메뉴 건너뛰기




Volumn 95, Issue 4, 2005, Pages 1047-1058

The scaffolding protein PSD-95 interacts with the glycine transporter GLYT1 and impairs its internalization

Author keywords

Glutamate receptors; Glycine transporters; Protein protein interaction; PSD 95 Dlg ZO 1 homology domains; Synapse

Indexed keywords

CARRIER PROTEIN; GLYCINE; GLYCINE TRANSPORTER 1; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PDZ PROTEIN; POSTSYNAPTIC DENSITY PROTEIN 95; TRIPEPTIDE; UNCLASSIFIED DRUG;

EID: 28244477440     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2005.03438.x     Document Type: Article
Times cited : (48)

References (35)
  • 1
    • 0036683846 scopus 로고    scopus 로고
    • Determinants within the C-terminus of the human norepinephrine transporter dictate transporter trafficking, stability, and activity
    • Bauman P. A. and Blakely R. D. (2002) Determinants within the C-terminus of the human norepinephrine transporter dictate transporter trafficking, stability, and activity. Arch. Biochem. Biophys. 404, 80-91.
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 80-91
    • Bauman, P.A.1    Blakely, R.D.2
  • 2
    • 0032441894 scopus 로고    scopus 로고
    • Modulation of N-methyl-D-aspartate receptor function by glycine transport
    • Bergeron R., Meyer T. M., Coyle J. T. and Greene R. W. (1998) Modulation of N-methyl-D-aspartate receptor function by glycine transport. Proc. Natl Acad. Sci. USA 95, 15 730-15 734.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95
    • Bergeron, R.1    Meyer, T.M.2    Coyle, J.T.3    Greene, R.W.4
  • 3
    • 3843062537 scopus 로고    scopus 로고
    • Surface targeting of the dopamine transporter involves discrete epitopes in the distal C terminus but does not require canonical PDZ domain interactions
    • Bjerggaard C., Fog J. U., Hastrup H., Madsen K., Loland C. J., Javitch J. A. and Gether U. (2004) Surface targeting of the dopamine transporter involves discrete epitopes in the distal C terminus but does not require canonical PDZ domain interactions. J. Neurosci. 24, 7024-7036.
    • (2004) J. Neurosci. , vol.24 , pp. 7024-7036
    • Bjerggaard, C.1    Fog, J.U.2    Hastrup, H.3    Madsen, K.4    Loland, C.J.5    Javitch, J.A.6    Gether, U.7
  • 4
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of trans-membrane proteins to endosomes and lysosomes
    • Bonifacino J. S. and Traub L. M. (2003) Signals for sorting of trans-membrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72, 395-447.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 5
    • 0037320805 scopus 로고    scopus 로고
    • Glycine tranporter-1 blockade potentiates NMDA-mediated responses in rat prefrontal cortical neurons in vitro and in vivo
    • Chen L., Muhlhauser M. and Yang C. R. (2003) Glycine tranporter-1 blockade potentiates NMDA-mediated responses in rat prefrontal cortical neurons in vitro and in vivo. J. Neurophysiol 89, 691-703.
    • (2003) J. Neurophysiol , vol.89 , pp. 691-703
    • Chen, L.1    Muhlhauser, M.2    Yang, C.R.3
  • 6
    • 15244347525 scopus 로고    scopus 로고
    • Localization of the GLYT1 glycine transporter at glutamatergic synapses in the rat brain
    • Cubelos B., Gimenez C. and Zafra F. (2005) Localization of the GLYT1 glycine transporter at glutamatergic synapses in the rat brain. Cereb. Cortex 15, 448-459.
    • (2005) Cereb. Cortex , vol.15 , pp. 448-459
    • Cubelos, B.1    Gimenez, C.2    Zafra, F.3
  • 7
    • 3142655360 scopus 로고    scopus 로고
    • Two discontinuous segments in the carboxyl terminus are required for membrane targeting of the rat γ-aminobutyric acid transporter-1 (GAT1)
    • Farhan H., Korkhov V. M., Paulitschke V., Dorostkar M. M., Scholze P., Kudlacek O., Freissmuth M. and Sitte H. H. (2004) Two discontinuous segments in the carboxyl terminus are required for membrane targeting of the rat γ-aminobutyric acid transporter-1 (GAT1). J. Biol. Chem. 279, 28 553-28 563.
    • (2004) J. Biol. Chem. , vol.279
    • Farhan, H.1    Korkhov, V.M.2    Paulitschke, V.3    Dorostkar, M.M.4    Scholze, P.5    Kudlacek, O.6    Freissmuth, M.7    Sitte, H.H.8
  • 9
    • 0030624529 scopus 로고    scopus 로고
    • Alternative yeast two-hybrid systems. The interaction trap and interaction mating
    • Golemis E. A. and Khazak V. (1997) Alternative yeast two-hybrid systems. The interaction trap and interaction mating. Meth. Mol Biol. 63, 197-218.
    • (1997) Meth. Mol Biol. , vol.63 , pp. 197-218
    • Golemis, E.A.1    Khazak, V.2
  • 10
    • 10744221393 scopus 로고    scopus 로고
    • Inactivation of the glycine transporter 1 gene discloses vital role of glial glycine uptake in glycinergic inhibition
    • Gomeza J., Hulsmann S., Ohno K., Eulenburg V., Szoke K., Richter D. and Betz H. (2003) Inactivation of the glycine transporter 1 gene discloses vital role of glial glycine uptake in glycinergic inhibition. Neuron 40, 785-796.
    • (2003) Neuron , vol.40 , pp. 785-796
    • Gomeza, J.1    Hulsmann, S.2    Ohno, K.3    Eulenburg, V.4    Szoke, K.5    Richter, D.6    Betz, H.7
  • 11
    • 0034740693 scopus 로고    scopus 로고
    • Mechanism and role of PDZ domains in signaling complex assembly
    • Harris B. Z. and Lim W. A. (2001) Mechanism and role of PDZ domains in signaling complex assembly. J. Cell Sci. 114, 3219-3231.
    • (2001) J. Cell Sci. , vol.114 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 12
  • 13
    • 0033966213 scopus 로고    scopus 로고
    • Internalization of the Kv1.4 potassium channel is suppressed by clustering interactions with PSD-95
    • Jugloff D. G., Khanna R., Schlichter L. C. and Jones O. T. (2000) Internalization of the Kv1.4 potassium channel is suppressed by clustering interactions with PSD-95. J. Biol. Chem. 275, 1357-1364.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1357-1364
    • Jugloff, D.G.1    Khanna, R.2    Schlichter, L.C.3    Jones, O.T.4
  • 14
    • 0027469106 scopus 로고
    • The glycine site of the NMDA receptor - Five years on
    • Kemp J. A. and Leeson P. D. (1993) The glycine site of the NMDA receptor - five years on. Trends Pharmacol. Sci. 14, 20-25.
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 20-25
    • Kemp, J.A.1    Leeson, P.D.2
  • 15
    • 0028882810 scopus 로고
    • Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases
    • Kim E., Niethammer M., Rothschild A., Jan Y. N. and Sheng M. (1995) Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases. Nature 378, 85-88.
    • (1995) Nature , vol.378 , pp. 85-88
    • Kim, E.1    Niethammer, M.2    Rothschild, A.3    Jan, Y.N.4    Sheng, M.5
  • 16
    • 0041920952 scopus 로고    scopus 로고
    • The glycine transporter type 1 inhibitor N-[3-(4′-fluorophenyl)-3- (4′-phenylphenoxy) propyl]sarcosine potentiates NMDA receptor-mediated responses in vivo and produces an antipsychotic profile in rodent behavior
    • Kinney G. G., Sur C., Burno M., Mallorga P. J., Williams J. B., Figueroa D. J., Wittmann M., Lemaire W. and Conn P. J. (2003) The glycine transporter type 1 inhibitor N-[3-(4′-fluorophenyl)-3-(4′-phenylphenoxy) propyl]sarcosine potentiates NMDA receptor-mediated responses in vivo and produces an antipsychotic profile in rodent behavior. J. Neurosci. 23, 7586-7591.
    • (2003) J. Neurosci. , vol.23 , pp. 7586-7591
    • Kinney, G.G.1    Sur, C.2    Burno, M.3    Mallorga, P.J.4    Williams, J.B.5    Figueroa, D.J.6    Wittmann, M.7    Lemaire, W.8    Conn, P.J.9
  • 17
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau H. C., Schenker L. T., Kennedy M. B. and Seeburg P. H. (1995) Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269, 1737-1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 18
    • 8544244897 scopus 로고    scopus 로고
    • Postsynaptic density protein-95 regulates NMDA channel gating and surface expression
    • Lin Y., Skeberdis V. A., Francesconi A., Bennett M. V. and Zukin R. S. (2004) Postsynaptic density protein-95 regulates NMDA channel gating and surface expression. J. Neurosci. 24, 10 138-10 148.
    • (2004) J. Neurosci. , vol.24
    • Lin, Y.1    Skeberdis, V.A.2    Francesconi, A.3    Bennett, M.V.4    Zukin, R.S.5
  • 19
    • 3242772137 scopus 로고    scopus 로고
    • The GABA transporter GAT1 and the MAGUK protein Palsl: Interaction, uptake modulation, and coexpression in the brain
    • McHugh E. M., Zhu W., Milgram S. and Mager S. (2004) The GABA transporter GAT1 and the MAGUK protein Palsl: interaction, uptake modulation, and coexpression in the brain. Mol. Cell Neurosci. 26, 406-417.
    • (2004) Mol. Cell Neurosci. , vol.26 , pp. 406-417
    • McHugh, E.M.1    Zhu, W.2    Milgram, S.3    Mager, S.4
  • 20
    • 6944247728 scopus 로고    scopus 로고
    • Neurotransmitter transporter trafficking: Endocytosis, recycling, and regulation
    • Melikian H. E. (2004) Neurotransmitter transporter trafficking: endocytosis, recycling, and regulation. Pharmacol. Ther 104, 17-27.
    • (2004) Pharmacol. Ther , vol.104 , pp. 17-27
    • Melikian, H.E.1
  • 21
    • 0032481058 scopus 로고    scopus 로고
    • Enhanced long-term potentiation and impaired learning in mice with mutant postsynaptic density-95 protein
    • Migaud M., Charlesworth P., Dempster M. et al. (1998) Enhanced long-term potentiation and impaired learning in mice with mutant postsynaptic density-95 protein. Nature 396, 433-439.
    • (1998) Nature , vol.396 , pp. 433-439
    • Migaud, M.1    Charlesworth, P.2    Dempster, M.3
  • 23
    • 3242756821 scopus 로고    scopus 로고
    • The neuronal glycine transporter 2 interacts with the PDZ domain protein syntenin-1
    • Ohno K., Koroll M., El Far O., Scholze P., Gomeza J. and Betz H. (2004) The neuronal glycine transporter 2 interacts with the PDZ domain protein syntenin-1. Mol. Cell Neurosci. 26, 518-529.
    • (2004) Mol. Cell Neurosci. , vol.26 , pp. 518-529
    • Ohno, K.1    Koroll, M.2    El Far, O.3    Scholze, P.4    Gomeza, J.5    Betz, H.6
  • 24
    • 0028930710 scopus 로고
    • The role of N-glycosylation in the targeting and activity of the GLYT1 glycine transporter
    • Olivares L., Aragon C., Gimenez C. and Zafra F. (1995) The role of N-glycosylation in the targeting and activity of the GLYT1 glycine transporter. J. Biol. Chem. 270, 9437-9442.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9437-9442
    • Olivares, L.1    Aragon, C.2    Gimenez, C.3    Zafra, F.4
  • 25
    • 0033522488 scopus 로고    scopus 로고
    • PDZ-mediated interactions retain the epithelial GABA transporter on the basolateral surface of polarized epithelial cells
    • Perego C., Vanoni C., Villa A., Longhi R., Kaech S. M., Frohli E., Hajnal A., Kim S. K. and Pietrini G. (1999) PDZ-mediated interactions retain the epithelial GABA transporter on the basolateral surface of polarized epithelial cells. EMBO J. 18, 2384-2393.
    • (1999) EMBO J , vol.18 , pp. 2384-2393
    • Perego, C.1    Vanoni, C.2    Villa, A.3    Longhi, R.4    Kaech, S.M.5    Frohli, E.6    Hajnal, A.7    Kim, S.K.8    Pietrini, G.9
  • 28
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M. and Sala C. (2001) PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24, 1-29.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 30
    • 0035947759 scopus 로고    scopus 로고
    • PDZ protein interactions regulating glutamate receptor function and plasticity
    • Tomita S., Nicoll R. A. and Bredt D. S. (2001) PDZ protein interactions regulating glutamate receptor function and plasticity. J. Cell Biol. 153, F19-F24.
    • (2001) J. Cell Biol. , vol.153
    • Tomita, S.1    Nicoll, R.A.2    Bredt, D.S.3
  • 31
    • 0035026044 scopus 로고    scopus 로고
    • Functional interaction between monoamine plasma membrane transporters and the synaptic PDZ domain-containing protein PICKl
    • Torres G. E., Yao W. D., Mohn A. R., Quan H., Kim K. M., Levey A. I., Staudinger J. and Caron M. G. (2001) Functional interaction between monoamine plasma membrane transporters and the synaptic PDZ domain-containing protein PICKl. Neuron 30, 121-134.
    • (2001) Neuron , vol.30 , pp. 121-134
    • Torres, G.E.1    Yao, W.D.2    Mohn, A.R.3    Quan, H.4    Kim, K.M.5    Levey, A.I.6    Staudinger, J.7    Caron, M.G.8
  • 32
    • 0037462827 scopus 로고    scopus 로고
    • Oligomerization and trafficking of the human dopamine transporter. Mutational analysis identifies critical domains important for the functional expression of the transporter
    • Torres G. E., Cameiro A., Seamans K., Fiorentini C., Sweeney A., Yao W. D. and Caron M. G. (2003) Oligomerization and trafficking of the human dopamine transporter. Mutational analysis identifies critical domains important for the functional expression of the transporter. J. Biol. Chem. 278, 2731-2739.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2731-2739
    • Torres, G.E.1    Cameiro, A.2    Seamans, K.3    Fiorentini, C.4    Sweeney, A.5    Yao, W.D.6    Caron, M.G.7
  • 34
    • 0037036410 scopus 로고    scopus 로고
    • Cell surface targeting and clustering interactions between heterologously expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2
    • Wong W., Newell E. W., Jugloff D. G., Jones O. T. and Schlichter L. C. (2002) Cell surface targeting and clustering interactions between heterologously expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2. J. Biol. Chem. 277, 20 423-20 430.
    • (2002) J. Biol. Chem. , vol.277
    • Wong, W.1    Newell, E.W.2    Jugloff, D.G.3    Jones, O.T.4    Schlichter, L.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.