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Volumn 111, Issue 2, 2002, Pages 219-230

Dual regulation of NMDA receptor functions by direct protein-protein interactions with the dopamine D1 receptor

Author keywords

[No Author keywords available]

Indexed keywords

6 CHLORO 2,3,4,5 TETRAHYDRO 7,8 DIHYDROXY 1 PHENYL 1H 3 BENZAZEPINE; DOPAMINE 1 RECEPTOR; GLUTAMATE RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PHOSPHATIDYLINOSITOL 3 KINASE; RECEPTOR SUBUNIT;

EID: 18644386370     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(02)00962-5     Document Type: Article
Times cited : (468)

References (47)
  • 2
    • 0030987069 scopus 로고    scopus 로고
    • How receptors talk to trimeric G proteins
    • Bourne H.R. How receptors talk to trimeric G proteins. Curr. Opin. Cell Biol. 9:1997;134-142.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 134-142
    • Bourne, H.R.1
  • 3
    • 0029015969 scopus 로고
    • Delayed antagonism of calpain reduces excitotoxicity in cultured neurons
    • Brorson J.R., Marcuccilli C.J., Miller R.J. Delayed antagonism of calpain reduces excitotoxicity in cultured neurons. Stroke. 26:1995;1259-1266.
    • (1995) Stroke , vol.26 , pp. 1259-1266
    • Brorson, J.R.1    Marcuccilli, C.J.2    Miller, R.J.3
  • 4
    • 0031939453 scopus 로고    scopus 로고
    • Dopamine and N-methyl-D-aspartate receptor interactions in the neostriatum
    • Cepeda C., Levine M.S. Dopamine and N-methyl-D-aspartate receptor interactions in the neostriatum. Dev. Neurosci. 20:1998;1-18.
    • (1998) Dev. Neurosci. , vol.20 , pp. 1-18
    • Cepeda, C.1    Levine, M.S.2
  • 5
    • 0027362945 scopus 로고
    • Neuromodulatory actions of dopamine in the neostriatum are dependent upon the excitatory amino acid receptor subtypes activated
    • Cepeda C., Buchwald N.A., Levine M.S. Neuromodulatory actions of dopamine in the neostriatum are dependent upon the excitatory amino acid receptor subtypes activated. Proc. Natl. Acad. Sci. USA. 90:1993;9576-9580.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9576-9580
    • Cepeda, C.1    Buchwald, N.A.2    Levine, M.S.3
  • 6
    • 0028799654 scopus 로고
    • Calcium: Still center-stage in hypoxic-ischemic neuronal death
    • Choi D.W. Calcium. still center-stage in hypoxic-ischemic neuronal death Trends Neurosci. 18:1995;58-60.
    • (1995) Trends Neurosci. , vol.18 , pp. 58-60
    • Choi, D.W.1
  • 8
    • 0034518449 scopus 로고    scopus 로고
    • 2+ in cell physiology and patho-physiology
    • 2+ in cell physiology and patho-physiology. Cell Calcium. 28:2000;339-348.
    • (2000) Cell Calcium , vol.28 , pp. 339-348
    • Duchen, M.R.1
  • 10
    • 0029991047 scopus 로고    scopus 로고
    • Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit
    • Ehlers M.D., Zhang S., Bernhadt J.P., Huganir R.L. Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit. Cell. 84:1996;745-755.
    • (1996) Cell , vol.84 , pp. 745-755
    • Ehlers, M.D.1    Zhang, S.2    Bernhadt, J.P.3    Huganir, R.L.4
  • 11
    • 0037047292 scopus 로고    scopus 로고
    • Selective inhibition of heterotrimeric Gs signaling: Targeting the receptor-G protein interface using a peptide minigene encoding the Gα s carboxyl terminus
    • Feldman D.S., Zamah A.M., Pierce K.L., Miller W.E., Kelly F., Rapacciuolo A., Rockman H.A., Koch W.J., Luttrell L.M. Selective inhibition of heterotrimeric Gs signaling. targeting the receptor-G protein interface using a peptide minigene encoding the Gα s carboxyl terminus J. Biol. Chem. 29:2002;29-35.
    • (2002) J. Biol. Chem. , vol.29 , pp. 29-35
    • Feldman, D.S.1    Zamah, A.M.2    Pierce, K.L.3    Miller, W.E.4    Kelly, F.5    Rapacciuolo, A.6    Rockman, H.A.7    Koch, W.J.8    Luttrell, L.M.9
  • 12
    • 0032549659 scopus 로고    scopus 로고
    • High affinity calmodulin target sequence in the signalling molecule PI 3-kinase
    • Fischer R., Julsgart J., Berchtold M.W. High affinity calmodulin target sequence in the signalling molecule PI 3-kinase. FEBS Lett. 425:1998;175-177.
    • (1998) FEBS Lett. , vol.425 , pp. 175-177
    • Fischer, R.1    Julsgart, J.2    Berchtold, M.W.3
  • 13
    • 0033556333 scopus 로고    scopus 로고
    • Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85α
    • Fruman D.A., Snapper S.B., Yballe C.M., Davidson L., Yu J.Y., Alt F.W., Cantley L.C. Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85α Science. 283:1999;393-397.
    • (1999) Science , vol.283 , pp. 393-397
    • Fruman, D.A.1    Snapper, S.B.2    Yballe, C.M.3    Davidson, L.4    Yu, J.Y.5    Alt, F.W.6    Cantley, L.C.7
  • 15
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., Reed J.C. Mitochondria and apoptosis. Science. 281:1998;1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 16
    • 0035798093 scopus 로고    scopus 로고
    • The neurobiology of slow synaptic transmission
    • Greengard P. The neurobiology of slow synaptic transmission. Science. 297:2001;1024-1030.
    • (2001) Science , vol.297 , pp. 1024-1030
    • Greengard, P.1
  • 17
    • 0036241207 scopus 로고    scopus 로고
    • Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways
    • Hardingham G.E., Fukunaga Y., Bading H. Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways. Nat. Neurosci. 5:2002;405-414.
    • (2002) Nat. Neurosci. , vol.5 , pp. 405-414
    • Hardingham, G.E.1    Fukunaga, Y.2    Bading, H.3
  • 18
    • 0030836538 scopus 로고    scopus 로고
    • A postsynaptic interaction between dopamine D1 and NMDA receptors promotes presynaptic inhibition in the rat nucleus accumbens via adenosine release
    • Harvey J., Lacey M.G. A postsynaptic interaction between dopamine D1 and NMDA receptors promotes presynaptic inhibition in the rat nucleus accumbens via adenosine release. J. Neurosci. 17:1997;5271-5280.
    • (1997) J. Neurosci. , vol.17 , pp. 5271-5280
    • Harvey, J.1    Lacey, M.G.2
  • 19
    • 0028270938 scopus 로고
    • Inhibition of G protein-coupled receptor signaling by expression of cytoplasmic domains of the receptor
    • Hawes B.E., Luttrell L.M., Exum S.T., Lefkowitz R.J. Inhibition of G protein-coupled receptor signaling by expression of cytoplasmic domains of the receptor. J. Biol. Chem. 269:1994;15776-15785.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15776-15785
    • Hawes, B.E.1    Luttrell, L.M.2    Exum, S.T.3    Lefkowitz, R.J.4
  • 21
    • 0027221998 scopus 로고
    • NMDA-dependent superoxide production and neurotoxicity
    • Lafon-Cazal M., Pietri S., Culcasi M., Bockaert J. NMDA-dependent superoxide production and neurotoxicity. Nature. 364:1993;535-537.
    • (1993) Nature , vol.364 , pp. 535-537
    • Lafon-Cazal, M.1    Pietri, S.2    Culcasi, M.3    Bockaert, J.4
  • 22
    • 0037088586 scopus 로고    scopus 로고
    • Distinct residues in the carboxyl tail mediate agonist induced desensitization and internalization of the human dopamine D1 receptor
    • Lamey M., Thompson M., Varghese G., Chi H., Sawzdargo M., George S.R., O'Dowd B.F. Distinct residues in the carboxyl tail mediate agonist induced desensitization and internalization of the human dopamine D1 receptor. J. Biol. Chem. 277:2002;9415-9421.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9415-9421
    • Lamey, M.1    Thompson, M.2    Varghese, G.3    Chi, H.4    Sawzdargo, M.5    George, S.R.6    O'Dowd, B.F.7
  • 23
  • 24
    • 0035066885 scopus 로고    scopus 로고
    • Direct binding and functional coupling of α-synuclein to the dopamine transporter
    • Lee F.J.S., Liu F., Pristupa Z.B., Niznik H.B. Direct binding and functional coupling of α-synuclein to the dopamine transporter. FASEB J. 15:2001;916-926.
    • (2001) FASEB J. , vol.15 , pp. 916-926
    • Lee, F.J.S.1    Liu, F.2    Pristupa, Z.B.3    Niznik, H.B.4
  • 27
    • 0028236667 scopus 로고
    • Regulation of NMDA channel function by endogenous Ca (2+)-dependent phosphatase
    • Lieberman D.N., Mody I. Regulation of NMDA channel function by endogenous Ca (2+)-dependent phosphatase. Nature. 369:1994;235-239.
    • (1994) Nature , vol.369 , pp. 235-239
    • Lieberman, D.N.1    Mody, I.2
  • 28
    • 0031942369 scopus 로고    scopus 로고
    • Calcium, free radicals and excitotoxins in neuronal apoptosis
    • Lipton S.A., Nicotera P. Calcium, free radicals and excitotoxins in neuronal apoptosis. Cell Calcium. 23:1998;165-171.
    • (1998) Cell Calcium , vol.23 , pp. 165-171
    • Lipton, S.A.1    Nicotera, P.2
  • 29
    • 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., Niznik H.B. Direct protein-protein coupling enables cross-talk between dopamine D5 and gamma-aminobutyric acid A receptors. Nature. 403:2000;274-280.
    • (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
  • 30
    • 0033681557 scopus 로고    scopus 로고
    • Regulation of AMPA receptor-mediated synaptic transmission by clathrin-dependent receptor internalization
    • Man H.Y., Lin J.W., Ju W.H., Ahmadian G., Liu L., Becker L.E., Sheng M., Wang Y.T. Regulation of AMPA receptor-mediated synaptic transmission by clathrin-dependent receptor internalization. Neuron. 25:2000;649-662.
    • (2000) Neuron , vol.25 , pp. 649-662
    • Man, H.Y.1    Lin, J.W.2    Ju, W.H.3    Ahmadian, G.4    Liu, L.5    Becker, L.E.6    Sheng, M.7    Wang, Y.T.8
  • 33
  • 34
    • 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., Patel Y.C. Receptors for dopamine and somatostatin. formation of hetero-oligomers with enhanced functional activity Science. 288:2000;154-157.
    • (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
  • 35
    • 0027258451 scopus 로고
    • Calcium-induced actin depolymerization reduces NMDA channel activity
    • Rosenmund C., Westbrook G.L. Calcium-induced actin depolymerization reduces NMDA channel activity. Neuron. 10:1993;805-814.
    • (1993) Neuron , vol.10 , pp. 805-814
    • Rosenmund, C.1    Westbrook, G.L.2
  • 36
    • 0031792791 scopus 로고    scopus 로고
    • Distinct influx pathways, not calcium load, determine neuronal vulnerability to calcium neurotoxicity
    • Sattler R., Charlton M.P., Hafner M., Tymianski M. Distinct influx pathways, not calcium load, determine neuronal vulnerability to calcium neurotoxicity. J. Neurochem. 71:1998;2349-2364.
    • (1998) J. Neurochem. , vol.71 , pp. 2349-2364
    • Sattler, R.1    Charlton, M.P.2    Hafner, M.3    Tymianski, M.4
  • 37
    • 0033546347 scopus 로고    scopus 로고
    • Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein
    • Sattler R., Xiong Z., Lu W.Y., MacDonald J.F., Hafner M., Tymianski M. Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein. Science. 284:1999;1845-1848.
    • (1999) Science , vol.284 , pp. 1845-1848
    • Sattler, R.1    Xiong, Z.2    Lu, W.Y.3    MacDonald, J.F.4    Hafner, M.5    Tymianski, M.6
  • 38
    • 0035912750 scopus 로고    scopus 로고
    • Molecular organization of the postsynaptic specialization
    • Sheng M. Molecular organization of the postsynaptic specialization. Proc. Natl. Acad. Sci. USA. 98:2001;7058-7061.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7058-7061
    • Sheng, M.1
  • 39
    • 0032535013 scopus 로고    scopus 로고
    • A dopamine/D1 receptor/protein kinase A/dopamine- and cAMP-regulated phosphoprotein (Mr 32 kDa)/protein phosphatase-1 pathway regulates dephosphorylation of the NMDA receptor
    • Snyder G.L., Fienberg A.A., Huganir R.L., Greengard P. A dopamine/D1 receptor/protein kinase A/dopamine- and cAMP-regulated phosphoprotein (Mr 32 kDa)/protein phosphatase-1 pathway regulates dephosphorylation of the NMDA receptor. J. Neurosci. 18:1998;10297-10303.
    • (1998) J. Neurosci. , vol.18 , pp. 10297-10303
    • Snyder, G.L.1    Fienberg, A.A.2    Huganir, R.L.3    Greengard, P.4
  • 41
    • 0030992837 scopus 로고    scopus 로고
    • Signalling through the lipid products of phosphoinositide-3-OH kinase
    • Toker A., Cantley L.C. Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature. 387:1997;673-676.
    • (1997) Nature , vol.387 , pp. 673-676
    • Toker, A.1    Cantley, L.C.2
  • 42
    • 0028235389 scopus 로고
    • Regulation of NMDA receptors in cultured hippocampal neurons by protein phosphatases 1 and 2A
    • Wang L.Y., Orser B.A., Brautigan D.L., MacDonald J.F. Regulation of NMDA receptors in cultured hippocampal neurons by protein phosphatases 1 and 2A. Nature. 369:1994;230-232.
    • (1994) Nature , vol.369 , pp. 230-232
    • Wang, L.Y.1    Orser, B.A.2    Brautigan, D.L.3    MacDonald, J.F.4
  • 44
    • 0031013896 scopus 로고    scopus 로고
    • Competitive binding of α-actinin and calmodulin to the NMDA receptor
    • Wyszynski M., Lin J., Rao A., Nigh E., Beggs A.H., Craig A.M., Sheng M. Competitive binding of α-actinin and calmodulin to the NMDA receptor. Nature. 385:1997;439-442.
    • (1997) Nature , vol.385 , pp. 439-442
    • Wyszynski, M.1    Lin, J.2    Rao, A.3    Nigh, E.4    Beggs, A.H.5    Craig, A.M.6    Sheng, M.7
  • 45
    • 0031053363 scopus 로고    scopus 로고
    • NMDA channel regulation by channel-associated protein tyrosine kinase Src
    • Yu X.M., Askalan R., Keil G.J. 2nd, Salter M.W. NMDA channel regulation by channel-associated protein tyrosine kinase Src. Science. 275:1997;674-678.
    • (1997) Science , vol.275 , pp. 674-678
    • Yu, X.M.1    Askalan, R.2    Keil G.J. II3    Salter, M.W.4
  • 46
    • 0032480890 scopus 로고    scopus 로고
    • The gain control of NMDA receptor mediated synaptic currents by intracellular sodium
    • Yu X.-M., Salter M.W. The gain control of NMDA receptor mediated synaptic currents by intracellular sodium. Nature. 396:1998;469-474.
    • (1998) Nature , vol.396 , pp. 469-474
    • Yu, X.-M.1    Salter, M.W.2
  • 47
    • 0027263019 scopus 로고
    • Aurintricarboxylic acid prevents NMDA-mediated excitotoxicity: Evidence for its action as an NMDA receptor antagonist
    • Zeevalk G.D., Schoepp D., Nicklas W.J. Aurintricarboxylic acid prevents NMDA-mediated excitotoxicity. evidence for its action as an NMDA receptor antagonist J. Neurochem. 61:1993;386-389.
    • (1993) J. Neurochem. , vol.61 , pp. 386-389
    • Zeevalk, G.D.1    Schoepp, D.2    Nicklas, W.J.3


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