메뉴 건너뛰기




Volumn 5, Issue 6, 2003, Pages 520-530

NMDA receptor trafficking through an interaction between PDZ proteins and the exocyst complex

Author keywords

[No Author keywords available]

Indexed keywords

EXOCYST; GUANYLATE KINASE; MEMBRANE PROTEIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PDZ PROTEIN; SECRETORY PROTEIN; SYNAPSE ASSOCIATED PROTEIN 102; UNCLASSIFIED DRUG;

EID: 0038713372     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb990     Document Type: Review
Times cited : (276)

References (47)
  • 3
    • 0034237258 scopus 로고    scopus 로고
    • PDZ Domains in synapse assembly and signalling
    • Garner, C. C., Nash, J. & Huganir, R. L. PDZ Domains in synapse assembly and signalling. Trends Cell Biol. 10, 274-280 (2000).
    • (2000) Trends Cell Biol. , vol.10 , pp. 274-280
    • Garner, C.C.1    Nash, J.2    Huganir, R.L.3
  • 4
    • 0034330386 scopus 로고    scopus 로고
    • Postsynaptic organization and regulation of excitatory synapses
    • Scannevin, R. H. & Huganir, R. L. Postsynaptic organization and regulation of excitatory synapses. Nat. Rev. Neurosci. 1, 133-141 (2000).
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 133-141
    • Scannevin, R.H.1    Huganir, R.L.2
  • 5
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng, M. & Sala, C. PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24, 1-29 (2001).
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 6
    • 0035947759 scopus 로고    scopus 로고
    • PDZ protein interactions regulating glutamate receptor function and plasticity
    • Tomita, S., Nicoll, R. A. & Bredt, D. S. PDZ protein interactions regulating glutamate receptor function and plasticity. J. Cell Biol. 153, F19-F24 (2001).
    • (2001) J. Cell Biol. , vol.153
    • Tomita, S.1    Nicoll, R.A.2    Bredt, D.S.3
  • 7
    • 0034929661 scopus 로고    scopus 로고
    • Neurotransmitter receptor trafficking and the regulation of synaptic strength
    • Kittler, J. T. & Moss, S. J. Neurotransmitter receptor trafficking and the regulation of synaptic strength. Traffic 2, 437-448 (2001).
    • (2001) Traffic , vol.2 , pp. 437-448
    • Kittler, J.T.1    Moss, S.J.2
  • 8
    • 0034520590 scopus 로고    scopus 로고
    • PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants
    • Standley, S., Roche, K. W., McCallum, J., Sans, N. & Wenthold, R. J. PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants. Neuron 28, 887-898 (2000).
    • (2000) Neuron , vol.28 , pp. 887-898
    • Standley, S.1    Roche, K.W.2    McCallum, J.3    Sans, N.4    Wenthold, R.J.5
  • 9
    • 0035341508 scopus 로고    scopus 로고
    • An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing
    • Scott, D. B., Blanpied, T. A., Swanson, G. T., Zhang, C. & Ehlers, M. D. An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing. J. Neurosci. 21, 3063-3072 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 3063-3072
    • Scott, D.B.1    Blanpied, T.A.2    Swanson, G.T.3    Zhang, C.4    Ehlers, M.D.5
  • 10
    • 0034788270 scopus 로고    scopus 로고
    • An ER retention signal explains differences in surface expression of NMDA and AMPA receptor subunits
    • Xia, H., Hornby, Z. D. & Malenka, R. C. An ER retention signal explains differences in surface expression of NMDA and AMPA receptor subunits. Neuropharmacology 41, 714-723 (2001).
    • (2001) Neuropharmacology , vol.41 , pp. 714-723
    • Xia, H.1    Hornby, Z.D.2    Malenka, R.C.3
  • 11
    • 0035478061 scopus 로고    scopus 로고
    • Synapse-associated protein 97 selectively associates with a subset of AMPA receptors early in their biosynthetic pathway
    • Sans, N. et al. Synapse-associated protein 97 selectively associates with a subset of AMPA receptors early in their biosynthetic pathway. J. Neurosci. 21, 7506-7516 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 7506-7516
    • Sans, N.1
  • 12
    • 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, 2262-2267 (2000).
    • (2000) Science , vol.287 , pp. 2262-2267
    • Hayashi, Y.1
  • 13
    • 0035805143 scopus 로고    scopus 로고
    • Subunit-specific rules governing AMPA receptor trafficking to synapses in hippocampal pyramidal neurons
    • Shi, S., Hayashi, Y., Esteban, J. A. & Malinow, R. Subunit-specific rules governing AMPA receptor trafficking to synapses in hippocampal pyramidal neurons. Cell 105, 331-343 (2001).
    • (2001) Cell , vol.105 , pp. 331-343
    • Shi, S.1    Hayashi, Y.2    Esteban, J.A.3    Malinow, R.4
  • 14
    • 0026672857 scopus 로고
    • Sec8p and Sec15p are components of a plasma membrane-associated 19.5S particle that may function downstream of Sec4p to control exocytosis
    • Bowser, R., Muller, H., Govindan, B. & Novick, P. Sec8p and Sec15p are components of a plasma membrane-associated 19.5S particle that may function downstream of Sec4p to control exocytosis. J. Cell Biol. 118, 1041-1056 (1992).
    • (1992) J. Cell Biol. , vol.118 , pp. 1041-1056
    • Bowser, R.1    Muller, H.2    Govindan, B.3    Novick, P.4
  • 15
    • 0030464563 scopus 로고    scopus 로고
    • The mammalian brain rsec6/8 complex
    • Hsu, S. C. et al. The mammalian brain rsec6/8 complex, Neuron 17, 1209-1219 (1996).
    • (1996) Neuron , vol.17 , pp. 1209-1219
    • Hsu, S.C.1
  • 16
    • 0032904433 scopus 로고    scopus 로고
    • Targeting vesicles to specific sites on the plasma membrane: The role of the sec6/8 complex
    • Hsu, S. C., Hazuka, C. D., Foletti, D. L. & Scheller, R. H. Targeting vesicles to specific sites on the plasma membrane: the role of the sec6/8 complex. Trends Cell Biol. 9, 150-153 (1999).
    • (1999) Trends Cell Biol. , vol.9 , pp. 150-153
    • Hsu, S.C.1    Hazuka, C.D.2    Foletti, D.L.3    Scheller, R.H.4
  • 17
    • 0033558032 scopus 로고    scopus 로고
    • The sec6/8 complex is located at neurite outgrowth and axonal synapse assembly domains
    • Hazuka, C. D. et al. The sec6/8 complex is located at neurite outgrowth and axonal synapse assembly domains. J. Neurosci. 19, 1324-1334 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 1324-1334
    • Hazuka, C.D.1
  • 18
    • 0035969243 scopus 로고    scopus 로고
    • Sec6/8 complexes on trans-Golgi network and plasma membrane regulate late stages of exacytosis in mammalian cells
    • Yeaman, C., Grindstaff, K. K., Wright, J. R. & Nelson, W. J. Sec6/8 complexes on trans-Golgi network and plasma membrane regulate late stages of exacytosis in mammalian cells. J. Cell Biol. 155, 593-604 (2001).
    • (2001) J. Cell Biol. , vol.155 , pp. 593-604
    • Yeaman, C.1    Grindstaff, K.K.2    Wright, J.R.3    Nelson, W.J.4
  • 19
    • 0035370951 scopus 로고    scopus 로고
    • The exocyst associates with microtubules to mediate vesicle targeting and neurite outgrowth
    • Vega, I. E. & Hsu, S. C. The exocyst associates with microtubules to mediate vesicle targeting and neurite outgrowth. J. Neurosci. 21, 3839-3848 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 3839-3848
    • Vega, I.E.1    Hsu, S.C.2
  • 21
    • 0036608158 scopus 로고    scopus 로고
    • Ras family therapy: Ralb, Rho and Ral talk to the exacyst
    • Novick, P. & Guo, W. Ras family therapy: Ralb, Rho and Ral talk to the exacyst. Trends Cell Biol. 12, 247-249 (2002).
    • (2002) Trends Cell Biol. , vol.12 , pp. 247-249
    • Novick, P.1    Guo, W.2
  • 22
    • 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, 255-265 (1996).
    • (1996) Neuron , vol.17 , pp. 255-265
    • Muller, B.M.1
  • 23
    • 0029788216 scopus 로고    scopus 로고
    • Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, SAP102
    • Lau, L. F. et al. Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, SAP102. J. Biol. Chem. 271, 21622-21628 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 21622-21628
    • Lau, L.F.1
  • 24
    • 8544258802 scopus 로고    scopus 로고
    • Cloning and characterization of NE-dlg: A novel human homolog of the Drosophila discs large (dlg) tumor suppressor protein interacts with the APC protein
    • Makino, K. et al. Cloning and characterization of NE-dlg: a novel human homolog of the Drosophila discs large (dlg) tumor suppressor protein interacts with the APC protein. Oncogene 22, 2425-2433 (1997).
    • (1997) Oncogene , vol.22 , pp. 2425-2433
    • Makino, K.1
  • 25
    • 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, 1260-1271 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 1260-1271
    • Sans, N.1
  • 26
    • 0031447173 scopus 로고    scopus 로고
    • Subunit structure of the mammalian exocyst complex
    • Kee, Y. et al. Subunit structure of the mammalian exocyst complex. Proc. Natl. Acad. Sci. U. S. A. 94, 14438-14443 (1997).
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 14438-14443
    • Kee, Y.1
  • 27
    • 0033578892 scopus 로고    scopus 로고
    • Biochemical evidence for the co-association of three N-methyl-D-aspartate (NMDA) R2 subunits in recombinant NMDA receptors
    • Hawkins, L. M., Chazot, P. L. & Stephenson, F. A. Biochemical evidence for the co-association of three N-methyl-D-aspartate (NMDA) R2 subunits in recombinant NMDA receptors. J. Biol. Chem. 274, 27211-27218 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 27211-27218
    • Hawkins, L.M.1    Chazot, P.L.2    Stephenson, F.A.3
  • 28
    • 0032192555 scopus 로고    scopus 로고
    • Assembly, intracellular targeting and cell surface expression of the human N-methyl-D-aspartate receptor subunits NR1a and NR2A in transfected cells
    • Mcellhinney, R. A. J. et al. Assembly, intracellular targeting and cell surface expression of the human N-methyl-D-aspartate receptor subunits NR1a and NR2A in transfected cells. Neuropharmacology 37, 1355-1367 (1998).
    • (1998) Neuropharmacology , vol.37 , pp. 1355-1367
    • Mcellhinney, R.A.J.1
  • 29
    • 0033568842 scopus 로고    scopus 로고
    • Alternative splicing of the C-terminal domain regulates cell surface expression of the NMDA receptor NR1 subunit
    • Okabe, S., Miwa, A. & Okada, H. Alternative splicing of the C-terminal domain regulates cell surface expression of the NMDA receptor NR1 subunit. J. Neurosci. 15, 7781-7792 (1999).
    • (1999) J. Neurosci. , vol.15 , pp. 7781-7792
    • Okabe, S.1    Miwa, A.2    Okada, H.3
  • 30
    • 0027746221 scopus 로고
    • Optimal expression of cloned NMDAR1/NMDAR2A heteromeric glutamate receptors: A biochemical characterization
    • Cik, M., Chazot, P. L. & Stephenson, F. A. Optimal expression of cloned NMDAR1/NMDAR2A heteromeric glutamate receptors: a biochemical characterization. Biochem. J. 296, 877-883 (1993).
    • (1993) Biochem. J. , vol.296 , pp. 877-883
    • Cik, M.1    Chazot, P.L.2    Stephenson, F.A.3
  • 31
    • 0036095402 scopus 로고    scopus 로고
    • Silent synapses in developing cerebellar granule neurons
    • Losi, G., Prybylowski, K., Fu, Z., Luo, J. H. & Vicini S. Silent synapses in developing cerebellar granule neurons. J. Neurophysiol. 87, 1263-1270 (2002).
    • (2002) J. Neurophysiol. , vol.87 , pp. 1263-1270
    • Losi, G.1    Prybylowski, K.2    Fu, Z.3    Luo, J.H.4    Vicini, S.5
  • 32
    • 0037109723 scopus 로고    scopus 로고
    • Relationship between availability of NMDA receptor subunits and their expression at the synapse
    • Prybylowski, K. et al. Relationship between availability of NMDA receptor subunits and their expression at the synapse. J. Neurosci. 22, 8902-8910 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 8902-8910
    • Prybylowski, K.1
  • 33
    • 0034740693 scopus 로고    scopus 로고
    • Mechanism and role of PDZ domains in signaling complex assembly
    • Harris, B. Z. & Lim, W. A. Mechanism and role of PDZ domains in signaling complex assembly. J. Cell Sci. 114, 3219-3231 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 34
    • 0036606360 scopus 로고    scopus 로고
    • ER transport signals and trafficking of potassium channels and receptors
    • Ma, D. & Jan, L. Y. ER transport signals and trafficking of potassium channels and receptors. Curr. Opin. Neurobiol. 12, 287-292 (2002).
    • (2002) Curr. Opin. Neurobiol. , vol.12 , pp. 287-292
    • Ma, D.1    Jan, L.Y.2
  • 35
    • 0032577562 scopus 로고    scopus 로고
    • Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells
    • Grindstaff, K. K. et al. Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell 93, 731-740 (1998).
    • (1998) Cell , vol.93 , pp. 731-740
    • Grindstaff, K.K.1
  • 36
    • 0032103420 scopus 로고    scopus 로고
    • Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments
    • Hsu, S. C. et al. Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments. Neuron 20, 1111-1122 (1998).
    • (1998) Neuron , vol.20 , pp. 1111-1122
    • Hsu, S.C.1
  • 37
    • 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, 279-289 (1998).
    • (1998) Cell , vol.92 , pp. 279-289
    • Sprengel, R.1
  • 38
    • 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, 571-580 (1998).
    • (1998) Neuron , vol.21 , pp. 571-580
    • Mori, H.1
  • 39
    • 0037130451 scopus 로고    scopus 로고
    • Subunit-specific NMDA receptor trafficking to synapses
    • Barria, A. & Malinow, R. Subunit-specific NMDA receptor trafficking to synapses. Neuron 35, 345-353 (2002).
    • (2002) Neuron , vol.35 , pp. 345-353
    • Barria, A.1    Malinow, R.2
  • 40
    • 0037061686 scopus 로고    scopus 로고
    • Mobile NMDA receptors at hippocampal synapses
    • Tovar, K. R. & Westbrook, G. L. Mobile NMDA receptors at hippocampal synapses. Neuron 34, 255-264 (2002).
    • (2002) Neuron , vol.34 , pp. 255-264
    • Tovar, K.R.1    Westbrook, G.L.2
  • 41
    • 0033573390 scopus 로고    scopus 로고
    • Distinct synaptic and extrasynaptic NMDA receptors in developing cerebellar granule neurons
    • Rumbaugh, G. & Vicini, S. Distinct synaptic and extrasynaptic NMDA receptors in developing cerebellar granule neurons. J. Neurosci. 19, 10603-10610 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 10603-10610
    • Rumbaugh, G.1    Vicini, S.2
  • 42
    • 0033562610 scopus 로고    scopus 로고
    • The incorporation of NMDA receptors with a distinct subunit composition at nascent hippocampal synapses in vitro
    • Tovar, K. R. & Westbrook, G. L. The incorporation of NMDA receptors with a distinct subunit composition at nascent hippocampal synapses in vitro. J. Neurosci. 19, 4180-4188 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 4180-4188
    • Tovar, K.R.1    Westbrook, G.L.2
  • 43
    • 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, 511-525 (2000).
    • (2000) Neuron , vol.28 , pp. 511-525
    • Ehlers, M.D.1
  • 44
    • 0034941552 scopus 로고    scopus 로고
    • Molecular determinants of NMDA receptor internalization
    • Roche, K. W. et al. Molecular determinants of NMDA receptor internalization. Nat. Neurosci. 4, 794-802 (2001).
    • (2001) Nat. Neurosci. , vol.4 , pp. 794-802
    • Roche, K.W.1
  • 45
    • 0034986665 scopus 로고    scopus 로고
    • A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux
    • Vissel, B., Krupp, J. J., Heinemann, S. F. & Westbrook, G. L. A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux. Nat. Neurosci. 4, 587-596 (2001).
    • (2001) Nat. Neurosci. , vol.4 , pp. 587-596
    • Vissel, B.1    Krupp, J.J.2    Heinemann, S.F.3    Westbrook, G.L.4
  • 46
    • 0035708880 scopus 로고    scopus 로고
    • Internalization of ionotropic glutamate receptors in response to mGluR activation
    • Snyder, E. M., Philpot, B. D., Huber, K. M., Deng, X., Fallon, J. R. & Bear, M. F. Internalization of ionotropic glutamate receptors in response to mGluR activation. Nat. Neurosci. 4, 1079-1085 (2001).
    • (2001) Nat. Neurosci. , vol.4 , pp. 1079-1085
    • Snyder, E.M.1    Philpot, B.D.2    Huber, K.M.3    Deng, X.4    Fallon, J.R.5    Bear, M.F.6
  • 47
    • 0031012570 scopus 로고    scopus 로고
    • Biochemical evidence for the existence of a pool of unassembled C2 exon-containing NR1 subunits of the mammalian forebrain NMDA receptor
    • Chazot, P. L. & Stephenson, F. A. Biochemical evidence for the existence of a pool of unassembled C2 exon-containing NR1 subunits of the mammalian forebrain NMDA receptor. J. Neurochem. 68, 507-516 (1997).
    • (1997) J. Neurochem. , vol.68 , pp. 507-516
    • Chazot, P.L.1    Stephenson, F.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.