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Volumn 13, Issue 5, 2003, Pages 520-526

The roles of cadherins and nectins in interneuronal synapse formation

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CADHERIN; GUANINE NUCLEOTIDE BINDING PROTEIN; NECTIN; PROTEIN; PROTEIN CDC42; UNCLASSIFIED DRUG;

EID: 0242656305     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.conb.2003.09.003     Document Type: Review
Times cited : (64)

References (40)
  • 1
    • 0025894092 scopus 로고
    • Cadherin cell adhesion receptors as a morphogenetic regulator
    • Takeichi M. Cadherin cell adhesion receptors as a morphogenetic regulator. Science. 251:1991;1451-1455.
    • (1991) Science , vol.251 , pp. 1451-1455
    • Takeichi, M.1
  • 2
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner B.M. Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell. 84:1996;345-357.
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 3
    • 0037459077 scopus 로고    scopus 로고
    • Sticky business: Orchestrating cellular signals at adherens junctions
    • Perez-Moreno M., Jamora C., Fuchs E. Sticky business: orchestrating cellular signals at adherens junctions. Cell. 112:2003;535-548.
    • (2003) Cell , vol.112 , pp. 535-548
    • Perez-Moreno, M.1    Jamora, C.2    Fuchs, E.3
  • 4
    • 0033168966 scopus 로고    scopus 로고
    • Occludin and claudins in tight-junction strands: Leading or supporting players?
    • Tsukita S., Furuse M. Occludin and claudins in tight-junction strands: leading or supporting players? Trends Cell Biol. 9:1999;268-273.
    • (1999) Trends Cell Biol. , vol.9 , pp. 268-273
    • Tsukita, S.1    Furuse, M.2
  • 5
    • 0028810956 scopus 로고
    • Synaptic structure and function: Dynamic organization yields architectural precision
    • Burns M.E., Augustine G.J. Synaptic structure and function: dynamic organization yields architectural precision. Cell. 83:1995;187-194.
    • (1995) Cell , vol.83 , pp. 187-194
    • Burns, M.E.1    Augustine, G.J.2
  • 6
    • 0034657319 scopus 로고    scopus 로고
    • Cadherin superfamily genes: Functions, genomic organization, and neurologic diversity
    • Yagi T., Takeichi M. Cadherin superfamily genes: functions, genomic organization, and neurologic diversity. Genes Dev. 14:2000;1169-1180.
    • (2000) Genes Dev. , vol.14 , pp. 1169-1180
    • Yagi, T.1    Takeichi, M.2
  • 7
    • 0037232646 scopus 로고    scopus 로고
    • Nectin and afadin: Novel organizers of intercellular junctions
    • Takai Y., Nakanishi H. Nectin and afadin: novel organizers of intercellular junctions. J. Cell Sci. 116:2003;17-27.
    • (2003) J. Cell Sci. , vol.116 , pp. 17-27
    • Takai, Y.1    Nakanishi, H.2
  • 8
    • 0037184967 scopus 로고    scopus 로고
    • Trans-interactions of nectins induce formation of filopodia and lamellipodia through the respective activation of Cdc42 and Rac small G proteins
    • The authors show that the trans-interactions of nectins induce activation of Cdc42 and Rac in both epithelial cells and fibroblasts
    • Kawakatsu T., Shimizu K., Honda T., Fukuhara T., Hoshino T., Takai Y. Trans-interactions of nectins induce formation of filopodia and lamellipodia through the respective activation of Cdc42 and Rac small G proteins. J. Biol. Chem. 277:2002;50749-50755 The authors show that the trans-interactions of nectins induce activation of Cdc42 and Rac in both epithelial cells and fibroblasts.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50749-50755
    • Kawakatsu, T.1    Shimizu, K.2    Honda, T.3    Fukuhara, T.4    Hoshino, T.5    Takai, Y.6
  • 9
    • 0037689074 scopus 로고    scopus 로고
    • Cdc42 and Rac small G proteins activated by trans-interactions of nectins are involved in activation of c-Jun N-terminal kinase, but not in association of nectins and cadherin to form adherens junctions, in fibroblasts
    • The authors show that the activation of Cdc42 and Rac by the trans-interactions of nectins induces activation of c-Jun amino-terminal kinase (JNK) in a phosphatidylinositol-3 (PI3) kinase-independent manner. It is suggested that the formation of the nectin-based cell-cell adhesion leads to regulation of gene expression through the activation of JNK
    • Honda T., Shimizu K., Kawakatsu T., Fukuhara A., Irie K., Nakamura T., Matsuda M., Takai Y. Cdc42 and Rac small G proteins activated by trans-interactions of nectins are involved in activation of c-Jun N-terminal kinase, but not in association of nectins and cadherin to form adherens junctions, in fibroblasts. Genes Cells. 8:2003;481-491 The authors show that the activation of Cdc42 and Rac by the trans-interactions of nectins induces activation of c-Jun amino-terminal kinase (JNK) in a phosphatidylinositol-3 (PI3) kinase-independent manner. It is suggested that the formation of the nectin-based cell-cell adhesion leads to regulation of gene expression through the activation of JNK.
    • (2003) Genes Cells , vol.8 , pp. 481-491
    • Honda, T.1    Shimizu, K.2    Kawakatsu, T.3    Fukuhara, A.4    Irie, K.5    Nakamura, T.6    Matsuda, M.7    Takai, Y.8
  • 10
    • 0037458707 scopus 로고    scopus 로고
    • Direct binding of cell polarity protein PAR-3 to cell-cell adhesion molecule nectin at neuroepithelial cells of developing mouse
    • The authors show that PAR-3 directly binds to nectin-1 and -3. It is suggested that nectin-1 and -3 are involved in cell polarization through PAR-3.
    • Takekuni K., Ikeda W., Fujito T., Morimoto K., Takeuchi M., Monden M., Takai Y. Direct binding of cell polarity protein PAR-3 to cell-cell adhesion molecule nectin at neuroepithelial cells of developing mouse. J. Biol. Chem. 278:2003;5497-5500 The authors show that PAR-3 directly binds to nectin-1 and -3. It is suggested that nectin-1 and -3 are involved in cell polarization through PAR-3.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5497-5500
    • Takekuni, K.1    Ikeda, W.2    Fujito, T.3    Morimoto, K.4    Takeuchi, M.5    Monden, M.6    Takai, Y.7
  • 11
    • 0035479930 scopus 로고    scopus 로고
    • Intercellular junctions and cellular polarity: The PAR-aPKC complex, a conserved core cassette playing fundamental roles in cell polarity
    • Ohno S. Intercellular junctions and cellular polarity: the PAR-aPKC complex, a conserved core cassette playing fundamental roles in cell polarity. Curr. Opin. Cell Biol. 13:2001;641-648.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 641-648
    • Ohno, S.1
  • 12
    • 0034614941 scopus 로고    scopus 로고
    • Regulation of cadherin adhesive activity
    • Gumbiner B.M. Regulation of cadherin adhesive activity. J. Cell Biol. 148:2000;399-404.
    • (2000) J. Cell Biol. , vol.148 , pp. 399-404
    • Gumbiner, B.M.1
  • 13
    • 0034994490 scopus 로고    scopus 로고
    • Recruitment and activation of Rac1 by the formation of E-cadherin-mediated cell-cell adhesion sites
    • Nakagawa M., Fukata M., Yamaga M., Itoh N., Kaibuchi K. Recruitment and activation of Rac1 by the formation of E-cadherin-mediated cell-cell adhesion sites. J. Cell Sci. 114:2001;1829-1838.
    • (2001) J. Cell Sci. , vol.114 , pp. 1829-1838
    • Nakagawa, M.1    Fukata, M.2    Yamaga, M.3    Itoh, N.4    Kaibuchi, K.5
  • 15
    • 0030245731 scopus 로고    scopus 로고
    • A model for central synaptic junctional complex formation based on the differential adhesive specificities of the cadherins
    • Fannon A.M., Colman D.R. A model for central synaptic junctional complex formation based on the differential adhesive specificities of the cadherins. Neuron. 17:1996;423-434.
    • (1996) Neuron , vol.17 , pp. 423-434
    • Fannon, A.M.1    Colman, D.R.2
  • 16
    • 0029807018 scopus 로고    scopus 로고
    • The catenin/cadherin adhesion system is localized in synaptic junctions bordering transmitter release zones
    • Uchida N., Honjo Y., Johnson K.R., Wheelock M.J., Takeichi M. The catenin/cadherin adhesion system is localized in synaptic junctions bordering transmitter release zones. J. Cell Biol. 135:1996;767-779.
    • (1996) J. Cell Biol. , vol.135 , pp. 767-779
    • Uchida, N.1    Honjo, Y.2    Johnson, K.R.3    Wheelock, M.J.4    Takeichi, M.5
  • 17
    • 0037017401 scopus 로고    scopus 로고
    • Nectin: An adhesion molecule involved in formation of synapses
    • The authors demonstrate that the nectin-afadin system plays an important role in the formation of synapses in cooperation with the cadherin-catenin system.
    • Mizoguchi A., Nakanishi H., Kimura K., Matsubara K., Ozaki-Kuroda K., Katata T., Honda T., Kiyohara Y., Heo K., Higashi M., et al. Nectin: an adhesion molecule involved in formation of synapses. J. Cell Biol. 156:2002;555-565 The authors demonstrate that the nectin-afadin system plays an important role in the formation of synapses in cooperation with the cadherin-catenin system.
    • (2002) J. Cell Biol. , vol.156 , pp. 555-565
    • Mizoguchi, A.1    Nakanishi, H.2    Kimura, K.3    Matsubara, K.4    Ozaki-Kuroda, K.5    Katata, T.6    Honda, T.7    Kiyohara, Y.8    Heo, K.9    Higashi, M.10
  • 18
    • 0034698975 scopus 로고    scopus 로고
    • Localization of l-afadin at puncta adhaerentia-like junctions between the mossy fiber terminals and the dendritic trunks of pyramidal cells in the adult mouse hippocampus
    • Nishioka H., Mizoguchi A., Nakanishi H., Mandai K., Takahashi K., Kimura K., Satoh-Moriya A., Takai Y. Localization of l-afadin at puncta adhaerentia-like junctions between the mossy fiber terminals and the dendritic trunks of pyramidal cells in the adult mouse hippocampus. J. Comp. Neurol. 424:2000;297-306.
    • (2000) J. Comp. Neurol. , vol.424 , pp. 297-306
    • Nishioka, H.1    Mizoguchi, A.2    Nakanishi, H.3    Mandai, K.4    Takahashi, K.5    Kimura, K.6    Satoh-Moriya, A.7    Takai, Y.8
  • 19
    • 0029038844 scopus 로고
    • Lamina-specific expression of adhesion molecules in developing chick optic tectum
    • Yamagata M., Herman J.P., Sanes J.R. Lamina-specific expression of adhesion molecules in developing chick optic tectum. J. Neurosci. 15:1995;4556-4571.
    • (1995) J. Neurosci. , vol.15 , pp. 4556-4571
    • Yamagata, M.1    Herman, J.P.2    Sanes, J.R.3
  • 20
    • 0037014446 scopus 로고    scopus 로고
    • Cadherin regulates dendritic spine morphogenesis
    • The authors show that the loss of N-cadherin function results in alterations of dendritic spine morphology along with concomitant disruption of the distribution of postsynaptic proteins. It is suggested that cadherins regulate dendritic spine morphogenesis.
    • Togashi H., Abe K., Mizoguchi A., Chisaka O., Takeichi M. Cadherin regulates dendritic spine morphogenesis. Neuron. 35:2002;77-89 The authors show that the loss of N-cadherin function results in alterations of dendritic spine morphology along with concomitant disruption of the distribution of postsynaptic proteins. It is suggested that cadherins regulate dendritic spine morphogenesis.
    • (2002) Neuron , vol.35 , pp. 77-89
    • Togashi, H.1    Abe, K.2    Mizoguchi, A.3    Chisaka, O.4    Takeichi, M.5
  • 21
    • 0037014456 scopus 로고    scopus 로고
    • Depolarization drives beta-Catenin into neuronal spines promoting changes in synaptic structure and function
    • The authors demonstrate that neural activity induces the redistribution of β-catenin into spines, and then interacts with cadherins there to influence synaptic size and strength.
    • Murase S., Mosser E., Schuman E.M. Depolarization drives beta-Catenin into neuronal spines promoting changes in synaptic structure and function. Neuron. 35:2002;91-105 The authors demonstrate that neural activity induces the redistribution of β-catenin into spines, and then interacts with cadherins there to influence synaptic size and strength.
    • (2002) Neuron , vol.35 , pp. 91-105
    • Murase, S.1    Mosser, E.2    Schuman, E.M.3
  • 22
    • 0032103412 scopus 로고    scopus 로고
    • A role for the cadherin family of cell adhesion molecules in hippocampal long-term potentiation
    • Tang L., Hung C.P., Schuman E.M. A role for the cadherin family of cell adhesion molecules in hippocampal long-term potentiation. Neuron. 20:1998;1165-1175.
    • (1998) Neuron , vol.20 , pp. 1165-1175
    • Tang, L.1    Hung, C.P.2    Schuman, E.M.3
  • 24
    • 0034425423 scopus 로고    scopus 로고
    • Mutations of PVRL1, encoding a cell-cell adhesion molecule/herpes virus receptor, in cleft lip/palate-ectodermal dysplasia
    • Suzuki K., Hu D., Bustos T., Zlotogora J., Richieri-Costa A., Helms J.A., Spritz R.A. Mutations of PVRL1, encoding a cell-cell adhesion molecule/herpes virus receptor, in cleft lip/palate-ectodermal dysplasia. Nat. Genet. 25:2000;427-430.
    • (2000) Nat. Genet. , vol.25 , pp. 427-430
    • Suzuki, K.1    Hu, D.2    Bustos, T.3    Zlotogora, J.4    Richieri-Costa, A.5    Helms, J.A.6    Spritz, R.A.7
  • 26
    • 0031027205 scopus 로고    scopus 로고
    • Rho family GTPases and neuronal growth cone remodelling: Relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid
    • Kozma R., Sarner S., Ahmed S., Lim L. Rho family GTPases and neuronal growth cone remodelling: relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid. Mol. Cell Biol. 17:1997;1201-1211.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 1201-1211
    • Kozma, R.1    Sarner, S.2    Ahmed, S.3    Lim, L.4
  • 27
    • 0019433958 scopus 로고
    • Development of the mossy fibers of the dentate gyrus: I. A light and electron microscopic study of the mossy fibers and their expansions
    • Amaral D.G., Dent J.A. Development of the mossy fibers of the dentate gyrus: I. A light and electron microscopic study of the mossy fibers and their expansions. J. Comp. Neurol. 195:1981;51-86.
    • (1981) J. Comp. Neurol. , vol.195 , pp. 51-86
    • Amaral, D.G.1    Dent, J.A.2
  • 29
    • 0035475301 scopus 로고    scopus 로고
    • Principles of glutamatergic synapse formation: Seeing the forest for the trees
    • Ziv N.E., Garner C.C. Principles of glutamatergic synapse formation: seeing the forest for the trees. Curr. Opin. Neurobiol. 11:2001;536-543.
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 536-543
    • Ziv, N.E.1    Garner, C.C.2
  • 30
    • 0035137129 scopus 로고    scopus 로고
    • Assembling the presynaptic active zone: A characterization of an active zone precursor vesicle
    • The authors show that PTVs are putative active zone precursor vesicles, which belong to one class of classic dense core vesicles. The PTVs are shown to contain not only the active zone proteins but also N-cadherin.
    • Zhai R.G., Vardinon-Friedman H., Cases-Langhoff C., Becker B., Gundelfinger E.D., Ziv N.E., Garner C.C. Assembling the presynaptic active zone: a characterization of an active zone precursor vesicle. Neuron. 29: 2001;131-143 The authors show that PTVs are putative active zone precursor vesicles, which belong to one class of classic dense core vesicles. The PTVs are shown to contain not only the active zone proteins but also N-cadherin.
    • (2001) Neuron , vol.29 , pp. 131-143
    • Zhai, R.G.1    Vardinon-Friedman, H.2    Cases-Langhoff, C.3    Becker, B.4    Gundelfinger, E.D.5    Ziv, N.E.6    Garner, C.C.7
  • 31
    • 0036329841 scopus 로고    scopus 로고
    • CAST: A novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and Munc13-1
    • The authors identify CAST as a novel protein of the cytomatrix at the active zone of synapses, which is likely to serve as an anchoring molecule of other active zone components.
    • Ohtsuka T., Takao-Rikitsu E., Inoue E., Inoue M., Takeuchi M., Matsubara K., Deguchi-Tawarada M., Satoh K., Morimoto K., Nakanishi H., et al. CAST: a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and Munc13-1. J. Cell Biol. 158:2002;577-590 The authors identify CAST as a novel protein of the cytomatrix at the active zone of synapses, which is likely to serve as an anchoring molecule of other active zone components.
    • (2002) J. Cell Biol. , vol.158 , pp. 577-590
    • Ohtsuka, T.1    Takao-Rikitsu, E.2    Inoue, E.3    Inoue, M.4    Takeuchi, M.5    Matsubara, K.6    Deguchi-Tawarada, M.7    Satoh, K.8    Morimoto, K.9    Nakanishi, H.10
  • 33
    • 0038301605 scopus 로고    scopus 로고
    • Nectin-dependent localization of ZO-1 at puncta adherentia junctions between the mossy fiber terminals and the dendrites of the pyramidal cells in the CA3 area of adult mouse hippocampus
    • Inagaki M., Irie K., Deguchi-Tawarada M., Ikeda W., Ohtsuka T., Takeuchi M., Takai Y. Nectin-dependent localization of ZO-1 at puncta adherentia junctions between the mossy fiber terminals and the dendrites of the pyramidal cells in the CA3 area of adult mouse hippocampus. J. Comp. Neurol. 460:2003;514-524.
    • (2003) J. Comp. Neurol. , vol.460 , pp. 514-524
    • Inagaki, M.1    Irie, K.2    Deguchi-Tawarada, M.3    Ikeda, W.4    Ohtsuka, T.5    Takeuchi, M.6    Takai, Y.7
  • 36
    • 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 2000, 101:657-69.
    • (2000) Cell , vol.101 , pp. 657-669
    • Scheiffele, P.1    Fan, J.2    Choih, J.3    Fetter, R.4    Serafini, T.5
  • 38
    • 0034928790 scopus 로고    scopus 로고
    • Morphological changes in dendritic spines associated with long-term synaptic plasticity
    • Yuste R., Bonhoeffer T. Morphological changes in dendritic spines associated with long-term synaptic plasticity. Annu. Rev. Neurosci. 24:2001;1071-1089.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1071-1089
    • Yuste, R.1    Bonhoeffer, T.2
  • 39
    • 0037146553 scopus 로고    scopus 로고
    • Nectin-1alpha, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/gamma-secretase-like cleavage
    • Kim D.Y., Ingano L.A., Kovacs D.M. Nectin-1alpha, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/gamma-secretase-like cleavage. J. Biol. Chem. 277:2002;49976-49981.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49976-49981
    • Kim, D.Y.1    Ingano, L.A.2    Kovacs, D.M.3


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