메뉴 건너뛰기




Volumn 6, Issue 7, 2003, Pages 708-716

Neurexin mediates the assembly of presynaptic terminals

Author keywords

[No Author keywords available]

Indexed keywords

BETA NEUREXIN; CELL SURFACE PROTEIN; MEMBRANE PROTEIN; NEUREXIN; NEUROLIGIN 1; UNCLASSIFIED DRUG;

EID: 0037743572     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/nn1074     Document Type: Article
Times cited : (498)

References (37)
  • 1
    • 0032936983 scopus 로고    scopus 로고
    • Development of the vertebrate neuromuscular junction
    • Sanes, J.R. & Lichtman, J.W. Development of the vertebrate neuromuscular junction. Annu. Rev. Neurosci, 22, 389-442 (1999).
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 389-442
    • Sanes, J.R.1    Lichtman, J.W.2
  • 3
    • 0038071095 scopus 로고    scopus 로고
    • Cell-cell signaling during synapse formation in the CNS
    • Scheiffele, P. Cell-cell signaling during synapse formation in the CNS. Annu. Rev. Neurosci. 26, 485-508 (2003).
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 485-508
    • Scheiffele, P.1
  • 4
    • 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
  • 5
    • 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
  • 6
    • 0034625250 scopus 로고    scopus 로고
    • Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons
    • Scheiffele, P. et al. 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
  • 7
    • 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
  • 8
    • 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
  • 9
    • 0031861717 scopus 로고    scopus 로고
    • CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins
    • Kurschner, C., Mermelstein, P.G., Holden, W.T. & Surmeier, D.J. CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins. Mol. Cell. Neurosci. 11, 161-172 (1998).
    • (1998) Mol. Cell. Neurosci. , vol.11 , pp. 161-172
    • Kurschner, C.1    Mermelstein, P.G.2    Holden, W.T.3    Surmeier, D.J.4
  • 10
    • 0033613931 scopus 로고    scopus 로고
    • Crystal'structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly
    • Bourne, Y., Taylor, P., Bougis, P.E. & Marchot, P. Crystal'structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly. J. Biol. Chem. 274, 2963-2970 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 2963-2970
    • Bourne, Y.1    Taylor, P.2    Bougis, P.E.3    Marchot, P.4
  • 11
    • 0035813131 scopus 로고    scopus 로고
    • Acetylcholinesterase H and T dimers are associated through the same contact. Mutations at this interface interfere with the C-terminal T peptide, inducing degradation rather than secretion
    • Morel, N. et al. Acetylcholinesterase H and T dimers are associated through the same contact. Mutations at this interface interfere with the C-terminal T peptide, inducing degradation rather than secretion. J. Biol. Chem. 276, 37379-37389 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 37379-37389
    • Morel, N.1
  • 12
    • 0023805444 scopus 로고
    • Amphiphilic and nonamphiphilic forms of Torpedo cholinesterases: Solubility and aggregation properties
    • Bon, S., Toutant, J.P., Meflah, K. & Massoulie, J. Amphiphilic and nonamphiphilic forms of Torpedo cholinesterases: solubility and aggregation properties. J. Neurochem. 51, 776-785 (1988).
    • (1988) J. Neurochem. , vol.51 , pp. 776-785
    • Bon, S.1    Toutant, J.P.2    Meflah, K.3    Massoulie, J.4
  • 13
    • 0026769035 scopus 로고
    • Neurexins: Synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin
    • Ushkaryov, Y.A., Petrenko, A.G., Geppert, M. & Sudhof, T.C. Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin. Science 257, 50-56 (1992).
    • (1992) Science , vol.257 , pp. 50-56
    • Ushkaryov, Y.A.1    Petrenko, A.G.2    Geppert, M.3    Sudhof, T.C.4
  • 14
    • 0037155203 scopus 로고    scopus 로고
    • Genetic analysis of alpha-latrotoxin receptors reveals functional interdependence of CIRL/latrophilin 1 and neurexin 1 alpha
    • Tobaben, S., Sudhof, T.C. & Stahl, B. Genetic analysis of alpha-latrotoxin receptors reveals functional interdependence of CIRL/latrophilin 1 and neurexin 1 alpha. J. Biol. Chem. 277, 6359-6365 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 6359-6365
    • Tobaben, S.1    Sudhof, T.C.2    Stahl, B.3
  • 15
    • 0033103549 scopus 로고    scopus 로고
    • Neurexins are functional alpha-latrotoxin receptors
    • Sugita, S., Khvochtev, M. & Sudhof, T.C. Neurexins are functional alpha-latrotoxin receptors. Neuron 22, 489-496 (1999).
    • (1999) Neuron , vol.22 , pp. 489-496
    • Sugita, S.1    Khvochtev, M.2    Sudhof, T.C.3
  • 16
    • 0030986342 scopus 로고    scopus 로고
    • Neurexin is expressed on nerves, but not at nerve terminals, in the electric organ
    • Russell, A.B. & Carlson, S.S. Neurexin is expressed on nerves, but not at nerve terminals, in the electric organ. J. Neurosci. 17, 4734-4743 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 4734-4743
    • Russell, A.B.1    Carlson, S.S.2
  • 17
    • 0030926546 scopus 로고    scopus 로고
    • Deciphering the function of neurexins at cellular junctions
    • Littleton, J.T., Bhat, M.A. & Bellen, H.J. Deciphering the function of neurexins at cellular junctions. J. Cell Biol. 137, 793-796 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 793-796
    • Littleton, J.T.1    Bhat, M.A.2    Bellen, H.J.3
  • 18
    • 0034917524 scopus 로고    scopus 로고
    • alpha-Latrotoxin and its receptors: Neurexins and ClRL/latrophitins
    • Sudhof, T.C. alpha-Latrotoxin and its receptors: neurexins and ClRL/latrophitins. Annu. Rev. Neurosci. 24, 933-962 (2001).
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 933-962
    • Sudhof, T.C.1
  • 19
    • 0037174639 scopus 로고    scopus 로고
    • Neural and immunological synaptic relations
    • Dustin, M.L. & Colman, D.R. Neural and immunological synaptic relations. Science 298, 785-789 (2002).
    • (2002) Science , vol.298 , pp. 785-789
    • Dustin, M.L.1    Colman, D.R.2
  • 20
    • 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
  • 21
    • 0032544613 scopus 로고    scopus 로고
    • A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain
    • Butz, S., Okamoto, M. & Sudhof, T.C. A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Cell 94, 773-782 (1998).
    • (1998) Cell , vol.94 , pp. 773-782
    • Butz, S.1    Okamoto, M.2    Sudhof, T.C.3
  • 22
    • 0036241054 scopus 로고    scopus 로고
    • EphrinB phosphorylation and reverse signaling: Regulation by Src kinases and PTP-BL phosphatase
    • Palmer, A. et al. EphrinB phosphorylation and reverse signaling: regulation by Src kinases and PTP-BL phosphatase. Mol. Cell. 9, 725-737 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 725-737
    • Palmer, A.1
  • 23
    • 0035855819 scopus 로고    scopus 로고
    • The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals
    • Cowan, C.A. & Henkemeyer, M. The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals. Nature 413, 174-179 (2001).
    • (2001) Nature , vol.413 , pp. 174-179
    • Cowan, C.A.1    Henkemeyer, M.2
  • 24
    • 0029851690 scopus 로고    scopus 로고
    • Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands
    • Holland, S.J. et al. Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands. Nature 383, 722-725 (1996).
    • (1996) Nature , vol.383 , pp. 722-725
    • Holland, S.J.1
  • 25
    • 0030891962 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of transmembrane ligands for Eph receptors
    • Brückner, K., Pasquale, E.B. & Klein, R. Tyrosine phosphorylation of transmembrane ligands for Eph receptors. Science 275, 1640-1643 (1997).
    • (1997) Science , vol.275 , pp. 1640-1643
    • Brückner, K.1    Pasquale, E.B.2    Klein, R.3
  • 26
    • 0034598921 scopus 로고    scopus 로고
    • Axonal remodeling and synaptic differentiation in the cerebellum is regulated by WNT-7a signaling
    • Hall, A.C., Lucas, F.R. & Salinas, P.C. Axonal remodeling and synaptic differentiation in the cerebellum is regulated by WNT-7a signaling. Cell 100, 525-535 (2000).
    • (2000) Cell , vol.100 , pp. 525-535
    • Hall, A.C.1    Lucas, F.R.2    Salinas, P.C.3
  • 27
    • 0033166657 scopus 로고    scopus 로고
    • The diversity of cadherins and implications for a synaptic adhesive code in the CNS
    • Shapiro, L. & Colman, D.R. The diversity of cadherins and implications for a synaptic adhesive code in the CNS. Neuron 23, 427-430 (1999).
    • (1999) Neuron , vol.23 , pp. 427-430
    • Shapiro, L.1    Colman, D.R.2
  • 28
    • 0032568797 scopus 로고    scopus 로고
    • The cadherin superfamily at the synapse: More members, more missions
    • Uemura, T. The cadherin superfamily at the synapse: more members, more missions. Cell 93, 1095-1098 (1998).
    • (1998) Cell , vol.93 , pp. 1095-1098
    • Uemura, T.1
  • 29
    • 0026554563 scopus 로고
    • Modulation of an NCAM-related adhesion molecule with longterm synaptic plasticity in Aplysia
    • Mayford, M. et al. Modulation of an NCAM-related adhesion molecule with longterm synaptic plasticity in Aplysia. Science 256, 638-644 (1992).
    • (1992) Science , vol.256 , pp. 638-644
    • Mayford, M.1
  • 30
    • 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
  • 31
    • 0037031592 scopus 로고    scopus 로고
    • Sidekicks. Synaptic adhesion molecules that promote lamina-specific connectivity in the retina
    • Yamagata, M., Weiner, J. & Sanes, J. 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.2    Sanes, J.3
  • 32
    • 0033635736 scopus 로고    scopus 로고
    • EphB receptors interact with NMDA receptors and regulate excitatory synapse formation
    • Dalva, M.B. et al. EphB receptors interact with NMDA receptors and regulate excitatory synapse formation. Cell 103, 945-956 (2000).
    • (2000) Cell , vol.103 , pp. 945-956
    • Dalva, M.B.1
  • 33
    • 0021952476 scopus 로고
    • Neuronal regulation of astroglial morphology and proliferation in vitro
    • Hatten, M.E. Neuronal regulation of astroglial morphology and proliferation in vitro. J. Cell Biol. 100, 384-396 (1985).
    • (1985) J. Cell Biol. , vol.100 , pp. 384-396
    • Hatten, M.E.1
  • 34
    • 0032031705 scopus 로고    scopus 로고
    • Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses
    • Stein, E. et al. Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses. Genes Dev. 12, 667-678 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 667-678
    • Stein, E.1
  • 35
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J.D. et al. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1
  • 36
    • 0031307019 scopus 로고    scopus 로고
    • Evaluation of comparative protein structure modeling by MODELLER-3
    • Sanchez, R. & Sali, A. Evaluation of comparative protein structure modeling by MODELLER-3. Proteins 1 (Suppl.), 50-58 (1997).
    • (1997) Proteins , vol.1 , Issue.SUPPL. , pp. 50-58
    • Sanchez, R.1    Sali, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.