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Volumn 10, Issue 7, 2000, Pages 274-280

PDZ domains in synapse assembly and signalling

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMINO 3 HYDROXY 5 METHYL 4 ISOXAZOLEPROPIONIC ACID; AMPA RECEPTOR; GLUTAMATE RECEPTOR; ION CHANNEL; IONOTROPIC RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; POSTSYNAPTIC RECEPTOR;

EID: 0034237258     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(00)01783-9     Document Type: Review
Times cited : (484)

References (75)
  • 1
    • 0027354449 scopus 로고
    • Synaptic structure and development: The neuromuscular junction
    • Hall Z., Sanes J. Synaptic structure and development. the neuromuscular junction Cell Neuron. 72:1993;99-121.
    • (1993) Cell Neuron , vol.72 , pp. 99-121
    • Hall, Z.1    Sanes, J.2
  • 2
    • 0030296378 scopus 로고    scopus 로고
    • Synaptic proteins and the assembly of synaptic junctions
    • Garner C.C., Kindler S. Synaptic proteins and the assembly of synaptic junctions. Trends Cell Biol. 6:1996;429-433.
    • (1996) Trends Cell Biol. , vol.6 , pp. 429-433
    • Garner, C.C.1    Kindler, S.2
  • 3
    • 0032524629 scopus 로고    scopus 로고
    • PDZ proteins organize synaptic signaling pathways
    • Craven S.E., Bredt D.S. PDZ proteins organize synaptic signaling pathways. Cell. 93:1998;495-498.
    • (1998) Cell , vol.93 , pp. 495-498
    • Craven, S.E.1    Bredt, D.S.2
  • 4
    • 0031789711 scopus 로고    scopus 로고
    • Synaptic PDZ domain-containing proteins
    • Hata Y.et al. Synaptic PDZ domain-containing proteins. Neurosci. Res. 32:1998;1-7.
    • (1998) Neurosci. Res. , vol.32 , pp. 1-7
    • Hata, Y.1
  • 5
    • 0032915393 scopus 로고    scopus 로고
    • Organization and regulation of proteins at synapses
    • Kim J.H., Huganir R.L. Organization and regulation of proteins at synapses. Curr. Opin. Cell Biol. 11:1999;248-254.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 248-254
    • Kim, J.H.1    Huganir, R.L.2
  • 6
    • 0030473797 scopus 로고    scopus 로고
    • PDZ domains bind carboxy-terminal sequences of target proteins
    • Saras J., Heldin C.H. PDZ domains bind carboxy-terminal sequences of target proteins. Trends Biochem Sci. 21:1996;455-458.
    • (1996) Trends Biochem Sci. , vol.21 , pp. 455-458
    • Saras, J.1    Heldin, C.H.2
  • 7
    • 0031960011 scopus 로고    scopus 로고
    • Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition
    • Daniels D.L.et al. Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition. Nat. Struct. Biol. 5:1998;317-325.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 317-325
    • Daniels, D.L.1
  • 8
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle D.A.et al. Crystal structures of a complexed and peptide-free membrane protein-binding domain. molecular basis of peptide recognition by PDZ Cell. 85:1996;1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1
  • 9
    • 0001643541 scopus 로고    scopus 로고
    • Crystal structure of a PDZ domain
    • Morais Cabral J.H.et al. Crystal structure of a PDZ domain. Nature. 382:1996;649-652.
    • (1996) Nature , vol.382 , pp. 649-652
    • Morais Cabral, J.H.1
  • 10
    • 15644379801 scopus 로고    scopus 로고
    • Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
    • Songyang Z.et al. Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science. 275:1997;73-77.
    • (1997) Science , vol.275 , pp. 73-77
    • Songyang, Z.1
  • 11
    • 0029664550 scopus 로고    scopus 로고
    • 2+ channel by INAD in Drosophila photoreceptors
    • 2+ channel by INAD in Drosophila photoreceptors. Neuron. 16:1996;991-998.
    • (1996) Neuron , vol.16 , pp. 991-998
    • Shieh, B.H.1    Zhu, M.Y.2
  • 12
    • 0032555496 scopus 로고    scopus 로고
    • Cyclic peptides as non-carboxyl-terminal ligands of syntrophin PDZ domains
    • Gee S.H.et al. Cyclic peptides as non-carboxyl-terminal ligands of syntrophin PDZ domains. J. Biol. Chem. 273:1998;21980-21987.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21980-21987
    • Gee, S.H.1
  • 14
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs - Large tumor suppressor protein
    • Cho K.O.et al. The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs - large tumor suppressor protein. Neuron. 9:1992;929-942.
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.O.1
  • 15
    • 0027415643 scopus 로고
    • SAP90, a rat presynaptic protein related to the product of the Drosophila tumor suppressor gene dlg-A
    • Kistner U.et al. SAP90, a rat presynaptic protein related to the product of the Drosophila tumor suppressor gene dlg-A. J. Biol. Chem. 268:1993;4580-4583.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4580-4583
    • Kistner, U.1
  • 16
    • 0032032224 scopus 로고    scopus 로고
    • Functional analysis of the guanylate kinase-like domain in the synapse-associated protein SAP97
    • Kuhlendahl S.et al. Functional analysis of the guanylate kinase-like domain in the synapse-associated protein SAP97. Eur. J. Biochem. 252:1998;305-313.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 305-313
    • Kuhlendahl, S.1
  • 17
    • 0028882810 scopus 로고
    • Clustering of Shaker-type K1 channels by interaction with a family of membrane-associated guanylate kinases
    • Kim E.et al. Clustering of Shaker-type K1 channels by interaction with a family of membrane-associated guanylate kinases. Nature. 378:1995;85-88.
    • (1995) Nature , vol.378 , pp. 85-88
    • Kim, E.1
  • 18
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau H.C.et al. Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science. 269:1995;1737-1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1
  • 19
    • 0039793622 scopus 로고    scopus 로고
    • SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo
    • Muller B.M.et al. SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo. Neuron. 17:1996;255-265.
    • (1996) Neuron , vol.17 , pp. 255-265
    • Muller, B.M.1
  • 20
    • 0030200438 scopus 로고    scopus 로고
    • Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins
    • Kim E.et al. Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins. Neuron. 17:1996;103-113.
    • (1996) Neuron , vol.17 , pp. 103-113
    • Kim, E.1
  • 21
    • 0032191152 scopus 로고    scopus 로고
    • SAP90 binds and clusters kainate receptors causing incomplete desensitization
    • Garcia E.P.et al. SAP90 binds and clusters kainate receptors causing incomplete desensitization. Neuron. 21:1998;727-739.
    • (1998) Neuron , vol.21 , pp. 727-739
    • Garcia, E.P.1
  • 22
    • 0030921919 scopus 로고    scopus 로고
    • Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95
    • Hsueh Y.P.et al. Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95. Neuron. 18:1997;803-814.
    • (1997) Neuron , vol.18 , pp. 803-814
    • Hsueh, Y.P.1
  • 23
    • 0031932282 scopus 로고    scopus 로고
    • N-terminal palmitoylation of PSD-95 regulates association with cell membranes and interaction with K1 channel Kv1.4
    • Topinka J.R., Bredt D.S. N-terminal palmitoylation of PSD-95 regulates association with cell membranes and interaction with K1 channel Kv1.4. Neuron. 20:1998;125-134.
    • (1998) Neuron , vol.20 , pp. 125-134
    • Topinka, J.R.1    Bredt, D.S.2
  • 24
    • 0033103971 scopus 로고    scopus 로고
    • Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs
    • Craven S.E.et al. Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs. Neuron. 22:1999;497-509.
    • (1999) Neuron , vol.22 , pp. 497-509
    • Craven, S.E.1
  • 25
    • 0031966321 scopus 로고    scopus 로고
    • E-cadherin mediated cell adhesion recruits SAP97 into the cortical cytoskeleton
    • Reuver S.M., Garner C.C. E-cadherin mediated cell adhesion recruits SAP97 into the cortical cytoskeleton. J. Cell Sci. 111:1998;1071-1080.
    • (1998) J. Cell Sci. , vol.111 , pp. 1071-1080
    • Reuver, S.M.1    Garner, C.C.2
  • 26
    • 0030469153 scopus 로고    scopus 로고
    • Synapse maturation and structural plasticity at Drosophila neuromuscular junctions
    • Budnik V. Synapse maturation and structural plasticity at Drosophila neuromuscular junctions. Curr. Opin. Neurobiol. 6:1996;858-867.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 858-867
    • Budnik, V.1
  • 27
    • 0031008787 scopus 로고    scopus 로고
    • Functional expression of rat synapse-associated proteins SAP97 and SAP102 in Drosophila dlg-1 mutants: Effects on tumor suppression and synaptic bouton structure
    • Thomas U.et al. Functional expression of rat synapse-associated proteins SAP97 and SAP102 in Drosophila dlg-1 mutants: effects on tumor suppression and synaptic bouton structure. Mech. Dev. 62:1997;161-174.
    • (1997) Mech. Dev. , vol.62 , pp. 161-174
    • Thomas, U.1
  • 28
    • 0031034750 scopus 로고    scopus 로고
    • Essential role for dlg in synaptic clustering of Shaker K1 channels in vivo
    • Tejedor F.J.et al. Essential role for dlg in synaptic clustering of Shaker K1 channels in vivo. J. Neurosci. 17:1997;152-159.
    • (1997) J. Neurosci. , vol.17 , pp. 152-159
    • Tejedor, F.J.1
  • 29
    • 0030777701 scopus 로고    scopus 로고
    • Synaptic clustering of the cell adhesion molecule fasciclin II by discs - Large and its role in the regulation of presynaptic structure
    • Thomas U.et al. Synaptic clustering of the cell adhesion molecule fasciclin II by discs - large and its role in the regulation of presynaptic structure. Neuron. 19:1997;787-799.
    • (1997) Neuron , vol.19 , pp. 787-799
    • Thomas, U.1
  • 30
    • 0032584656 scopus 로고    scopus 로고
    • SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit
    • Leonard A.S.et al. SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit. J. Biol. Chem. 273:1998;19518-19524.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19518-19524
    • Leonard, A.S.1
  • 31
    • 0032520191 scopus 로고    scopus 로고
    • Heterogeneity in the molecular composition of excitatory postsynaptic sites during development of hippocampal neurons in culture
    • Rao A.et al. Heterogeneity in the molecular composition of excitatory postsynaptic sites during development of hippocampal neurons in culture. J. Neurosci. 18:1998;1217-1229.
    • (1998) J. Neurosci. , vol.18 , pp. 1217-1229
    • Rao, A.1
  • 32
    • 0032559283 scopus 로고    scopus 로고
    • Importance of the intracellular domain of NR2 subunits for NMDA receptor function in vivo
    • Sprengel R.et al. Importance of the intracellular domain of NR2 subunits for NMDA receptor function in vivo. Cell. 92:1998;279-289.
    • (1998) Cell , vol.92 , pp. 279-289
    • Sprengel, R.1
  • 33
    • 0032168178 scopus 로고    scopus 로고
    • Role of the carboxy-terminal region of the GluR epsilon2 subunit in synaptic localization of the NMDA receptor channel
    • Mori H.et al. Role of the carboxy-terminal region of the GluR epsilon2 subunit in synaptic localization of the NMDA receptor channel. Neuron. 21:1998;571-580.
    • (1998) Neuron , vol.21 , pp. 571-580
    • Mori, H.1
  • 34
    • 0032481058 scopus 로고    scopus 로고
    • Enhanced long-term potentiation and impaired learning in mice with mutant postsynaptic density-95 protein
    • Migaud M.et al. Enhanced long-term potentiation and impaired learning in mice with mutant postsynaptic density-95 protein. Nature. 396:1998;433-439.
    • (1998) Nature , vol.396 , pp. 433-439
    • Migaud, M.1
  • 35
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors
    • Dong H.et al. GRIP. a synaptic PDZ domain-containing protein that interacts with AMPA receptors Nature. 386:1997;279-284.
    • (1997) Nature , vol.386 , pp. 279-284
    • Dong, H.1
  • 36
    • 0032169143 scopus 로고    scopus 로고
    • Novel anchorage of GluR2/3 to the postsynaptic density by the AMPA receptor-binding protein ABP
    • Srivastava S.et al. Novel anchorage of GluR2/3 to the postsynaptic density by the AMPA receptor-binding protein ABP. Neuron. 21:1998;581-591.
    • (1998) Neuron , vol.21 , pp. 581-591
    • Srivastava, S.1
  • 37
    • 0032907948 scopus 로고    scopus 로고
    • Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1
    • Xia J.et al. Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1. Neuron. 22:1999;179-187.
    • (1999) Neuron , vol.22 , pp. 179-187
    • Xia, J.1
  • 38
    • 0028906288 scopus 로고
    • Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs - Large tumor suppressor protein
    • Muller B.M.et al. Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs - large tumor suppressor protein. J. Neurosci. 15:1995;2354-2366.
    • (1995) J. Neurosci. , vol.15 , pp. 2354-2366
    • Muller, B.M.1
  • 39
    • 0034143323 scopus 로고    scopus 로고
    • A developmental change in NMDA receptor-associated proteins at hippocampal synapses
    • Sans N.et al. A developmental change in NMDA receptor-associated proteins at hippocampal synapses. J. Neurosci. 20:2000;1260-1271.
    • (2000) J. Neurosci. , vol.20 , pp. 1260-1271
    • Sans, N.1
  • 40
    • 0033359994 scopus 로고    scopus 로고
    • Rapid redistribution of glutamate receptors contributes to long-term depression in hippocampal cultures
    • Carroll R.C.et al. Rapid redistribution of glutamate receptors contributes to long-term depression in hippocampal cultures. Nat. Neurosci. 2:1999;454-460.
    • (1999) Nat. Neurosci. , vol.2 , pp. 454-460
    • Carroll, R.C.1
  • 41
    • 0033360169 scopus 로고    scopus 로고
    • Morphological detection of postsynaptic silent synapses in developing hippocampal neurons
    • Liao D.et al. Morphological detection of postsynaptic silent synapses in developing hippocampal neurons. Nat. Neurosci. 2:1999;37-43.
    • (1999) Nat. Neurosci. , vol.2 , pp. 37-43
    • Liao, D.1
  • 42
    • 0032215078 scopus 로고    scopus 로고
    • Activity-dependent modulation of synaptic AMPA receptor accumulation
    • O'Brien R.J.et al. Activity-dependent modulation of synaptic AMPA receptor accumulation. Neuron. 21:1998;1067-1078.
    • (1998) Neuron , vol.21 , pp. 1067-1078
    • O'Brien, R.J.1
  • 43
    • 0033546052 scopus 로고    scopus 로고
    • Rapid spine delivery and redistribution of AMPA receptors after synaptic NMDA receptor activation
    • Shi S.H.et al. 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
  • 44
    • 0032078872 scopus 로고    scopus 로고
    • A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by CaM kinase II
    • Chen H.J.et al. A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by CaM kinase II. Neuron. 20:1998;895-904.
    • (1998) Neuron , vol.20 , pp. 895-904
    • Chen, H.J.1
  • 45
    • 0032055396 scopus 로고    scopus 로고
    • SynGAP: A synaptic RasGAP that associates with the PSD-95/SAP90 protein family
    • Kim J.H.et al. SynGAP. a synaptic RasGAP that associates with the PSD-95/SAP90 protein family Neuron. 20:1998;683-691.
    • (1998) Neuron , vol.20 , pp. 683-691
    • Kim, J.H.1
  • 46
    • 0029670941 scopus 로고    scopus 로고
    • Ca(2+)-dependent routes to Ras: Mechanisms for neuronal survival, differentiation, and plasticity?
    • Finkbeiner S., Greenberg M.E. Ca(2+)-dependent routes to Ras. mechanisms for neuronal survival, differentiation, and plasticity? Neuron. 16:1996;233-236.
    • (1996) Neuron , vol.16 , pp. 233-236
    • Finkbeiner, S.1    Greenberg, M.E.2
  • 47
    • 0032911942 scopus 로고    scopus 로고
    • Citron, a Rho-target, interacts with PSD-95/SAP-90 at glutamatergic synapses in the thalamus
    • Furuyashiki T.et al. Citron, a Rho-target, interacts with PSD-95/SAP-90 at glutamatergic synapses in the thalamus. J. Neurosci. 19:1999;109-118.
    • (1999) J. Neurosci. , vol.19 , pp. 109-118
    • Furuyashiki, T.1
  • 48
    • 0032946267 scopus 로고    scopus 로고
    • Citron binds to PSD-95 at glutamatergic synapses on inhibitory neurons in the hippocampus
    • Zhang W.et al. Citron binds to PSD-95 at glutamatergic synapses on inhibitory neurons in the hippocampus. J. Neurosci. 19:1999;96-108.
    • (1999) J. Neurosci. , vol.19 , pp. 96-108
    • Zhang, W.1
  • 49
    • 0030973545 scopus 로고    scopus 로고
    • Kalirin, a cytosolic protein with spectrin-like and GDP/GTP exchange factor-like domains that interacts with peptidylglycine alpha-amidating monooxygenase, an integral membrane peptide-processing enzyme
    • Alam M.R.et al. Kalirin, a cytosolic protein with spectrin-like and GDP/GTP exchange factor-like domains that interacts with peptidylglycine alpha-amidating monooxygenase, an integral membrane peptide-processing enzyme. J. Biol. Chem. 272:1997;12667-12675.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12667-12675
    • Alam, M.R.1
  • 50
    • 0033103887 scopus 로고    scopus 로고
    • EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains
    • Bruckner K.et al. EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains. Neuron. 22:1999;511-524.
    • (1999) Neuron , vol.22 , pp. 511-524
    • Bruckner, K.1
  • 51
    • 0032408173 scopus 로고    scopus 로고
    • PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands
    • Torres R.et al. PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands. Neuron. 21:1998;1453-1463.
    • (1998) Neuron , vol.21 , pp. 1453-1463
    • Torres, R.1
  • 52
    • 0033679909 scopus 로고    scopus 로고
    • GRASP-1: A neuronal rasGEF associated with the AMPA receptor/GRIP complex
    • (in press)
    • Ye B.et al. GRASP-1: a neuronal rasGEF associated with the AMPA receptor/GRIP complex. Neuron. 2000;. (in press).
    • (2000) Neuron
    • Ye, B.1
  • 53
    • 0032055632 scopus 로고    scopus 로고
    • CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90
    • Niethammer M.et al. CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90. Neuron. 20:1998;693-707.
    • (1998) Neuron , vol.20 , pp. 693-707
    • Niethammer, M.1
  • 54
    • 0031661170 scopus 로고    scopus 로고
    • The making of neurexins
    • Missler M.et al. The making of neurexins. J. Neurochem. 71:1998;1339-1347.
    • (1998) J. Neurochem. , vol.71 , pp. 1339-1347
    • Missler, M.1
  • 56
    • 0033178969 scopus 로고    scopus 로고
    • Proline-rich synapse-associated protein-1/cortactin binding protein 1 (ProSAP1/CortBP1) is a PDZ-domain protein highly enriched in the postsynaptic density
    • Boeckers T.M.et al. Proline-rich synapse-associated protein-1/cortactin binding protein 1 (ProSAP1/CortBP1) is a PDZ-domain protein highly enriched in the postsynaptic density. J. Neurosci. 19:1999;6506-6518.
    • (1999) J. Neurosci. , vol.19 , pp. 6506-6518
    • Boeckers, T.M.1
  • 57
    • 0033554563 scopus 로고    scopus 로고
    • Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family
    • Boeckers T.M.et al. Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family. Biochem. Biophys. Res. Commun. 264:1999;247-252.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 247-252
    • Boeckers, T.M.1
  • 58
    • 0033165926 scopus 로고    scopus 로고
    • Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin
    • Naisbitt S.et al. Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin. Neuron. 23:1999;569-582.
    • (1999) Neuron , vol.23 , pp. 569-582
    • Naisbitt, S.1
  • 59
    • 0033166537 scopus 로고    scopus 로고
    • Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins
    • Tu J.C.et al. Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins. Neuron. 23:1999;583-592.
    • (1999) Neuron , vol.23 , pp. 583-592
    • Tu, J.C.1
  • 60
    • 0032516885 scopus 로고    scopus 로고
    • A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins
    • Hirao K.et al. A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins. J. Biol. Chem. 273:1998;21105-21110.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21105-21110
    • Hirao, K.1
  • 61
    • 0032544613 scopus 로고    scopus 로고
    • A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain
    • Butz S.et al. A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Cell. 94:1998;773-782.
    • (1998) Cell , vol.94 , pp. 773-782
    • Butz, S.1
  • 62
    • 0031465172 scopus 로고    scopus 로고
    • Mints, Munc18-interacting proteins in synaptic vesicle exocytosis
    • Okamoto M., Sudhof T.C. Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. J. Biol. Chem. 272:1997;31459-31464.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31459-31464
    • Okamoto, M.1    Sudhof, T.C.2
  • 63
    • 0034042637 scopus 로고    scopus 로고
    • Molecular determinants of presynaptic active zones
    • (in press)
    • Garner C.C. Molecular determinants of presynaptic active zones. Curr. Opin. Neurobiol. 2000;. (in press).
    • (2000) Curr. Opin. Neurobiol.
    • Garner, C.C.1
  • 64
    • 0032544535 scopus 로고    scopus 로고
    • Sorting out genes that regulate epithelial and neuronal polarity
    • Bredt D.S. Sorting out genes that regulate epithelial and neuronal polarity. Cell. 94:1998;691-694.
    • (1998) Cell , vol.94 , pp. 691-694
    • Bredt, D.S.1
  • 65
    • 0033575916 scopus 로고    scopus 로고
    • A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor
    • Cao T.T.et al. A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor. Nature. 401:1999;286-290.
    • (1999) Nature , vol.401 , pp. 286-290
    • Cao, T.T.1
  • 66
    • 0033522488 scopus 로고    scopus 로고
    • PDZ-mediated interactions retain the epithelial GABA transporter on the basolateral surface of polarized epithelial cells
    • Perego C.et al. PDZ-mediated interactions retain the epithelial GABA transporter on the basolateral surface of polarized epithelial cells. EMBO J. 18:1999;2384-2393.
    • (1999) EMBO J. , vol.18 , pp. 2384-2393
    • Perego, C.1
  • 67
    • 0032544612 scopus 로고    scopus 로고
    • LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia
    • Rongo C.et al. LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia. Cell. 94:1998;751-759.
    • (1998) Cell , vol.94 , pp. 751-759
    • Rongo, C.1
  • 68
    • 0032498963 scopus 로고    scopus 로고
    • +exchange
    • +exchange. Nature. 392:1998;626-630.
    • (1998) Nature , vol.392 , pp. 626-630
    • Hall, R.A.1
  • 69
    • 0032127472 scopus 로고    scopus 로고
    • NSF binding to GluR2 regulates synaptic transmission
    • Nishimune A.et al. NSF binding to GluR2 regulates synaptic transmission. Neuron. 21:1998;87-97.
    • (1998) Neuron , vol.21 , pp. 87-97
    • Nishimune, A.1
  • 70
    • 0032125884 scopus 로고    scopus 로고
    • The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs
    • Osten P.et al. The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs. Neuron. 21:1998;99-110.
    • (1998) Neuron , vol.21 , pp. 99-110
    • Osten, P.1
  • 71
    • 0032143945 scopus 로고    scopus 로고
    • Interaction of the N-ethylmaleimide sensitive factor with AMPA receptors
    • Song I.et al. Interaction of the N-ethylmaleimide sensitive factor with AMPA receptors. Neuron. 21:1998;393-400.
    • (1998) Neuron , vol.21 , pp. 393-400
    • Song, I.1
  • 72
    • 1542310123 scopus 로고    scopus 로고
    • Role of AMPA receptor cycling in synaptic transmission and plasticity
    • Luscher C.et al. Role of AMPA receptor cycling in synaptic transmission and plasticity. Neuron. 24:1999;649-658.
    • (1999) Neuron , vol.24 , pp. 649-658
    • Luscher, C.1
  • 73
    • 0033213634 scopus 로고    scopus 로고
    • Hippocampal LTD expression involves a pool of AMPARs regulated by the NSF-GluR2 interaction [see comments]
    • Luthi A.et al. Hippocampal LTD expression involves a pool of AMPARs regulated by the NSF-GluR2 interaction [see comments]. Neuron. 24:1999;389-399.
    • (1999) Neuron , vol.24 , pp. 389-399
    • Luthi, A.1
  • 74
    • 0034708587 scopus 로고    scopus 로고
    • Driving AMPA receptors into synapses by LTP and CaMKII: Requirement for GluR1 and PDZ domain interaction
    • Hayashi Y.et al. Driving AMPA receptors into synapses by LTP and CaMKII. requirement for GluR1 and PDZ domain interaction Science. 287:2000;2262-2267.
    • (2000) Science , vol.287 , pp. 2262-2267
    • Hayashi, Y.1
  • 75
    • 0033352862 scopus 로고    scopus 로고
    • AMPA receptor-PDZ interactions in facilitation of spinal sensory synapses
    • Li P.et al. AMPA receptor-PDZ interactions in facilitation of spinal sensory synapses. Nat. Neurosci. 2:1999;972-977.
    • (1999) Nat. Neurosci , vol.2 , pp. 972-977
    • Li, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.