메뉴 건너뛰기




Volumn 109, Issue 47, 2012, Pages 19432-19437

Dimerization of postsynaptic neuroligin drives synaptic assembly via transsynaptic clustering of neurexin

Author keywords

Development; Electrophysiology; Hippocampus; Synaptic adhesion molecule

Indexed keywords

NEUREXIN; NEUROLIGIN;

EID: 84869779549     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1217633109     Document Type: Article
Times cited : (52)

References (34)
  • 1
    • 54049091941 scopus 로고    scopus 로고
    • Neuroligins and neurexins link synaptic function to cognitive disease
    • Südhof TC (2008) Neuroligins and neurexins link synaptic function to cognitive disease. Nature 455(7215):903-911.
    • (2008) Nature , vol.455 , Issue.7215 , pp. 903-911
    • Südhof, T.C.1
  • 2
    • 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(1):43-52.
    • (2007) Curr Opin Neurobiol , vol.17 , Issue.1 , pp. 43-52
    • Craig, A.M.1    Kang, Y.2
  • 3
    • 0346121341 scopus 로고    scopus 로고
    • Functional excitatory synapses in HEK293 cells expressing neuroligin and glutamate receptors
    • Fu Z, Washbourne P, Ortinski P, Vicini S (2003) Functional excitatory synapses in HEK293 cells expressing neuroligin and glutamate receptors. J Neurophysiol 90(6): 3950-3957.
    • (2003) J Neurophysiol , vol.90 , Issue.6 , pp. 3950-3957
    • Fu, Z.1    Washbourne, P.2    Ortinski, P.3    Vicini, S.4
  • 4
    • 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(7): 1013-1026.
    • (2004) Cell , vol.119 , Issue.7 , pp. 1013-1026
    • Graf, E.R.1    Zhang, X.2    Jin, S.X.3    Linhoff, M.W.4    Craig, A.M.5
  • 5
    • 33748531328 scopus 로고    scopus 로고
    • Neuroligins determine synapse maturation and function
    • Varoqueaux F, et al. (2006) Neuroligins determine synapse maturation and function. Neuron 51(6):741-754.
    • (2006) Neuron , vol.51 , Issue.6 , pp. 741-754
    • Varoqueaux, F.1
  • 6
    • 72149130256 scopus 로고    scopus 로고
    • LRRTM2 functions as a neurexin ligand in promoting excitatory synapse formation
    • Ko J, Fuccillo MV, Malenka RC, Südhof TC (2009) LRRTM2 functions as a neurexin ligand in promoting excitatory synapse formation. Neuron 64(6):791-798.
    • (2009) Neuron , vol.64 , Issue.6 , pp. 791-798
    • Ko, J.1    Fuccillo, M.V.2    Malenka, R.C.3    Südhof, T.C.4
  • 7
    • 61549142067 scopus 로고    scopus 로고
    • An unbiased expression screen for synaptogenic proteins identifies the LRRTM protein family as synaptic organizers
    • Linhoff MW, et al. (2009) An unbiased expression screen for synaptogenic proteins identifies the LRRTM protein family as synaptic organizers. Neuron 61(5):734-749.
    • (2009) Neuron , vol.61 , Issue.5 , pp. 734-749
    • Linhoff, M.W.1
  • 8
    • 72449202226 scopus 로고    scopus 로고
    • LRRTM2 interacts with Neurexin1 and regulates excitatory synapse formation
    • de Wit J, et al. (2009) LRRTM2 interacts with Neurexin1 and regulates excitatory synapse formation. Neuron 64(6):799-806.
    • (2009) Neuron , vol.64 , Issue.6 , pp. 799-806
    • De Wit, J.1
  • 9
    • 77953725365 scopus 로고    scopus 로고
    • Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
    • Uemura T, et al. (2010) Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum. Cell 141(6):1068-1079.
    • (2010) Cell , vol.141 , Issue.6 , pp. 1068-1079
    • Uemura, T.1
  • 10
    • 37049027105 scopus 로고    scopus 로고
    • Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions
    • Araç D, et al. (2007) Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions. Neuron 56(6): 992-1003.
    • (2007) Neuron , vol.56 , Issue.6 , pp. 992-1003
    • Araç, D.1
  • 11
    • 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(6): 979-991.
    • (2007) Neuron , vol.56 , Issue.6 , pp. 979-991
    • Fabrichny, I.P.1
  • 12
    • 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(6):693-705.
    • (2007) Structure , vol.15 , Issue.6 , pp. 693-705
    • Comoletti, D.1
  • 13
    • 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(7):708-716.
    • (2003) Nat Neurosci , vol.6 , Issue.7 , pp. 708-716
    • Dean, C.1
  • 14
    • 70350336261 scopus 로고    scopus 로고
    • Neuroligin-1 performs neurexin-dependent and neurexin-independent functions in synapse validation
    • Ko J, et al. (2009) Neuroligin-1 performs neurexin-dependent and neurexin-independent functions in synapse validation. EMBO J 28(20):3244-3255.
    • (2009) EMBO J , vol.28 , Issue.20 , pp. 3244-3255
    • Ko, J.1
  • 15
    • 34250211762 scopus 로고    scopus 로고
    • Activity-dependent validation of excitatory versus inhibitory synapses by neuroligin-1 versus neuroligin-2
    • Chubykin AA, et al. (2007) Activity-dependent validation of excitatory versus inhibitory synapses by neuroligin-1 versus neuroligin-2. Neuron 54(6):919-931.
    • (2007) Neuron , vol.54 , Issue.6 , pp. 919-931
    • Chubykin, A.A.1
  • 16
    • 33846564563 scopus 로고    scopus 로고
    • Retrograde modulation of presynaptic release probability through signaling mediated by PSD-95-neuroligin
    • Futai K, et al. (2007) Retrograde modulation of presynaptic release probability through signaling mediated by PSD-95-neuroligin. Nat Neurosci 10(2):186-195.
    • (2007) Nat Neurosci , vol.10 , Issue.2 , pp. 186-195
    • Futai, K.1
  • 17
    • 84865154636 scopus 로고    scopus 로고
    • Homodimerization and isoform-specific heterodimerization of neuroligins
    • Poulopoulos A, et al. (2012) Homodimerization and isoform-specific heterodimerization of neuroligins. Biochem J 446(2):321-330.
    • (2012) Biochem J , vol.446 , Issue.2 , pp. 321-330
    • Poulopoulos, A.1
  • 18
    • 13544269142 scopus 로고    scopus 로고
    • Control of excitatory and inhibitory synapse formation by neuroligins
    • Chih B, Engelman H, Scheiffele P (2005) Control of excitatory and inhibitory synapse formation by neuroligins. Science 307(5713):1324-1328.
    • (2005) Science , vol.307 , Issue.5713 , pp. 1324-1328
    • Chih, B.1    Engelman, H.2    Scheiffele, P.3
  • 19
    • 48249156612 scopus 로고    scopus 로고
    • Neuroligin-1 is required for normal expression of LTP and associative fear memory in the amygdala of adult animals
    • Kim J, et al. (2008) Neuroligin-1 is required for normal expression of LTP and associative fear memory in the amygdala of adult animals. Proc Natl Acad Sci USA 105(26): 9087-9092.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.26 , pp. 9087-9092
    • Kim, J.1
  • 20
    • 4644353516 scopus 로고    scopus 로고
    • A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin
    • Prange O, Wong TP, Gerrow K, Wang YT, El-Husseini A (2004) A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin. Proc Natl Acad Sci USA 101(38):13915-13920.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.38 , pp. 13915-13920
    • Prange, O.1    Wong, T.P.2    Gerrow, K.3    Wang, Y.T.4    El-Husseini, A.5
  • 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 JN, et al. (2005) Neuroligins mediate excitatory and inhibitory synapse formation: Involvement of PSD-95 and neurexin-1beta in neuroligin-induced synaptic specificity. J Biol Chem 280(17):17312-17319.
    • (2005) J Biol Chem , vol.280 , Issue.17 , pp. 17312-17319
    • Levinson, J.N.1
  • 22
    • 26944444692 scopus 로고    scopus 로고
    • A splice code for trans-synaptic cell adhesion mediated by binding of neuroligin 1 to alpha- And betaneurexins
    • Boucard AA, Chubykin AA, Comoletti D, Taylor P, Südhof TC (2005) A splice code for trans-synaptic cell adhesion mediated by binding of neuroligin 1 to alpha- and betaneurexins. Neuron 48(2):229-236.
    • (2005) Neuron , vol.48 , Issue.2 , pp. 229-236
    • Boucard, A.A.1    Chubykin, A.A.2    Comoletti, D.3    Taylor, P.4    Südhof, T.C.5
  • 23
    • 0027756895 scopus 로고
    • Controlling signal transduction with synthetic ligands
    • Spencer DM, Wandless TJ, Schreiber SL, Crabtree GR (1993) Controlling signal transduction with synthetic ligands. Science 262(5136):1019-1024.
    • (1993) Science , vol.262 , Issue.5136 , pp. 1019-1024
    • Spencer, D.M.1    Wandless, T.J.2    Schreiber, S.L.3    Crabtree, G.R.4
  • 24
    • 13144276290 scopus 로고    scopus 로고
    • Redesigning an FKBP-ligand interface to generate chemical dimerizers with novel specificity
    • Clackson T, et al. (1998) Redesigning an FKBP-ligand interface to generate chemical dimerizers with novel specificity. Proc Natl Acad Sci USA 95(18):10437-10442.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.18 , pp. 10437-10442
    • Clackson, T.1
  • 25
    • 79960834029 scopus 로고    scopus 로고
    • Functional dependence of neuroligin on a new non-PDZ intracellular domain
    • Shipman SL, et al. (2011) Functional dependence of neuroligin on a new non-PDZ intracellular domain. Nat Neurosci 14(6):718-726.
    • (2011) Nat Neurosci , vol.14 , Issue.6 , pp. 718-726
    • Shipman, S.L.1
  • 26
    • 84864301573 scopus 로고    scopus 로고
    • Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin
    • Tanaka H, et al. (2012) Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin. Cell Rep 2(1): 101-110.
    • (2012) Cell Rep , vol.2 , Issue.1 , pp. 101-110
    • Tanaka, H.1
  • 27
    • 84862005664 scopus 로고    scopus 로고
    • Transcellular neuroligin-2 interactions enhance insulin secretion and are integral to pancreatic â cell function
    • Suckow AT, et al. (2012) Transcellular neuroligin-2 interactions enhance insulin secretion and are integral to pancreatic â cell function. J Biol Chem 287(24): 19816-19826.
    • (2012) J Biol Chem , vol.287 , Issue.24 , pp. 19816-19826
    • Suckow, A.T.1
  • 28
    • 84858597379 scopus 로고    scopus 로고
    • High affinity neurexin binding to cell adhesion G-protein- Coupled receptor CIRL1/latrophilin-1 produces an intercellular adhesion complex
    • Boucard AA, Ko J, Südhof TC (2012) High affinity neurexin binding to cell adhesion G-protein- coupled receptor CIRL1/latrophilin-1 produces an intercellular adhesion complex. J Biol Chem 287(12):9399-9413.
    • (2012) J Biol Chem , vol.287 , Issue.12 , pp. 9399-9413
    • Boucard, A.A.1    Ko, J.2    Südhof, T.C.3
  • 29
    • 50549097328 scopus 로고    scopus 로고
    • Cadherins and catenins at synapses: Roles in synaptogenesis and synaptic plasticity
    • Arikkath J, Reichardt LF (2008) Cadherins and catenins at synapses: Roles in synaptogenesis and synaptic plasticity. Trends Neurosci 31(9):487-494.
    • (2008) Trends Neurosci , vol.31 , Issue.9 , pp. 487-494
    • Arikkath, J.1    Reichardt, L.F.2
  • 30
    • 0037200037 scopus 로고    scopus 로고
    • SynCAM, a synaptic adhesion molecule that drives synapse assembly
    • Biederer T, et al. (2002) SynCAM, a synaptic adhesion molecule that drives synapse assembly. Science 297(5586):1525-1531.
    • (2002) Science , vol.297 , Issue.5586 , pp. 1525-1531
    • Biederer, T.1
  • 31
    • 77951577057 scopus 로고    scopus 로고
    • Trans-synaptic adhesions between netrin-G ligand-3 (NGL-3) and receptor tyrosine phosphatases LAR, protein-tyrosine phosphatase delta (PTPdelta), and PTPsigma via specific domains regulate excitatory synapse formation
    • Kwon SK, Woo J, Kim SY, Kim H, Kim E (2010) Trans-synaptic adhesions between netrin-G ligand-3 (NGL-3) and receptor tyrosine phosphatases LAR, protein-tyrosine phosphatase delta (PTPdelta), and PTPsigma via specific domains regulate excitatory synapse formation. J Biol Chem 285(18):13966-13978.
    • (2010) J Biol Chem , vol.285 , Issue.18 , pp. 13966-13978
    • Kwon, S.K.1    Woo, J.2    Kim, S.Y.3    Kim, H.4    Kim, E.5
  • 32
    • 63649101646 scopus 로고    scopus 로고
    • Trans-synaptic adhesion between NGL-3 and LAR regulates the formation of excitatory synapses
    • Woo J, et al. (2009) Trans-synaptic adhesion between NGL-3 and LAR regulates the formation of excitatory synapses. Nat Neurosci 12(4):428-437.
    • (2009) Nat Neurosci , vol.12 , Issue.4 , pp. 428-437
    • Woo, J.1
  • 33
    • 84859579185 scopus 로고    scopus 로고
    • Trans-synaptic Teneurin signalling in neuromuscular synapse organization and target choice
    • Mosca TJ, Hong W, Dani VS, Favaloro V, Luo L (2012) Trans-synaptic Teneurin signalling in neuromuscular synapse organization and target choice. Nature 484(7393): 237-241.
    • (2012) Nature , vol.484 , Issue.7393 , pp. 237-241
    • Mosca, T.J.1    Hong, W.2    Dani, V.S.3    Favaloro, V.4    Luo, L.5
  • 34
    • 0025805120 scopus 로고
    • A simple method for organotypic cultures of nervous tissue
    • Stoppini L, Buchs PA, Muller D (1991) A simple method for organotypic cultures of nervous tissue. J Neurosci Methods 37(2):173-182.
    • (1991) J Neurosci Methods , vol.37 , Issue.2 , pp. 173-182
    • Stoppini, L.1    Buchs, P.A.2    Muller, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.