메뉴 건너뛰기




Volumn 10, Issue 5, 2004, Pages 287-292

Functional plasticity in the organization of signaling complexes in the striatum

Author keywords

AMPA receptor; cAMP; Neurabin; Protein phosphatase 1; Spinophilin

Indexed keywords

DOPAMINE; ION CHANNEL; NEURABIN; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN; SPINOPHILIN; UNCLASSIFIED DRUG;

EID: 2942577569     PISSN: 13538020     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.parkreldis.2004.02.016     Document Type: Conference Paper
Times cited : (15)

References (52)
  • 1
    • 0030922920 scopus 로고    scopus 로고
    • Spinophilin, a novel protein phosphatase 1 binding protein localized to dendritic spines
    • Allen P.B., Ouimet C.C., Greengard P. Spinophilin, a novel protein phosphatase 1 binding protein localized to dendritic spines. Proc Natl Acad Sci USA. 94:1997;9956-9961
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9956-9961
    • Allen, P.B.1    Ouimet, C.C.2    Greengard, P.3
  • 3
    • 0031283172 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in the alpha-amino-3-hydroxyl-5-methyl-4- isoxazole-propionate-type glutamate receptor
    • 2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in the alpha-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate-type glutamate receptor. J Biol Chem. 272:1997;32727-32730
    • (1997) J Biol Chem , vol.272 , pp. 32727-32730
    • Barria, A.1    Derkach, V.2    Soderling, T.3
  • 4
    • 0030744875 scopus 로고    scopus 로고
    • Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation
    • Barria A., Muller D., Derkach V., Griffith L.C., Soderling T.R. Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation. Science. 276:1997;2042-2045
    • (1997) Science , vol.276 , pp. 2042-2045
    • Barria, A.1    Muller, D.2    Derkach, V.3    Griffith, L.C.4    Soderling, T.R.5
  • 5
    • 0029560902 scopus 로고
    • Regional, cellular, and subcellular variations in the distribution of D1 and D5 dopamine receptors in primate brain
    • Bergson C., Mrzljak L., Smiley J.F., Pappy M., Levenson R., Goldman-Rakic P.S. Regional, cellular, and subcellular variations in the distribution of D1 and D5 dopamine receptors in primate brain. J Neurosci. 15:1995;7821-7836
    • (1995) J Neurosci , vol.15 , pp. 7821-7836
    • Bergson, C.1    Mrzljak, L.2    Smiley, J.F.3    Pappy, M.4    Levenson, R.5    Goldman-Rakic, P.S.6
  • 6
    • 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., Limbird L.E. Spinophilin stabilizes cell surface expression of alpha 2B-adrenergic receptors. J Biol Chem. 278:2003;32405-32412
    • (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
  • 7
    • 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
  • 8
    • 0036829202 scopus 로고    scopus 로고
    • D1 dopamine receptor stimulation increases GluR1 surface expression in nucleus accumbens neurons
    • Chao S.Z., Ariano M.A., Peterson D.A., Wolf M.E. D1 dopamine receptor stimulation increases GluR1 surface expression in nucleus accumbens neurons. J Neurochem. 83:2002;704-712
    • (2002) J Neurochem , vol.83 , pp. 704-712
    • Chao, S.Z.1    Ariano, M.A.2    Peterson, D.A.3    Wolf, M.E.4
  • 9
    • 0034307444 scopus 로고    scopus 로고
    • Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins
    • Chung H.J., Xia J., Scannevin R.H., Zhang X., Huganir R.L. Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins. J Neurosci. 20:2000;7258-7267
    • (2000) J Neurosci , vol.20 , pp. 7258-7267
    • Chung, H.J.1    Xia, J.2    Scannevin, R.H.3    Zhang, X.4    Huganir, R.L.5
  • 10
    • 0037081563 scopus 로고    scopus 로고
    • Protein phosphatase 1 - Targeted in many directions
    • Cohen P.T. Protein phosphatase 1 - targeted in many directions. J Cell Sci. 115:2002;241-256
    • (2002) J Cell Sci , vol.115 , pp. 241-256
    • Cohen, P.T.1
  • 11
    • 0030977268 scopus 로고    scopus 로고
    • Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1
    • Egloff M.P., Johnson D.F., Moorhead G., Cohen P.T., Cohen P., Barford D. Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1. EMBO J. 16:1997;1876-1887
    • (1997) EMBO J , vol.16 , pp. 1876-1887
    • Egloff, M.P.1    Johnson, D.F.2    Moorhead, G.3    Cohen, P.T.4    Cohen, P.5    Barford, D.6
  • 12
    • 0033639083 scopus 로고    scopus 로고
    • Reinsertion or degradation of AMPA receptors determined by activity-dependent endocytic sorting
    • Ehlers M.D. Reinsertion or degradation of AMPA receptors determined by activity-dependent endocytic sorting. Neuron. 28:2000;511-525
    • (2000) Neuron , vol.28 , pp. 511-525
    • Ehlers, M.D.1
  • 15
    • 0033166545 scopus 로고    scopus 로고
    • Beyond the dopamine receptor: The DARPP-32/protein phosphatase-1 cascade
    • Greengard P., Allen P.B., Nairn A.C. Beyond the dopamine receptor: the DARPP-32/protein phosphatase-1 cascade. Neuron. 23:1999;435-447
    • (1999) Neuron , vol.23 , pp. 435-447
    • Greengard, P.1    Allen, P.B.2    Nairn, A.C.3
  • 16
    • 0036357311 scopus 로고    scopus 로고
    • The actin-binding domain of spinophilin is necessary and sufficient for targeting to dendritic spines
    • Grossman S.D., Hsieh-Wilson L.C., Allen P.B., Nairn A.C., Greengard P. The actin-binding domain of spinophilin is necessary and sufficient for targeting to dendritic spines. Neuromol Med. 2:2002;61-69
    • (2002) Neuromol Med , vol.2 , pp. 61-69
    • Grossman, S.D.1    Hsieh-Wilson, L.C.2    Allen, P.B.3    Nairn, A.C.4    Greengard, P.5
  • 17
    • 0021162349 scopus 로고
    • DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1
    • Hemmings H.C. Jr, Greengard P., Tung H.Y., Cohen P. DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1. Nature. 310:1984;503-505
    • (1984) Nature , vol.310 , pp. 503-505
    • Hemmings Jr., H.C.1    Greengard, P.2    Tung, H.Y.3    Cohen, P.4
  • 19
    • 0034670368 scopus 로고    scopus 로고
    • D2 dopamine receptors in striatal medium spiny neurons reduce L-type Ca2+currents and excitability via a novel PLC[beta]1-IP3-calcineurin-signaling cascade
    • Hernandez-Lopez S., Tkatch T., Perez-Garci E., Galarraga E., Bargas J., Hamm H., Surmeier D.J. D2 dopamine receptors in striatal medium spiny neurons reduce L-type Ca2+currents and excitability via a novel PLC[beta]1-IP3- calcineurin-signaling cascade. J Neurosci. 20:2000;8987-8995
    • (2000) J Neurosci , vol.20 , pp. 8987-8995
    • Hernandez-Lopez, S.1    Tkatch, T.2    Perez-Garci, E.3    Galarraga, E.4    Bargas, J.5    Hamm, H.6    Surmeier, D.J.7
  • 20
    • 0033528669 scopus 로고    scopus 로고
    • Characterization of the neuronal targeting protein spinophilin and its interactions with protein phosphatase-1
    • Hsieh-Wilson L.C., Allen P.B., Watanabe T., Nairn A.C., Greengard P. Characterization of the neuronal targeting protein spinophilin and its interactions with protein phosphatase-1. Biochemistry. 38:1999;4365-4373
    • (1999) Biochemistry , vol.38 , pp. 4365-4373
    • Hsieh-Wilson, L.C.1    Allen, P.B.2    Watanabe, T.3    Nairn, A.C.4    Greengard, P.5
  • 22
    • 0028880861 scopus 로고
    • Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism
    • Lledo P.M., Hjelmstad G.O., Mukherji S., Soderling T.R., Malenka R.C., Nicoll R.A. Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism. Proc Natl Acad Sci USA. 92:1995;11175-11179
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11175-11179
    • Lledo, P.M.1    Hjelmstad, G.O.2    Mukherji, S.3    Soderling, T.R.4    Malenka, R.C.5    Nicoll, R.A.6
  • 23
    • 0030332790 scopus 로고    scopus 로고
    • Synaptic transmission and modulation in the neostriatum
    • Lovinger D.M., Tyler E. Synaptic transmission and modulation in the neostriatum. Int Rev Neurobiol. 39:1996;77-111
    • (1996) Int Rev Neurobiol , vol.39 , pp. 77-111
    • Lovinger, D.M.1    Tyler, E.2
  • 24
    • 0033544907 scopus 로고    scopus 로고
    • Brain actin-associated protein phosphatase 1 holoenzymes containing spinophilin, neurabin, and selected catalytic subunit isoforms
    • MacMillan L.B., Bass M.A., Cheng N., Howard E.F., Tamura M., Strack S., Wadzinski B.E., Colbran R.J. Brain actin-associated protein phosphatase 1 holoenzymes containing spinophilin, neurabin, and selected catalytic subunit isoforms. J Biol Chem. 274:1999;35845-35854
    • (1999) J Biol Chem , vol.274 , pp. 35845-35854
    • MacMillan, L.B.1    Bass, M.A.2    Cheng, N.3    Howard, E.F.4    Tamura, M.5    Strack, S.6    Wadzinski, B.E.7    Colbran, R.J.8
  • 25
    • 0036305484 scopus 로고    scopus 로고
    • AMPA receptor trafficking and synaptic plasticity
    • Malinow R., Malenka R.C. AMPA receptor trafficking and synaptic plasticity. Annu Rev Neurosci. 25:2002;103-126
    • (2002) Annu Rev Neurosci , vol.25 , pp. 103-126
    • Malinow, R.1    Malenka, R.C.2
  • 26
    • 0032823580 scopus 로고    scopus 로고
    • Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein
    • Matsuda S., Mikawa S., Hirai H. Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein. J Neurochem. 73:1999;1765-1768
    • (1999) J Neurochem , vol.73 , pp. 1765-1768
    • Matsuda, S.1    Mikawa, S.2    Hirai, H.3
  • 30
    • 0030201051 scopus 로고    scopus 로고
    • The distribution and significance of CNS adrenoceptors examined with in situ hybridization
    • Nicholas A.P., Hokfelt T., Pieribone V.A. The distribution and significance of CNS adrenoceptors examined with in situ hybridization. Trends Pharmacol Sci. 17:1996;245-255
    • (1996) Trends Pharmacol Sci , vol.17 , pp. 245-255
    • Nicholas, A.P.1    Hokfelt, T.2    Pieribone, V.A.3
  • 31
    • 17544368654 scopus 로고    scopus 로고
    • Dopaminergic modulation of neuronal excitability in the striatum and nucleus accumbens
    • Nicola S.M., Surmeier J., Malenka R.C. Dopaminergic modulation of neuronal excitability in the striatum and nucleus accumbens. Annu Rev Neurosci. 23:2000;185-215
    • (2000) Annu Rev Neurosci , vol.23 , pp. 185-215
    • Nicola, S.M.1    Surmeier, J.2    Malenka, R.C.3
  • 32
    • 0028985603 scopus 로고
    • The alpha and gamma 1 isoforms of protein phosphatase 1 are highly and specifically concentrated in dendritic spines
    • Ouimet C.C., da Cruz e Silva E.F., Greengard P. The alpha and gamma 1 isoforms of protein phosphatase 1 are highly and specifically concentrated in dendritic spines. Proc Natl Acad Sci USA. 92:1995;3396-3400
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3396-3400
    • Ouimet, C.C.1    Da Cruz Silva, E.E.F.2    Greengard, P.3
  • 33
    • 0035425710 scopus 로고    scopus 로고
    • PICK1 targets activated protein kinase Calpha to AMPA receptor clusters in spines of hippocampal neurons and reduces surface levels of the AMPA-type glutamate receptor subunit 2
    • Perez J.L., Khatri L., Chang C., Srivastava S., Osten P., Ziff E.B. PICK1 targets activated protein kinase Calpha to AMPA receptor clusters in spines of hippocampal neurons and reduces surface levels of the AMPA-type glutamate receptor subunit 2. J Neurosci. 21:2001;5417-5428
    • (2001) J Neurosci , vol.21 , pp. 5417-5428
    • Perez, J.L.1    Khatri, L.2    Chang, C.3    Srivastava, S.4    Osten, P.5    Ziff, E.B.6
  • 34
    • 0035805560 scopus 로고    scopus 로고
    • Agonist-regulated interaction between alpha2-adrenergic receptors and spinophilin
    • Richman J.G., Brady A.E., Wang Q., Hensel J.L., Colbran R.J., Limbird L.E. Agonist-regulated interaction between alpha2-adrenergic receptors and spinophilin. J Biol Chem. 276:2001;15003-15008
    • (2001) J Biol Chem , vol.276 , pp. 15003-15008
    • Richman, J.G.1    Brady, A.E.2    Wang, Q.3    Hensel, J.L.4    Colbran, R.J.5    Limbird, L.E.6
  • 35
    • 0030175899 scopus 로고    scopus 로고
    • Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit
    • Roche K.W., O'Brien R.J., Mammen A.L., Bernhardt J., Huganir R.L. Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit. Neuron. 16:1996;1179-1188
    • (1996) Neuron , vol.16 , pp. 1179-1188
    • Roche, K.W.1    O'Brien, R.J.2    Mammen, A.L.3    Bernhardt, J.4    Huganir, R.L.5
  • 36
    • 0028274544 scopus 로고
    • Anchoring of protein kinase a is required for modulation of AMPA/kainate receptors on hippocampal neurons
    • Rosenmund C., Carr D.W., Bergeson S.E., Nilaver G., Scott J.D., Westbrook G.L. Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons. Nature. 368:1994;853-856
    • (1994) Nature , vol.368 , pp. 853-856
    • Rosenmund, C.1    Carr, D.W.2    Bergeson, S.E.3    Nilaver, G.4    Scott, J.D.5    Westbrook, G.L.6
  • 38
    • 0037174634 scopus 로고    scopus 로고
    • Postsynaptic signaling and plasticity mechanisms
    • Sheng M., Kim M.J. Postsynaptic signaling and plasticity mechanisms. Science. 298:2002;776-780
    • (2002) Science , vol.298 , pp. 776-780
    • Sheng, M.1    Kim, M.J.2
  • 39
    • 0033546052 scopus 로고    scopus 로고
    • Rapid spine delivery and redistribution of AMPA receptors after synaptic NMDA receptor activation
    • Shi S.H., Hayashi Y., Petralia R.S., Zaman S.H., Wenthold R.J., Svoboda K., Malinow R. Rapid spine delivery and redistribution of AMPA receptors after synaptic NMDA receptor activation. Science. 284:1999;1811-1816
    • (1999) Science , vol.284 , pp. 1811-1816
    • Shi, S.H.1    Hayashi, Y.2    Petralia, R.S.3    Zaman, S.H.4    Wenthold, R.J.5    Svoboda, K.6    Malinow, R.7
  • 40
    • 0022351014 scopus 로고
    • Identification of protein phosphatase 1 in synaptic junctions: Dephosphorylation of endogenous calmodulin-dependent kinase II and synapse-enriched phosphoproteins
    • Shields S.M., Ingebritsen T.S., Kelly P.T. Identification of protein phosphatase 1 in synaptic junctions: dephosphorylation of endogenous calmodulin-dependent kinase II and synapse-enriched phosphoproteins. J Neurosci. 5:1985;3414-3422
    • (1985) J Neurosci , vol.5 , pp. 3414-3422
    • Shields, S.M.1    Ingebritsen, T.S.2    Kelly, P.T.3
  • 41
  • 42
    • 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., Milgram S.L. Association of the D2 dopamine receptor third cytoplasmic loop with spinophilin, a protein phosphatase-1- interacting protein. J Biol Chem. 274:1999;19894-19900
    • (1999) J Biol Chem , vol.274 , pp. 19894-19900
    • Smith, F.D.1    Oxford, G.S.2    Milgram, S.L.3
  • 43
    • 0030911904 scopus 로고    scopus 로고
    • Differential inactivation of postsynaptic density-associated and soluble Ca2+/calmodulin-dependent protein kinase II by protein phosphatases 1 and 2A
    • Strack S., Barban M.A., Wadzinski B.E., Colbran R.J. Differential inactivation of postsynaptic density-associated and soluble Ca2+/calmodulin- dependent protein kinase II by protein phosphatases 1 and 2A. J Neurochem. 68:1997;2119-2128
    • (1997) J Neurochem , vol.68 , pp. 2119-2128
    • Strack, S.1    Barban, M.A.2    Wadzinski, B.E.3    Colbran, R.J.4
  • 44
    • 0030946102 scopus 로고    scopus 로고
    • Translocation of autophosphorylated calcium/calmodulin-dependent protein kinase II to the postsynaptic density
    • Strack S., Choi S., Lovinger D.M., Colbran R.J. Translocation of autophosphorylated calcium/calmodulin-dependent protein kinase II to the postsynaptic density. J Biol Chem. 272:1997;13467-13470
    • (1997) J Biol Chem , vol.272 , pp. 13467-13470
    • Strack, S.1    Choi, S.2    Lovinger, D.M.3    Colbran, R.J.4
  • 45
    • 0020696442 scopus 로고
    • A dopamine- and cyclic AMP-regulated phosphoprotein enriched in dopamine-innervated brain regions
    • Walaas S.I., Aswad D.W., Greengard P. A dopamine- and cyclic AMP-regulated phosphoprotein enriched in dopamine-innervated brain regions. Nature. 301:1983;69-71
    • (1983) Nature , vol.301 , pp. 69-71
    • Walaas, S.I.1    Aswad, D.W.2    Greengard, P.3
  • 46
    • 0037184945 scopus 로고    scopus 로고
    • Regulated interactions of the alpha 2A adrenergic receptor with spinophilin, 14-3-3zeta, and arrestin 3
    • Wang Q., Limbird L.E. Regulated interactions of the alpha 2A adrenergic receptor with spinophilin, 14-3-3zeta, and arrestin 3. J Biol Chem. 277:2002;50589-50596
    • (2002) J Biol Chem , vol.277 , pp. 50589-50596
    • Wang, Q.1    Limbird, L.E.2
  • 48
    • 0027138193 scopus 로고
    • The generation of natural firing patterns in neostriatal neurons
    • Wilson C.J. The generation of natural firing patterns in neostriatal neurons. Prog Brain Res. 99:1993;277-297
    • (1993) Prog Brain Res , vol.99 , pp. 277-297
    • Wilson, C.J.1
  • 49
    • 0029886175 scopus 로고    scopus 로고
    • The origins of two-state spontaneous membrane potential fluctuations of neostriatal spiny neurons
    • Wilson C.J., Kawaguchi Y. The origins of two-state spontaneous membrane potential fluctuations of neostriatal spiny neurons. J Neurosci. 16:1996;2397-2410
    • (1996) J Neurosci , vol.16 , pp. 2397-2410
    • Wilson, C.J.1    Kawaguchi, Y.2
  • 51
    • 0028987178 scopus 로고
    • Immunocytochemical localization of D1 and D2 dopamine receptors in the basal ganglia of the rat: Light and electron microscopy
    • Yung K.K., Bolam J.P., Smith A.D., Hersch S.M., Ciliax B.J., Levey A.I. Immunocytochemical localization of D1 and D2 dopamine receptors in the basal ganglia of the rat: light and electron microscopy. Neuroscience. 65:1995;709-730
    • (1995) Neuroscience , vol.65 , pp. 709-730
    • Yung, K.K.1    Bolam, J.P.2    Smith, A.D.3    Hersch, S.M.4    Ciliax, B.J.5    Levey, A.I.6
  • 52
    • 0032589266 scopus 로고    scopus 로고
    • Alpha2C adrenoceptors inhibit adenylyl cyclase in mouse striatum: Potential activation by dopamine
    • Zhang W., Klimek V., Farley J.T., Zhu M.Y., Ordway G.A. alpha2C adrenoceptors inhibit adenylyl cyclase in mouse striatum: potential activation by dopamine. J Pharmacol Exp Ther. 289:1999;1286-1292
    • (1999) J Pharmacol Exp Ther , vol.289 , pp. 1286-1292
    • Zhang, W.1    Klimek, V.2    Farley, J.T.3    Zhu, M.Y.4    Ordway, G.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.