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Volumn 172, Issue 3, 2006, Pages 441-451

Neuronal cotransport of glycine receptor and the scaffold protein gephyrin

Author keywords

[No Author keywords available]

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE; GEPHYRIN; GLYCINE RECEPTOR; POSTSYNAPTIC RECEPTOR; SCAFFOLD PROTEIN;

EID: 31944448850     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200506066     Document Type: Article
Times cited : (114)

References (52)
  • 1
    • 0242384720 scopus 로고    scopus 로고
    • Activity-induced targeting of profilin and stabilization of dendritic spine morphology
    • Ackermann, M., and A. Matus. 2003. Activity-induced targeting of profilin and stabilization of dendritic spine morphology. Nat. Neurosci. 6:1194-1200.
    • (2003) Nat. Neurosci. , vol.6 , pp. 1194-1200
    • Ackermann, M.1    Matus, A.2
  • 2
    • 0032567765 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin are required for the transport of microtubules into the axon
    • Ahmad, F.J., C.J. Echeverri, R.B. Vallee, and P.W. Baas. 1998. Cytoplasmic dynein and dynactin are required for the transport of microtubules into the axon. J. Cell Biol. 140:391-401.
    • (1998) J. Cell Biol. , vol.140 , pp. 391-401
    • Ahmad, F.J.1    Echeverri, C.J.2    Vallee, R.B.3    Baas, P.W.4
  • 3
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dyneindependent maintenance of membrane organelle distribution
    • Burkhardt, J.K., C.J. Echeverri, T. Nilsson, and R.B. Vallee. 1997. Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dyneindependent maintenance of membrane organelle distribution. J. Cell Biol. 139:469-484.
    • (1997) J. Cell Biol. , vol.139 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 4
    • 0038439320 scopus 로고    scopus 로고
    • The role of receptor diffusion in the organization of the postsynaptic membrane
    • Choquet, D., and A. Triller. 2003. The role of receptor diffusion in the organization of the postsynaptic membrane. Nat. Rev. Neurosci. 4:251-265.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 251-265
    • Choquet, D.1    Triller, A.2
  • 5
    • 9144269975 scopus 로고    scopus 로고
    • Morphologically identified glycinergic synapses in the hippocampus
    • Danglot, L., P. Rostaing, A. Triller, and A. Bessis. 2004. Morphologically identified glycinergic synapses in the hippocampus. Mol. Cell. Neurosci. 27:394-403.
    • (2004) Mol. Cell. Neurosci. , vol.27 , pp. 394-403
    • Danglot, L.1    Rostaing, P.2    Triller, A.3    Bessis, A.4
  • 6
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors
    • Dong, H., R.J. O'Brien, E.T. Fung, A.A. Lanahan, P.F. Worley, and R.L. Huganir. 1997. GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature. 386:279-284.
    • (1997) Nature , vol.386 , pp. 279-284
    • Dong, H.1    O'Brien, R.J.2    Fung, E.T.3    Lanahan, A.A.4    Worley, P.F.5    Huganir, R.L.6
  • 8
    • 0032924485 scopus 로고    scopus 로고
    • Presence of the vesicular inhibitory amino acid transporter in GABAergic and glycinergic synaptic terminal boutons
    • Dumoulin, A., P. Rostaing, C. Bedet, S. Levi, M.F. Isambert, J.P. Henry, A. Triller, and B. Gasnier. 1999. Presence of the vesicular inhibitory amino acid transporter in GABAergic and glycinergic synaptic terminal boutons. J. Cell Sci. 112:811-823.
    • (1999) J. Cell Sci. , vol.112 , pp. 811-823
    • Dumoulin, A.1    Rostaing, P.2    Bedet, C.3    Levi, S.4    Isambert, M.F.5    Henry, J.P.6    Triller, A.7    Gasnier, B.8
  • 9
    • 33644665247 scopus 로고    scopus 로고
    • Postsynaptic clustering of major GABAA receptor subtypes requires the gamma 2 subunit and gephyrin
    • Essrich, C., M. Lorez, J.A. Benson, J.M. Fritschy, and B. Luscher. 1998. Postsynaptic clustering of major GABAA receptor subtypes requires the gamma 2 subunit and gephyrin. Nat. Neurosci. 1:563-571.
    • (1998) Nat. Neurosci. , vol.1 , pp. 563-571
    • Essrich, C.1    Lorez, M.2    Benson, J.A.3    Fritschy, J.M.4    Luscher, B.5
  • 10
    • 0026726318 scopus 로고
    • The synaptic vesicle protein SV2 is a novel type of transmembrane transporter
    • Feany, M.B., S. Lee, R.H. Edwards, and K.M. Buckley. 1992. The synaptic vesicle protein SV2 is a novel type of transmembrane transporter. Cell. 70:861-867.
    • (1992) Cell , vol.70 , pp. 861-867
    • Feany, M.B.1    Lee, S.2    Edwards, R.H.3    Buckley, K.M.4
  • 11
    • 0033855708 scopus 로고    scopus 로고
    • Glutamate receptors regulate actin-based plasticity in dendritic spines
    • Fischer, M., S. Kaech, U. Wagner, H. Brinkhaus, and A. Matus. 2000. Glutamate receptors regulate actin-based plasticity in dendritic spines. Nat. Neurosci. 3:887-894.
    • (2000) Nat. Neurosci. , vol.3 , pp. 887-894
    • Fischer, M.1    Kaech, S.2    Wagner, U.3    Brinkhaus, H.4    Matus, A.5
  • 14
    • 0037223301 scopus 로고    scopus 로고
    • KIF17 dynamics and regulation of NR2B trafficking in hippocampal neurons
    • Guillaud, L., M. Setou, and N. Hirokawa. 2003. KIF17 dynamics and regulation of NR2B trafficking in hippocampal neurons. J. Neurosci. 23:131-140.
    • (2003) J. Neurosci. , vol.23 , pp. 131-140
    • Guillaud, L.1    Setou, M.2    Hirokawa, N.3
  • 15
    • 3142516228 scopus 로고    scopus 로고
    • Microtubule-dependent transport in neurons: Steps towards an understanding of regulation, function and dysfunction
    • Guzik, B.W., and L.S. Goldstein. 2004. Microtubule-dependent transport in neurons: steps towards an understanding of regulation, function and dysfunction. Curr. Opin. Cell Biol. 16:443-450.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 443-450
    • Guzik, B.W.1    Goldstein, L.S.2
  • 16
    • 0034351414 scopus 로고    scopus 로고
    • The molecular anatomy of dynein
    • Harrison, A., and S.M. King. 2000. The molecular anatomy of dynein. Essays Biochem. 35:75-87.
    • (2000) Essays Biochem. , vol.35 , pp. 75-87
    • Harrison, A.1    King, S.M.2
  • 17
    • 14844331501 scopus 로고    scopus 로고
    • Molecular motors and mechanisms of directional transport in neurons
    • Hirokawa, N., and R. Takemura. 2005. Molecular motors and mechanisms of directional transport in neurons. Nat. Rev. Neurosci. 6:201-214.
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 201-214
    • Hirokawa, N.1    Takemura, R.2
  • 18
    • 2342561865 scopus 로고    scopus 로고
    • Motor neurons rely on motor proteins
    • Holzbaur, E.L. 2004. Motor neurons rely on motor proteins. Trends Cell Biol. 14:233-240.
    • (2004) Trends Cell Biol. , vol.14 , pp. 233-240
    • Holzbaur, E.L.1
  • 19
    • 0033004145 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin in cell division and intracellular transport
    • Karki, S., and E.L. Holzbaur. 1999. Cytoplasmic dynein and dynactin in cell division and intracellular transport. Curr. Opin. Cell Biol. 11:45-53.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 45-53
    • Karki, S.1    Holzbaur, E.L.2
  • 20
    • 0034721678 scopus 로고    scopus 로고
    • Signal-processing machines at the postsynaptic density
    • Kennedy, M.B. 2000. Signal-processing machines at the postsynaptic density. Science. 290:750-754.
    • (2000) Science , vol.290 , pp. 750-754
    • Kennedy, M.B.1
  • 21
    • 0033789351 scopus 로고    scopus 로고
    • Dynactin increases the processivity of the cytoplasmic dynein motor
    • King, S.J., and T.A. Schroer. 2000. Dynactin increases the processivity of the cytoplasmic dynein motor. Nat. Cell Biol. 2:20-24.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 20-24
    • King, S.J.1    Schroer, T.A.2
  • 23
    • 0028998303 scopus 로고
    • The postsynaptic localization of the glycine receptor-associated protein gephyrin is regulated by the cytoskeleton
    • Kirsch, J., and H. Betz. 1995. The postsynaptic localization of the glycine receptor-associated protein gephyrin is regulated by the cytoskeleton. J. Neurosci. 15:4148-4156.
    • (1995) J. Neurosci. , vol.15 , pp. 4148-4156
    • Kirsch, J.1    Betz, H.2
  • 24
    • 0032537056 scopus 로고    scopus 로고
    • Glycine-receptor activation is required for receptor clustering in spinal neurons
    • Kirsch, J., and H. Betz. 1998. Glycine-receptor activation is required for receptor clustering in spinal neurons. Nature. 392:717-720.
    • (1998) Nature , vol.392 , pp. 717-720
    • Kirsch, J.1    Betz, H.2
  • 25
    • 21444447912 scopus 로고    scopus 로고
    • Postsynaptic scaffold proteins at non-synaptic sites
    • Kneussel, M. 2005. Postsynaptic scaffold proteins at non-synaptic sites. EMBO Rep. 6:22-27.
    • (2005) EMBO Rep. , vol.6 , pp. 22-27
    • Kneussel, M.1
  • 26
    • 0034284148 scopus 로고    scopus 로고
    • Clustering of inhibitory neurotransmitter receptors at developing postsynaptic sites: The membrane activation model
    • Kneussel, M., and H. Betz. 2000. Clustering of inhibitory neurotransmitter receptors at developing postsynaptic sites: the membrane activation model. Trends Neurosci. 23:429-435.
    • (2000) Trends Neurosci. , vol.23 , pp. 429-435
    • Kneussel, M.1    Betz, H.2
  • 27
  • 28
    • 0028942256 scopus 로고
    • Actin- and microtubule-dependent organelle motors: Interrelationships between the two motility systems
    • Langford, G.M. 1995. Actin- and microtubule-dependent organelle motors: interrelationships between the two motility systems. Curr. Opin. Cell Biol. 7:82-88.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 82-88
    • Langford, G.M.1
  • 29
    • 2642625663 scopus 로고    scopus 로고
    • Strychnine-sensitive stabilization of postsynaptic glycine receptor clusters
    • Levi, S., C. Vannier, and A. Triller. 1998. Strychnine-sensitive stabilization of postsynaptic glycine receptor clusters. J. Cell Sci. 111:335-345.
    • (1998) J. Cell Sci. , vol.111 , pp. 335-345
    • Levi, S.1    Vannier, C.2    Triller, A.3
  • 30
    • 0242551549 scopus 로고    scopus 로고
    • Some assembly required: The development of neuronal synapses
    • Li, Z., and M. Sheng. 2003. Some assembly required: the development of neuronal synapses. Nat. Rev. Mol. Cell Biol. 4:833-841.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 833-841
    • Li, Z.1    Sheng, M.2
  • 31
    • 3042857703 scopus 로고    scopus 로고
    • Mapping and quantitative analysis of gephyrin cytoplasmic trafficking pathways in motoneurons, using an optimized transmission electron microscopy color imaging (TEMCI) procedure
    • Lorenzo, L.E., A. Barbe, and H. Bras. 2004. Mapping and quantitative analysis of gephyrin cytoplasmic trafficking pathways in motoneurons, using an optimized transmission electron microscopy color imaging (TEMCI) procedure. J. Neurocytol. 33:241-249.
    • (2004) J. Neurocytol. , vol.33 , pp. 241-249
    • Lorenzo, L.E.1    Barbe, A.2    Bras, H.3
  • 32
    • 0034810292 scopus 로고    scopus 로고
    • Rapid formation and remodeling of postsynaptic densities in developing dendrites
    • Marrs, G.S., S.H. Green, and M.E. Dailey. 2001. Rapid formation and remodeling of postsynaptic densities in developing dendrites. Nat. Neurosci. 4:1006-1013.
    • (2001) Nat. Neurosci. , vol.4 , pp. 1006-1013
    • Marrs, G.S.1    Green, S.H.2    Dailey, M.E.3
  • 33
    • 0035319805 scopus 로고    scopus 로고
    • Constructing inhibitory synapses
    • Moss, S.J., and T.G. Smart. 2001. Constructing inhibitory synapses. Nat. Rev. Neurosci. 2:240-250.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 240-250
    • Moss, S.J.1    Smart, T.G.2
  • 34
    • 0034660288 scopus 로고    scopus 로고
    • Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein
    • Naisbitt, S., J. Valtschanoff, D.W. Allison, C. Sala, E. Kim, A.M. Craig, R.J. Weinberg, and M. Sheng. 2000. Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein. J. Neurosci. 20:4524-4534.
    • (2000) J. Neurosci. , vol.20 , pp. 4524-4534
    • Naisbitt, S.1    Valtschanoff, J.2    Allison, D.W.3    Sala, C.4    Kim, E.5    Craig, A.M.6    Weinberg, R.J.7    Sheng, M.8
  • 35
    • 13244278242 scopus 로고    scopus 로고
    • The actin-binding protein profilin I is localized at synaptic sites in an activity-regulated manner
    • Neuhoff, H., M. Sassoe-Pognetto, P. Panzanelli, C. Maas, W. Witke, and M. Kneussel. 2005. The actin-binding protein profilin I is localized at synaptic sites in an activity-regulated manner. Eur. J. Neurosci. 21:15-25.
    • (2005) Eur. J. Neurosci. , vol.21 , pp. 15-25
    • Neuhoff, H.1    Sassoe-Pognetto, M.2    Panzanelli, P.3    Maas, C.4    Witke, W.5    Kneussel, M.6
  • 36
    • 0032754578 scopus 로고    scopus 로고
    • Gamma-tubulin at ten: Progress and prospects
    • Oakley, B.R., and Y.N. Akkari. 1999. Gamma-tubulin at ten: progress and prospects. Cell Struct. Funct. 24:365-372.
    • (1999) Cell Struct. Funct. , vol.24 , pp. 365-372
    • Oakley, B.R.1    Akkari, Y.N.2
  • 37
    • 0033492575 scopus 로고    scopus 로고
    • Microtubule binding by CRIPT and its potential role in the synaptic clustering of PSD-95
    • Passafaro, M., C. Sala, M. Niethammer, and M. Sheng. 1999. Microtubule binding by CRIPT and its potential role in the synaptic clustering of PSD-95. Nat. Neurosci. 2:1063-1069.
    • (1999) Nat. Neurosci. , vol.2 , pp. 1063-1069
    • Passafaro, M.1    Sala, C.2    Niethammer, M.3    Sheng, M.4
  • 38
    • 0023746658 scopus 로고
    • Single cell assay with an automated capillary microinjection system
    • Pepperkok, R., C. Schneider, L. Philipson, and W. Ansorge. 1988. Single cell assay with an automated capillary microinjection system. Exp. Cell Res. 178:369-376.
    • (1988) Exp. Cell Res. , vol.178 , pp. 369-376
    • Pepperkok, R.1    Schneider, C.2    Philipson, L.3    Ansorge, W.4
  • 39
    • 0029909492 scopus 로고    scopus 로고
    • Emergence of activity-dependent, bidirectional control of microtubule-associated protein MAP2 phosphorylation during postnatal development
    • Quinlan, E.M., and S. Halpain. 1996. Emergence of activity-dependent, bidirectional control of microtubule-associated protein MAP2 phosphorylation during postnatal development. J. Neurosci. 16:7627-7637.
    • (1996) J. Neurosci. , vol.16 , pp. 7627-7637
    • Quinlan, E.M.1    Halpain, S.2
  • 40
    • 0036195310 scopus 로고    scopus 로고
    • Strychnine-blocked glycine receptor is removed from synapses by a shift in insertion/degradation equilibrium
    • Rasmussen, H., T. Rasmussen, A. Triller, and C. Vannier. 2002. Strychnine-blocked glycine receptor is removed from synapses by a shift in insertion/degradation equilibrium. Mol. Cell. Neurosci. 19:201-215.
    • (2002) Mol. Cell. Neurosci. , vol.19 , pp. 201-215
    • Rasmussen, H.1    Rasmussen, T.2    Triller, A.3    Vannier, C.4
  • 41
    • 0030939131 scopus 로고    scopus 로고
    • KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multivesicular body-like organelles
    • Saito, N., Y. Okada, Y. Noda, Y. Kinoshita, S. Kondo, and N. Hirokawa. 1997. KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multivesicular body-like organelles. Neuron. 18:425-438.
    • (1997) Neuron , vol.18 , pp. 425-438
    • Saito, N.1    Okada, Y.2    Noda, Y.3    Kinoshita, Y.4    Kondo, S.5    Hirokawa, N.6
  • 43
    • 0035511932 scopus 로고    scopus 로고
    • Induction, assembly, maturation and maintenance of a postsynaptic apparatus
    • Sanes, J.R., and J.W. Lichtman. 2001. Induction, assembly, maturation and maintenance of a postsynaptic apparatus. Nat. Rev. Neurosci. 2:791-805.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 791-805
    • Sanes, J.R.1    Lichtman, J.W.2
  • 44
    • 0023160121 scopus 로고
    • The Mr 93,000 polypeptide of the postsynaptic glycine receptor complex is a peripheral membrane protein
    • Schmitt, B., P. Knaus, C.M. Becker, and H. Betz. 1987. The Mr 93,000 polypeptide of the postsynaptic glycine receptor complex is a peripheral membrane protein. Biochemistry. 26:805-811.
    • (1987) Biochemistry , vol.26 , pp. 805-811
    • Schmitt, B.1    Knaus, P.2    Becker, C.M.3    Betz, H.4
  • 45
    • 0034625631 scopus 로고    scopus 로고
    • Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport
    • Setou, M., T. Nakagawa, D.H. Seog, and N. Hirokawa. 2000. Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport. Science. 288:1796-1802.
    • (2000) Science , vol.288 , pp. 1796-1802
    • Setou, M.1    Nakagawa, T.2    Seog, D.H.3    Hirokawa, N.4
  • 46
    • 0037007668 scopus 로고    scopus 로고
    • Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites
    • Setou, M., D.H. Seog, Y. Tanaka, Y. Kanai, Y. Takei, M. Kawagishi, and N. Hirokawa. 2002. Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites. Nature. 417:83-87.
    • (2002) Nature , vol.417 , pp. 83-87
    • Setou, M.1    Seog, D.H.2    Tanaka, Y.3    Kanai, Y.4    Takei, Y.5    Kawagishi, M.6    Hirokawa, N.7
  • 47
    • 0035816706 scopus 로고    scopus 로고
    • X-ray crystal structure of the trimeric N-terminal domain of gephyrin
    • Sola, M., M. Kneussel, I.S. Heck, H. Betz, and W. Weissenhorn. 2001. X-ray crystal structure of the trimeric N-terminal domain of gephyrin. J. Biol. Chem. 276:25294-25301.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25294-25301
    • Sola, M.1    Kneussel, M.2    Heck, I.S.3    Betz, H.4    Weissenhorn, W.5
  • 49
    • 0036176244 scopus 로고    scopus 로고
    • Rapid turnover of actin in dendritic spines and its regulation by activity
    • Star, E.N., D.J. Kwiatkowski, and V.N. Murthy. 2002. Rapid turnover of actin in dendritic spines and its regulation by activity. Nat. Neurosci. 5:239-246.
    • (2002) Nat. Neurosci. , vol.5 , pp. 239-246
    • Star, E.N.1    Kwiatkowski, D.J.2    Murthy, V.N.3
  • 50
    • 0036323370 scopus 로고    scopus 로고
    • Rapid recruitment of NMDA receptor transport packets to nascent synapses
    • Washbourne, P., J.E. Bennett, and A.K. McAllister. 2002. Rapid recruitment of NMDA receptor transport packets to nascent synapses. Nat. Neurosci. 5:751-759.
    • (2002) Nat. Neurosci. , vol.5 , pp. 751-759
    • Washbourne, P.1    Bennett, J.E.2    McAllister, A.K.3
  • 51
    • 0037163078 scopus 로고    scopus 로고
    • Interaction of SAP97 with minus-end-directed actin motor myosin VI. Implications for AMPA receptor trafficking
    • Wu, H., J.E. Nash, P. Zamorano, and C.C. Garner. 2002. Interaction of SAP97 with minus-end-directed actin motor myosin VI. Implications for AMPA receptor trafficking. J. Biol. Chem. 277:30928-30934.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30928-30934
    • Wu, H.1    Nash, J.E.2    Zamorano, P.3    Garner, C.C.4
  • 52
    • 0032192512 scopus 로고    scopus 로고
    • Biochemical and immunocytochemical characterization of GRIP, a putative AMPA receptor anchoring protein, in rat brain
    • Wyszynski, M., E. Kim, F.C. Yang, and M. Sheng. 1998. Biochemical and immunocytochemical characterization of GRIP, a putative AMPA receptor anchoring protein, in rat brain. Neuropharmacology. 37:1335-1344.
    • (1998) Neuropharmacology , vol.37 , pp. 1335-1344
    • Wyszynski, M.1    Kim, E.2    Yang, F.C.3    Sheng, M.4


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