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Volumn 9, Issue 10, 2006, Pages 1294-1301

NGL family PSD-95-interacting adhesion molecules regulate excitatory synapse formation

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CELL ADHESION MOLECULE; ISOPROTEIN; NETRIN; NETRIN G LIGAND 2; POSTSYNAPTIC DENSITY PROTEIN 95; UNCLASSIFIED DRUG;

EID: 33749026932     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/nn1763     Document Type: Article
Times cited : (216)

References (50)
  • 1
    • 0242551549 scopus 로고    scopus 로고
    • Some assembly required: The development of neuronal synapses
    • Li, Z. & Sheng, M. Some assembly required: the development of neuronal synapses. Nat. Rev. Mol. Cell Biol. 4, 833-841 (2003).
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 833-841
    • Li, Z.1    Sheng, M.2
  • 3
    • 7044270780 scopus 로고    scopus 로고
    • Cell adhesion molecules in synapse formation
    • Washbourne, P. et al. Cell adhesion molecules in synapse formation. J. Neurosci. 24, 9244-9249 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 9244-9249
    • Washbourne, P.1
  • 5
    • 26944453998 scopus 로고    scopus 로고
    • Building excitatory and inhibitory synapses: Balancing neuroligin partnerships
    • Levinson, J.N. & El-Husseini, A. Building excitatory and inhibitory synapses: balancing neuroligin partnerships. Neuron 48, 171-174 (2005).
    • (2005) Neuron , vol.48 , pp. 171-174
    • Levinson, J.N.1    El-Husseini, A.2
  • 6
    • 30344456451 scopus 로고    scopus 로고
    • How to build a central synapse: Clues from cell culture
    • Craig, A.M., Graf, E.R. & Linhoff, M.W. How to build a central synapse: clues from cell culture. Trends Neurosci. 29, 8-20 (2006).
    • (2006) Trends Neurosci. , vol.29 , pp. 8-20
    • Craig, A.M.1    Graf, E.R.2    Linhoff, M.W.3
  • 7
    • 30344454380 scopus 로고    scopus 로고
    • Neuroligins and neurexins: Linking cell adhesion, synapse formation and cognitive function
    • Dean, C. & Dresbach, T. Neuroligins and neurexins: linking cell adhesion, synapse formation and cognitive function. Trends Neurosci. 29, 21-29 (2006).
    • (2006) Trends Neurosci. , vol.29 , pp. 21-29
    • Dean, C.1    Dresbach, T.2
  • 8
    • 32344432703 scopus 로고    scopus 로고
    • Cell-cell interactions in synaptogenesis
    • Akins, M.R. & Biederer, T. Cell-cell interactions in synaptogenesis. Curr. Opin. Neurobiol. 16, 83-89 (2006).
    • (2006) Curr. Opin. Neurobiol. , vol.16 , pp. 83-89
    • Akins, M.R.1    Biederer, T.2
  • 9
    • 0037200037 scopus 로고    scopus 로고
    • SynCAM, a synaptic adhesion molecule that drives synapse assembly
    • Biederer, T. et al. SynCAM, a synaptic adhesion molecule that drives synapse assembly. Science 297, 1525-1531 (2002).
    • (2002) Science , vol.297 , pp. 1525-1531
    • Biederer, T.1
  • 10
    • 0037031592 scopus 로고    scopus 로고
    • Sidekicks: Synaptic adhesion molecules that promote lamina-specific connectivity in the retina
    • Yamagata, M., Weiner, J.A. & Sanes, J.R. Sidekicks: synaptic adhesion molecules that promote lamina-specific connectivity in the retina. Cell 110, 649-660 (2002).
    • (2002) Cell , vol.110 , pp. 649-660
    • Yamagata, M.1    Weiner, J.A.2    Sanes, J.R.3
  • 11
    • 0029036374 scopus 로고
    • Neuroligin 1: A splice site-specific ligand for beta-neurexins
    • Ichtchenko, K. et al. Neuroligin 1: a splice site-specific ligand for beta-neurexins. Cell 81, 435-443 (1995).
    • (1995) Cell , vol.81 , pp. 435-443
    • Ichtchenko, K.1
  • 12
    • 0033063445 scopus 로고    scopus 로고
    • A striking organization of a large family of human neural cadherinlike cell adhesion genes
    • Wu, Q. & Maniatis, T. A striking organization of a large family of human neural cadherinlike cell adhesion genes. Cell 97, 779-790 (1999).
    • (1999) Cell , vol.97 , pp. 779-790
    • Wu, Q.1    Maniatis, T.2
  • 13
    • 0030026657 scopus 로고    scopus 로고
    • Structures, alternative splicing, and neurexin binding of multiple neuroligins
    • Ichtchenko, K., Nguyen, T. & Sudhof, T.C. Structures, alternative splicing, and neurexin binding of multiple neuroligins. J. Biol. Chem. 271, 2676-2682 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 2676-2682
    • Ichtchenko, K.1    Nguyen, T.2    Sudhof, T.C.3
  • 14
    • 0030770840 scopus 로고    scopus 로고
    • Binding of neuroligins to PSD-95
    • Irie, M. et al. Binding of neuroligins to PSD-95. Science 277, 1511-1515 (1997).
    • (1997) Science , vol.277 , pp. 1511-1515
    • Irie, M.1
  • 15
    • 0037743572 scopus 로고    scopus 로고
    • Neurexin mediates the assembly of presynaptic terminals
    • Dean, C. et al. Neurexin mediates the assembly of presynaptic terminals. Nat. Neurosci. 6, 708-716 (2003).
    • (2003) Nat. Neurosci. , vol.6 , pp. 708-716
    • Dean, C.1
  • 16
    • 13544269142 scopus 로고    scopus 로고
    • Control of excitatory and inhibitory synapse formation by neuroligins
    • Chih, B., Engelman, H. & Scheiffele, P. Control of excitatory and inhibitory synapse formation by neuroligins. Science 307, 1324-1328 (2005).
    • (2005) Science , vol.307 , pp. 1324-1328
    • Chih, B.1    Engelman, H.2    Scheiffele, P.3
  • 17
    • 11144352245 scopus 로고    scopus 로고
    • Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins
    • Graf, E.R., Zhang, X., Jin, S.X., Linhoff, M.W. & Craig, A.M. Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins. Cell 119, 1013-1026 (2004).
    • (2004) Cell , vol.119 , pp. 1013-1026
    • Graf, E.R.1    Zhang, X.2    Jin, S.X.3    Linhoff, M.W.4    Craig, A.M.5
  • 18
    • 0034625250 scopus 로고    scopus 로고
    • Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons
    • Scheiffele, P., Fan, J., Choih, J., Fetter, R. & Serafini, T. Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons. Cell 101, 657-669 (2000).
    • (2000) Cell , vol.101 , pp. 657-669
    • Scheiffele, P.1    Fan, J.2    Choih, J.3    Fetter, R.4    Serafini, T.5
  • 19
    • 17844363471 scopus 로고    scopus 로고
    • Postsynaptic assembly induced by neurexin-neuroligin interaction and neurotransmitter
    • Nam, C.I. & Chen, L. Postsynaptic assembly induced by neurexin-neuroligin interaction and neurotransmitter. Proc. Natl. Acad. Sci. USA 102, 6137-6142 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6137-6142
    • Nam, C.I.1    Chen, L.2
  • 20
    • 0346121341 scopus 로고    scopus 로고
    • Functional excitatory synapses in HEK293 cells expressing neuroligin and glutamate receptors
    • Fu, Z., Washbourne, P., Ortinski, P. & Vicini, S. Functional excitatory synapses in HEK293 cells expressing neuroligin and glutamate receptors. J. Neurophysiol. 90, 3950-3957 (2003).
    • (2003) J. Neurophysiol. , vol.90 , pp. 3950-3957
    • Fu, Z.1    Washbourne, P.2    Ortinski, P.3    Vicini, S.4
  • 21
    • 20444434316 scopus 로고    scopus 로고
    • Neuroligins mediate excitatory and inhibitory synapse formation: Involvement of PSD-95 and neurexin-1beta in neuroligin-induced synaptic specificity
    • Levinson, J.N. et al. Neuroligins mediate excitatory and inhibitory synapse formation: involvement of PSD-95 and neurexin-1beta in neuroligin-induced synaptic specificity. J. Biol. Chem. 280, 17312-17319 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 17312-17319
    • Levinson, J.N.1
  • 22
    • 0029914941 scopus 로고    scopus 로고
    • CASK: A novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins
    • Hata, Y., Butz, S. & Sudhof, T.C. CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins. J. Neurosci. 16, 2488-2494 (1996).
    • (1996) J. Neurosci. , vol.16 , pp. 2488-2494
    • Hata, Y.1    Butz, S.2    Sudhof, T.C.3
  • 23
    • 0034704089 scopus 로고    scopus 로고
    • Mints as adaptors. Direct binding to neurexins and recruitment of munc18
    • Biederer, T. & Sudhof, T.C. Mints as adaptors. Direct binding to neurexins and recruitment of munc18. J. Biol. Chem. 275, 39803-39806 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 39803-39806
    • Biederer, T.1    Sudhof, T.C.2
  • 24
    • 26944444692 scopus 로고    scopus 로고
    • A splice code for trans-synaptic cell adhesion mediated by binding of neuroligin 1 to alpha- and beta-neurexins
    • Boucard, A.A., Chubykin, A.A., Comoletti, D., Taylor, P. & Sudhof, T.C. A splice code for trans-synaptic cell adhesion mediated by binding of neuroligin 1 to alpha- and beta-neurexins. Neuron 48, 229-236 (2005).
    • (2005) Neuron , vol.48 , pp. 229-236
    • Boucard, A.A.1    Chubykin, A.A.2    Comoletti, D.3    Taylor, P.4    Sudhof, T.C.5
  • 25
    • 0036270811 scopus 로고    scopus 로고
    • Structure and evolution of neurexin genes: Insight into the mechanism of alternative splicing
    • Tabuchi, K. & Sudhof, T.C. Structure and evolution of neurexin genes: insight into the mechanism of alternative splicing. Genomics 79, 849-859 (2002).
    • (2002) Genomics , vol.79 , pp. 849-859
    • Tabuchi, K.1    Sudhof, T.C.2
  • 26
    • 0033215463 scopus 로고    scopus 로고
    • The structure of the ligand-binding domain of neurexin Ibeta: Regulation of LNS domain function by alternative splicing
    • Rudenko, G., Nguyen, T., Chelliah, Y., Sudhof, T.C. & Deisenhofer, J. The structure of the ligand-binding domain of neurexin Ibeta: regulation of LNS domain function by alternative splicing. Cell 99, 93-101 (1999).
    • (1999) Cell , vol.99 , pp. 93-101
    • Rudenko, G.1    Nguyen, T.2    Chelliah, Y.3    Sudhof, T.C.4    Deisenhofer, J.5
  • 27
    • 33745994650 scopus 로고    scopus 로고
    • Alternative splicing controls selective trans-synaptic interactions of the neuroligin-neurexin complex
    • Chih, B., Gollan, L. & Scheiffele, P. Alternative splicing controls selective trans-synaptic interactions of the neuroligin-neurexin complex. Neuron 51, 171-178 (2006).
    • (2006) Neuron , vol.51 , pp. 171-178
    • Chih, B.1    Gollan, L.2    Scheiffele, P.3
  • 28
    • 33646464124 scopus 로고    scopus 로고
    • Structure function and splice site analysis of the synaptogenic activity of the neurexin-1 beta LNS domain
    • Graf, E.R., Kang, Y., Hauner, A.M. & Craig, A.M. Structure function and splice site analysis of the synaptogenic activity of the neurexin-1 beta LNS domain. J. Neurosci. 26, 4256-4265 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 4256-4265
    • Graf, E.R.1    Kang, Y.2    Hauner, A.M.3    Craig, A.M.4
  • 29
    • 0033514448 scopus 로고    scopus 로고
    • Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses
    • Song, J.Y., Ichtchenko, K., Sudhof, T.C. & Brose, N. Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses. Proc. Natl. Acad. Sci. USA 96, 1100-1105 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1100-1105
    • Song, J.Y.1    Ichtchenko, K.2    Sudhof, T.C.3    Brose, N.4
  • 30
    • 7244232730 scopus 로고    scopus 로고
    • Neuroligin 2 is exclusively localized to inhibitory synapses
    • Varoqueaux, F., Jamain, S. & Brose, N. Neuroligin 2 is exclusively localized to inhibitory synapses. Eur. J. Cell Biol. 83, 449-456 (2004).
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 449-456
    • Varoqueaux, F.1    Jamain, S.2    Brose, N.3
  • 31
    • 4644353516 scopus 로고    scopus 로고
    • A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin
    • Prange, O., Wong, T.P., Gerrow, K., Wang, Y.T. & El-Husseini, A. A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin. Proc. Natl. Acad. Sci. USA 101, 13915-13920 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13915-13920
    • Prange, O.1    Wong, T.P.2    Gerrow, K.3    Wang, Y.T.4    El-Husseini, A.5
  • 32
    • 12144278370 scopus 로고    scopus 로고
    • Selective capability of SynCAM and neuroligin for functional synapse assembly
    • Sara, Y. et al. Selective capability of SynCAM and neuroligin for functional synapse assembly. J. Neurosci. 25, 260-270 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 260-270
    • Sara, Y.1
  • 33
    • 0034279190 scopus 로고    scopus 로고
    • Netrin-G1: A novel glycosyl phosphatidylinositol-linked mammalian netrin that is functionally divergent from classical netrins
    • Nakashiba, T. et al. Netrin-G1: a novel glycosyl phosphatidylinositol- linked mammalian netrin that is functionally divergent from classical netrins. J. Neurosci. 20, 6540-6550 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 6540-6550
    • Nakashiba, T.1
  • 34
    • 0036170165 scopus 로고    scopus 로고
    • Complementary expression and neurite outgrowth activity of netrin-G subfamily members
    • Nakashiba, T., Nishimura, S., Ikeda, T. & Itohara, S. Complementary expression and neurite outgrowth activity of netrin-G subfamily members. Mech. Dev. 111, 47-60 (2002).
    • (2002) Mech. Dev. , vol.111 , pp. 47-60
    • Nakashiba, T.1    Nishimura, S.2    Ikeda, T.3    Itohara, S.4
  • 35
    • 0036215967 scopus 로고    scopus 로고
    • Laminets: Laminin- and netrin-related genes expressed in distinct neuronal subsets
    • Yin, Y., Miner, J.H. & Sanes, J.R. Laminets: laminin- and netrin-related genes expressed in distinct neuronal subsets. Mol. Cell. Neurosci. 19, 344-358 (2002).
    • (2002) Mol. Cell. Neurosci. , vol.19 , pp. 344-358
    • Yin, Y.1    Miner, J.H.2    Sanes, J.R.3
  • 36
    • 0344442833 scopus 로고    scopus 로고
    • The netrin-G1 ligand NGL-1 promotes the outgrowth of thalamocortical axons
    • Lin, J.C., Ho, W.H., Gurney, A. & Rosenthal, A. The netrin-G1 ligand NGL-1 promotes the outgrowth of thalamocortical axons. Nat. Neurosci. 6, 1270-1276 (2003).
    • (2003) Nat. Neurosci. , vol.6 , pp. 1270-1276
    • Lin, J.C.1    Ho, W.H.2    Gurney, A.3    Rosenthal, A.4
  • 37
    • 0035865546 scopus 로고    scopus 로고
    • Laminar organization of the NMDA receptor complex within the postsynaptic density
    • Valtschanoff, J.G. & Weinberg, R.J. Laminar organization of the NMDA receptor complex within the postsynaptic density. J. Neurosci. 21, 1211-1217 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 1211-1217
    • Valtschanoff, J.G.1    Weinberg, R.J.2
  • 38
    • 0029031896 scopus 로고
    • Synaptic vesicle dynamics in living cultured hippocampal neurons visualized with CY3-conjugated antibodies directed against the lumenal domain of synaptotagmin
    • Kraszewski, K. et al. Synaptic vesicle dynamics in living cultured hippocampal neurons visualized with CY3-conjugated antibodies directed against the lumenal domain of synaptotagmin. J. Neurosci. 15, 4328-4342 (1995).
    • (1995) J. Neurosci. , vol.15 , pp. 4328-4342
    • Kraszewski, K.1
  • 39
    • 0033178747 scopus 로고    scopus 로고
    • GPI-microdomains: A role in signalling via immunoreceptors
    • Horejsi, V. et al. GPI-microdomains: a role in signalling via immunoreceptors. Immunol. Today 20, 356-361 (1999).
    • (1999) Immunol. Today , vol.20 , pp. 356-361
    • Horejsi, V.1
  • 40
    • 20444390412 scopus 로고    scopus 로고
    • Human netrin-G1 isoforms show evidence of differential expression
    • Meerabux, J.M. et al. Human netrin-G1 isoforms show evidence of differential expression. Genomics 86, 112-116 (2005).
    • (2005) Genomics , vol.86 , pp. 112-116
    • Meerabux, J.M.1
  • 41
    • 0346118881 scopus 로고    scopus 로고
    • Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1beta
    • Comoletti, D. et al. Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1beta. J. Biol. Chem. 278, 50497-50505 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 50497-50505
    • Comoletti, D.1
  • 42
    • 0032898374 scopus 로고    scopus 로고
    • Requirement of N-terminal cysteines of PSD-95 for PSD-95 multimerization and ternary complex formation, but not for binding to potassium channel Kv1.4
    • Hsueh, Y.P. & Sheng, M. Requirement of N-terminal cysteines of PSD-95 for PSD-95 multimerization and ternary complex formation, but not for binding to potassium channel Kv1.4. J. Biol. Chem. 274, 532-536 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 532-536
    • Hsueh, Y.P.1    Sheng, M.2
  • 43
    • 0042386445 scopus 로고    scopus 로고
    • Lipid- and protein-mediated multimerization of PSD-95: Implications for receptor clustering and assembly of synaptic protein networks
    • Christopherson, K.S. et al. Lipid- and protein-mediated multimerization of PSD-95: implications for receptor clustering and assembly of synaptic protein networks. J. Cell Sci. 116, 3213-3219 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 3213-3219
    • Christopherson, K.S.1
  • 44
    • 0037656313 scopus 로고    scopus 로고
    • Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are associated with autism
    • Jamain, S. et al. Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are associated with autism. Nat. Genet. 34, 27-29 (2003).
    • (2003) Nat. Genet. , vol.34 , pp. 27-29
    • Jamain, S.1
  • 45
    • 12144291350 scopus 로고    scopus 로고
    • X-linked mental retardation and autism are associated with a mutation in the NLGN4 gene, a member of the neuroligin family
    • Laumonnier, F. et al. X-linked mental retardation and autism are associated with a mutation in the NLGN4 gene, a member of the neuroligin family. Am. J. Hum. Genet. 74, 552-557 (2004).
    • (2004) Am. J. Hum. Genet. , vol.74 , pp. 552-557
    • Laumonnier, F.1
  • 46
    • 20144389549 scopus 로고    scopus 로고
    • Analysis of the neuroligin 3 and 4 genes in autism and other neuropsychiatric patients
    • Yan, J. et al. Analysis of the neuroligin 3 and 4 genes in autism and other neuropsychiatric patients. Mol. Psychiatry 10, 329-332 (2005).
    • (2005) Mol. Psychiatry , vol.10 , pp. 329-332
    • Yan, J.1
  • 47
    • 3543136466 scopus 로고    scopus 로고
    • Disorder-associated mutations lead to functional inactivation of neuroligins
    • Chih, B., Afridi, S.K., Clark, L. & Scheiffele, P. Disorder-associated mutations lead to functional inactivation of neuroligins. Hum. Mol. Genet. 13, 1471-1477 (2004).
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1471-1477
    • Chih, B.1    Afridi, S.K.2    Clark, L.3    Scheiffele, P.4
  • 48
    • 2442713977 scopus 로고    scopus 로고
    • The Arg451Cys-neuroligin-3 mutation associated with autism reveals a defect in protein processing
    • Comoletti, D. et al. The Arg451Cys-neuroligin-3 mutation associated with autism reveals a defect in protein processing. J. Neurosci. 24, 4889-4893 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 4889-4893
    • Comoletti, D.1
  • 49
    • 20644443891 scopus 로고    scopus 로고
    • Dissection of synapse induction by neuroligins: Effect of a neuroligin mutation associated with autism
    • Chubykin, A.A. et al. Dissection of synapse induction by neuroligins: effect of a neuroligin mutation associated with autism. J. Biol. Chem. 280, 22365-22374 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 22365-22374
    • Chubykin, A.A.1
  • 50
    • 13444283651 scopus 로고    scopus 로고
    • A family-based association study and gene expression nalyses of netrin-G1 and -G2 genes in schizophrenia
    • Aoki-Suzuki, M. et al. A family-based association study and gene expression nalyses of netrin-G1 and -G2 genes in schizophrenia. Biol. Psychiatry 57, 382-393 (2005).
    • (2005) Biol. Psychiatry , vol.57 , pp. 382-393
    • Aoki-Suzuki, M.1


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