메뉴 건너뛰기




Volumn 105, Issue 39, 2008, Pages 15124-15129

Mutational analysis of the neurexin/neuroligin complex reveals essential and regulatory components

Author keywords

Calcium; Cell adhesion; LNS domain; Neurotransmission; Synaptogenesis

Indexed keywords

ASPARTIC ACID; CALCIUM; NEUREXIN; NEUROLIGIN; NEU DIFFERENTIATION FACTOR; NEUROTOXIN;

EID: 54449086786     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0801639105     Document Type: Article
Times cited : (79)

References (45)
  • 1
    • 33846867244 scopus 로고    scopus 로고
    • Neurexin-neuroligin signaling in synapse development
    • Craig AM, Kang Y (2007) Neurexin-neuroligin signaling in synapse development. Curr Opin Neurobiol 17:43-52.
    • (2007) Curr Opin Neurobiol , vol.17 , pp. 43-52
    • Craig, A.M.1    Kang, Y.2
  • 3
    • 0037774700 scopus 로고    scopus 로고
    • Alpha-neurexins couple Ca2+ channels to synaptic vesicle exocytosis
    • Missler M, et al. (2003) Alpha-neurexins couple Ca2+ channels to synaptic vesicle exocytosis. Nature 423:939-948.
    • (2003) Nature , vol.423 , pp. 939-948
    • Missler, M.1
  • 4
    • 33748531328 scopus 로고    scopus 로고
    • Neuroligins determine synapse maturation and function
    • Varoqueaux F, et al. (2006) Neuroligins determine synapse maturation and function. Neuron 51:741-754.
    • (2006) Neuron , vol.51 , pp. 741-754
    • Varoqueaux, F.1
  • 5
    • 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 (2000) Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons. Cell 101:657-669.
    • (2000) Cell , vol.101 , pp. 657-669
    • Scheiffele, P.1    Fan, J.2    Choih, J.3    Fetter, R.4    Serafini, T.5
  • 6
    • 11144352245 scopus 로고    scopus 로고
    • Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins
    • Graf ER, Zhang X, Jin SX, Linhoff MW, Craig AM (2004) Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins. Cell 119:1013-1026.
    • (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
  • 7
    • 0037656313 scopus 로고    scopus 로고
    • Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are associated with autism
    • Jamain S, et al. (2003) Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are associated with autism. Nat Genet 34:27-29.
    • (2003) Nat Genet , vol.34 , pp. 27-29
    • Jamain, S.1
  • 8
    • 33847327313 scopus 로고    scopus 로고
    • Mapping autism risk loci using genetic linkage and chromosomal rearrangements
    • Szatmari P, et al. (2007) Mapping autism risk loci using genetic linkage and chromosomal rearrangements. Nat Genet 39:319-328.
    • (2007) Nat Genet , vol.39 , pp. 319-328
    • Szatmari, P.1
  • 9
    • 0031983653 scopus 로고    scopus 로고
    • Neurexins: Three genes and 1001 products
    • Missler M, Südhof TC (1998) Neurexins: Three genes and 1001 products. Trends Genet 14:20-26.
    • (1998) Trends Genet , vol.14 , pp. 20-26
    • Missler, M.1    Südhof, T.C.2
  • 10
    • 18244407522 scopus 로고    scopus 로고
    • Extracellular domains of alpha-neurexins participate in regulating synaptic transmission by selectively affecting N- and P/Q-type Ca2+ channels
    • Zhang W, et al. (2005) Extracellular domains of alpha-neurexins participate in regulating synaptic transmission by selectively affecting N- and P/Q-type Ca2+ channels. J Neurosci 25:4330-4342.
    • (2005) J Neurosci , vol.25 , pp. 4330-4342
    • Zhang, W.1
  • 11
    • 0032567532 scopus 로고    scopus 로고
    • Neurexophilin binding to alpha-neurexins. A single LNS domain functions as an independently folding ligand-binding unit
    • Missler M, Hammer RE, Sudhof TC (1998) Neurexophilin binding to alpha-neurexins. A single LNS domain functions as an independently folding ligand-binding unit. J Biol Chem 273:34716-34723.
    • (1998) J Biol Chem , vol.273 , pp. 34716-34723
    • Missler, M.1    Hammer, R.E.2    Sudhof, T.C.3
  • 12
    • 0029036374 scopus 로고
    • Neuroligin 1: A splice site-specific ligand for beta-neurexins
    • Ichtchenko K, et al. (1995) Neuroligin 1: A splice site-specific ligand for beta-neurexins. Cell 81:435-443.
    • (1995) Cell , vol.81 , pp. 435-443
    • Ichtchenko, K.1
  • 13
    • 1842328567 scopus 로고    scopus 로고
    • Binding properties of neuroligin 1 and neurexin 1beta reveal function as heterophilic cell adhesion molecules
    • Nguyen T, Sudhof TC (1997) Binding properties of neuroligin 1 and neurexin 1beta reveal function as heterophilic cell adhesion molecules. J Biol Chem 272:26032-26039.
    • (1997) J Biol Chem , vol.272 , pp. 26032-26039
    • Nguyen, T.1    Sudhof, T.C.2
  • 14
    • 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 AA, Chubykin AA, Comoletti D, Taylor P, Sudhof TC (2005) A splice code for trans-synaptic cell adhesion mediated by binding of neuroligin 1 to alpha- and beta-neurexins. Neuron 48:229-236.
    • (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
  • 15
    • 37849021314 scopus 로고    scopus 로고
    • Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions
    • Chen X, Liu H, Shim AH, Focia PJ, He X (2008) Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions. Nat Struct Mol Biol 15:50-56.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 50-56
    • Chen, X.1    Liu, H.2    Shim, A.H.3    Focia, P.J.4    He, X.5
  • 16
    • 37049027105 scopus 로고    scopus 로고
    • Structures of neuroligin-1 and the neuroligin-1/neurexin-1beta complex reveal specific protein-protein and protein-Ca(2+) interactions
    • Arac D, et al. (2007) Structures of neuroligin-1 and the neuroligin-1/neurexin-1beta complex reveal specific protein-protein and protein-Ca(2+) interactions. Neuron 56:992-1003.
    • (2007) Neuron , vol.56 , pp. 992-1003
    • Arac, D.1
  • 17
    • 37049028145 scopus 로고    scopus 로고
    • Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: Determinants for folding and cell adhesion
    • Fabrichny IP, et al. (2007) Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: Determinants for folding and cell adhesion. Neuron 56:979-991.
    • (2007) Neuron , vol.56 , pp. 979-991
    • Fabrichny, I.P.1
  • 18
    • 0026769035 scopus 로고
    • Neurexins: Synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin
    • Ushkaryov YA, Petrenko AG, Geppert M, Sudhof TC (1992) Neurexins: Synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin. Science 257:50-56.
    • (1992) Science , vol.257 , pp. 50-56
    • Ushkaryov, Y.A.1    Petrenko, A.G.2    Geppert, M.3    Sudhof, T.C.4
  • 19
    • 34249902781 scopus 로고    scopus 로고
    • Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by x-ray and neutron scattering
    • Comoletti D, et al. (2007) Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by x-ray and neutron scattering. Structure 15:693-705.
    • (2007) Structure , vol.15 , pp. 693-705
    • Comoletti, D.1
  • 20
    • 0035369647 scopus 로고    scopus 로고
    • LG/LNS domains: Multiple functions - one business end?
    • Rudenko G, Hohenester E, Muller YA (2001) LG/LNS domains: Multiple functions - one business end? Trends Biochem Sci 26:363-368.
    • (2001) Trends Biochem Sci , vol.26 , pp. 363-368
    • Rudenko, G.1    Hohenester, E.2    Muller, Y.A.3
  • 21
    • 33747349745 scopus 로고    scopus 로고
    • Crystal structure of the second LNS/LG domain from neurexin 1alpha: Ca2+ binding and the effects of alternative splicing
    • Sheckler LR, Henry L, Sugita S, Sudhof TC, Rudenko G (2006) Crystal structure of the second LNS/LG domain from neurexin 1alpha: Ca2+ binding and the effects of alternative splicing. J Biol Chem 281:22896-22905.
    • (2006) J Biol Chem , vol.281 , pp. 22896-22905
    • Sheckler, L.R.1    Henry, L.2    Sugita, S.3    Sudhof, T.C.4    Rudenko, G.5
  • 22
    • 38349098974 scopus 로고    scopus 로고
    • Induction of GABAergic postsynaptic differentiation by alpha-neurexins
    • Kang Y, Zhang X, Dobie F, Wu H, Craig AM (2008) Induction of GABAergic postsynaptic differentiation by alpha-neurexins. J Biol Chem 283:2323-2334.
    • (2008) J Biol Chem , vol.283 , pp. 2323-2334
    • Kang, Y.1    Zhang, X.2    Dobie, F.3    Wu, H.4    Craig, A.M.5
  • 23
    • 33646761687 scopus 로고    scopus 로고
    • Structural basis for diversity of the EF-hand calcium-binding proteins
    • Grabarek Z (2006) Structural basis for diversity of the EF-hand calcium-binding proteins. J Mol Biol 359:509-525.
    • (2006) J Mol Biol , vol.359 , pp. 509-525
    • Grabarek, Z.1
  • 25
    • 0028982166 scopus 로고
    • The structure of a Ca(2+)-binding epidermal growth factor-like domain: Its role in protein-protein interactions
    • Rao Z, et al. (1995) The structure of a Ca(2+)-binding epidermal growth factor-like domain: Its role in protein-protein interactions. Cell 82:131-141.
    • (1995) Cell , vol.82 , pp. 131-141
    • Rao, Z.1
  • 26
    • 0033231551 scopus 로고    scopus 로고
    • The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin
    • Hohenester E, Tisi D, Talts JF, Timpl R (1999) The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin. Mol Cell 4:783-792.
    • (1999) Mol Cell , vol.4 , pp. 783-792
    • Hohenester, E.1    Tisi, D.2    Talts, J.F.3    Timpl, R.4
  • 27
    • 33646464124 scopus 로고    scopus 로고
    • Structure function and splice site analysis of the synaptogenic activity of the neurexin-1 beta LNS domain
    • Graf ER, Kang Y, Hauner AM, Craig AM (2006) Structure function and splice site analysis of the synaptogenic activity of the neurexin-1 beta LNS domain. J Neurosci 26:4256-4265.
    • (2006) J Neurosci , vol.26 , pp. 4256-4265
    • Graf, E.R.1    Kang, Y.2    Hauner, A.M.3    Craig, A.M.4
  • 28
    • 33750348559 scopus 로고    scopus 로고
    • Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins
    • Comoletti D, et al. (2006) Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins. Biochemistry 45:12816-12827.
    • (2006) Biochemistry , vol.45 , pp. 12816-12827
    • Comoletti, D.1
  • 29
    • 18644386251 scopus 로고    scopus 로고
    • Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
    • Ogiso H, et al. (2002) Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell 110:775-787.
    • (2002) Cell , vol.110 , pp. 775-787
    • Ogiso, H.1
  • 30
    • 0033960385 scopus 로고    scopus 로고
    • Common EF-hand motifs in cholinesterases and neuroligins suggest a role for Ca2+ binding in cell surface associations
    • Tsigelny I, Shindyalov IN, Bourne PE, Sudhof TC, Taylor P (2000) Common EF-hand motifs in cholinesterases and neuroligins suggest a role for Ca2+ binding in cell surface associations. Protein Sci 9:180-185.
    • (2000) Protein Sci , vol.9 , pp. 180-185
    • Tsigelny, I.1    Shindyalov, I.N.2    Bourne, P.E.3    Sudhof, T.C.4    Taylor, P.5
  • 31
    • 41149087217 scopus 로고    scopus 로고
    • Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2
    • Koehnke J, et al. (2008) Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2. Proc Natl Acad Sci USA 105:1873-1878.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1873-1878
    • Koehnke, J.1
  • 32
    • 30444433575 scopus 로고    scopus 로고
    • Structural basis for Gas6-Axl signalling
    • Sasaki T, et al. (2006) Structural basis for Gas6-Axl signalling. EMBO J 25:80-87.
    • (2006) EMBO J , vol.25 , pp. 80-87
    • Sasaki, T.1
  • 33
    • 0034651691 scopus 로고    scopus 로고
    • Crystal structure ofhumansex hormone-binding globulin: Steroid transport by a laminin G-like domain
    • Grishkovskaya I, et al. (2000) Crystal structure ofhumansex hormone-binding globulin: Steroid transport by a laminin G-like domain. EMBO J 19:504-512.
    • (2000) EMBO J , vol.19 , pp. 504-512
    • Grishkovskaya, I.1
  • 34
    • 34249729332 scopus 로고    scopus 로고
    • Crystal structure and cell surface anchorage sites of laminin alpha1LG4-5
    • Harrison D, et al. (2007) Crystal structure and cell surface anchorage sites of laminin alpha1LG4-5. J Biol Chem 282:11573-11581.
    • (2007) J Biol Chem , vol.282 , pp. 11573-11581
    • Harrison, D.1
  • 35
    • 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 TC, Deisenhofer J (1999) The structure of the ligand-binding domain of neurexin Ibeta: Regulation of LNS domain function by alternative splicing. Cell 99:93-101.
    • (1999) Cell , vol.99 , pp. 93-101
    • Rudenko, G.1    Nguyen, T.2    Chelliah, Y.3    Sudhof, T.C.4    Deisenhofer, J.5
  • 36
    • 34548154535 scopus 로고    scopus 로고
    • Crystal structure of the amino-terminal NC4 domain of collagen IX, a zinc binding member of the LNS domain family
    • Leppanen VM, et al. (2007) Crystal structure of the amino-terminal NC4 domain of collagen IX, a zinc binding member of the LNS domain family. J Biol Chem 282:23219-23230.
    • (2007) J Biol Chem , vol.282 , pp. 23219-23230
    • Leppanen, V.M.1
  • 37
    • 0028144369 scopus 로고
    • Structure of pentameric human serum amyloid P component
    • Emsley J, et al. (1994) Structure of pentameric human serum amyloid P component. Nature 367:338-345.
    • (1994) Nature , vol.367 , pp. 338-345
    • Emsley, J.1
  • 38
    • 0038607100 scopus 로고    scopus 로고
    • Calcium plays a critical role in determining the acetylcholine receptor-clustering activities of alternatively spliced isoforms of Agrin
    • Tseng CN, Zhang L, Cascio M, Wang ZZ (2003) Calcium plays a critical role in determining the acetylcholine receptor-clustering activities of alternatively spliced isoforms of Agrin. J Biol Chem 278:17236-17245.
    • (2003) J Biol Chem , vol.278 , pp. 17236-17245
    • Tseng, C.N.1    Zhang, L.2    Cascio, M.3    Wang, Z.Z.4
  • 39
    • 40049089434 scopus 로고    scopus 로고
    • Regulation of neurexin 1beta tertiary structure and ligand binding through alternative splicing
    • Shen KC, et al. (2008) Regulation of neurexin 1beta tertiary structure and ligand binding through alternative splicing. Structure 16:422-431.
    • (2008) Structure , vol.16 , pp. 422-431
    • Shen, K.C.1
  • 40
    • 40049083518 scopus 로고    scopus 로고
    • Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and dynamics of splice insertion sequence 4
    • Koehnke J, et al. (2008) Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and dynamics of splice insertion sequence 4. Structure 16:410-421.
    • (2008) Structure , vol.16 , pp. 410-421
    • Koehnke, J.1
  • 41
    • 20644443891 scopus 로고    scopus 로고
    • Dissection of synapse induction by neuroligins: Effect of a neuroligin mutation associated with autism
    • Chubykin AA, et al. (2005) Dissection of synapse induction by neuroligins: Effect of a neuroligin mutation associated with autism. J Biol Chem 280:22365-22374.
    • (2005) J Biol Chem , vol.280 , pp. 22365-22374
    • Chubykin, A.A.1
  • 42
    • 0037743572 scopus 로고    scopus 로고
    • Neurexin mediates the assembly of presynaptic terminals
    • Dean C, et al. (2003) Neurexin mediates the assembly of presynaptic terminals. Nat Neurosci 6:708-716.
    • (2003) Nat Neurosci , vol.6 , pp. 708-716
    • Dean, C.1
  • 43
    • 2442713977 scopus 로고    scopus 로고
    • The Arg451Cys-neuroligin-3 mutation associated with autism reveals a defect in protein processing
    • Comoletti D, et al. (2004) The Arg451Cys-neuroligin-3 mutation associated with autism reveals a defect in protein processing. J Neurosci 24:4889-4893.
    • (2004) J Neurosci , vol.24 , pp. 4889-4893
    • Comoletti, D.1
  • 44
    • 7244261850 scopus 로고    scopus 로고
    • Synaptic targeting of neuroligin is independent of neurexin and SAP90/PSD95 binding
    • Dresbach T, Neeb A, Meyer G, Gundelfinger ED, Brose N (2004) Synaptic targeting of neuroligin is independent of neurexin and SAP90/PSD95 binding. Mol Cell Neurosci 27:227-235.
    • (2004) Mol Cell Neurosci , vol.27 , pp. 227-235
    • Dresbach, T.1    Neeb, A.2    Meyer, G.3    Gundelfinger, E.D.4    Brose, N.5
  • 45
    • 0033514448 scopus 로고    scopus 로고
    • Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses
    • Song JY, Ichtchenko K, Sudhof TC, Brose N (1999) Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses. Proc Natl Acad Sci USA 96:1100-1105.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.