.W.3    Limbird, L.E.4
  • 50
    • 0033166740 scopus 로고    scopus 로고
    • Interactions of c-Raf-1 with phosphatidylserine and 14-3-3
    • McPherson, R. A., Harding, A., Roy, S., Lane, A. and Hancock, J. F. (1999) Interactions of c-Raf-1 with phosphatidylserine and 14-3-3. Oncogene 18, 3862-3869
    • (1999) Oncogene , vol.18 , pp. 3862-3869
    • McPherson, R.A.1    Harding, A.2    Roy, S.3    Lane, A.4    Hancock, J.F.5
  • 51
    • 0032568944 scopus 로고    scopus 로고
    • Mutations in the hydrophobic surface of an amphipathic groove of 14-3-3 zeta disrupt its interaction with Raf-1 kinase
    • Wang, H., Zhang, L., Liddington, R. and Fu, H. (1998) Mutations in the hydrophobic surface of an amphipathic groove of 14-3-3 zeta disrupt its interaction with Raf-1 kinase. J. Biol. Chem. 273, 16297-16304
    • (1998) J. Biol. Chem. , vol.273 , pp. 16297-16304
    • Wang, H.1    Zhang, L.2    Liddington, R.3    Fu, H.4
  • 55
    • 0030879697 scopus 로고    scopus 로고
    • Characterization of human activating transcription factor 4, a transcriptional activator that interacts with multiple domains of cAMP-responsive element-binding protein (CREB)-binding protein
    • Liang, G. and Hai, T. (1997) Characterization of human activating transcription factor 4, a transcriptional activator that interacts with multiple domains of cAMP-responsive element-binding protein (CREB)-binding protein. J. Biol. Chem. 272, 24088-24096
    • (1997) J. Biol. Chem. , vol.272 , pp. 24088-24096
    • Liang, G.1    Hai, T.2
  • 56
    • 0026728645 scopus 로고
    • Molecular cloning of human CREB-2: An ATF/CREB transcription factor that can negatively regulate transcription from the cAMP response element
    • Karpinski, B. A., Morle, G. D., Huggenvik, J., Uhler, M. D. and Leiden, J. M. (1992) Molecular cloning of human CREB-2: an ATF/CREB transcription factor that can negatively regulate transcription from the cAMP response element. Proc. Natl. Acad. Sci. U.S.A. 89, 4820-4824
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4820-4824
    • Karpinski, B.A.1    Morle, G.D.2    Huggenvik, J.3    Uhler, M.D.4    Leiden, J.M.5
  • 58
    • 0031789711 scopus 로고    scopus 로고
    • Synaptic PDZ domain-containing proteins
    • Hata, Y., Nakanishi, H. and Takai, Y. (1998) Synaptic PDZ domain-containing proteins. Neurosci. Res. 32, 1-7
    • (1998) Neurosci. Res. , vol.32 , pp. 1-7
    • Hata, Y.1    Nakanishi, H.2    Takai, Y.3
  • 60
  • 61
    • 0037124377 scopus 로고    scopus 로고
    • PICK1 is required for the control of synaptic transmission by the metabotropic glutamate receptor 7
    • in the press
    • Perroy, J., El Far, O., Bertaso, F., Pín, J. P., Betz, H., Bockaert, J. and Fagni, L. (2002) PICK1 is required for the control of synaptic transmission by the metabotropic glutamate receptor 7. EMBO J., in the press
    • (2002) EMBO J.
    • Perroy, J.1    El Far, O.2    Bertaso, F.3    Pín, J.P.4    Betz, H.5    Bockaert, J.6    Fagni, L.7
  • 62
    • 0036312940 scopus 로고    scopus 로고
    • The metabotropic glutamate receptor mGluR7b binds to the catalytic γ-subunit of protein phosphatase 1
    • Enz, R. (2002) The metabotropic glutamate receptor mGluR7b binds to the catalytic γ-subunit of protein phosphatase 1. J. Neurochem. 81, 1130-1140
    • (2002) J. Neurochem. , vol.81 , pp. 1130-1140
    • Enz, R.1
  • 63
    • 0037070641 scopus 로고    scopus 로고
    • The actin binding protein filamin A interacts with the metabotropic glutamate receptor type 7
    • Enz, R. (2002) The actin binding protein filamin A interacts with the metabotropic glutamate receptor type 7. FEBS Lett. 514, 184-188
    • (2002) FEBS Lett. , vol.514 , pp. 184-188
    • Enz, R.1


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