메뉴 건너뛰기




Volumn 144, Issue 3, 1999, Pages 519-532

δ-catenin, an adhesive junction-associated protein which promotes cell scattering

Author keywords

catenin; Adhesive junctions; Armadillo; Cell motility; Neural development

Indexed keywords

BETA CATENIN; CADHERIN; CATENIN; CELL ADHESION MOLECULE;

EID: 0033535058     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.144.3.519     Document Type: Article
Times cited : (169)

References (63)
  • 1
    • 0028578064 scopus 로고
    • Assembly of the cadherin-catenin complex in vitro with recombinant proteins
    • Aberle, H., S. Butz, J. Stappert, H. Weissig, R. Kemler, and H. Hoschuetzky. 1994. Assembly of the cadherin-catenin complex in vitro with recombinant proteins. J. Cell Sci. 107:3655-3663.
    • (1994) J. Cell Sci. , vol.107 , pp. 3655-3663
    • Aberle, H.1    Butz, S.2    Stappert, J.3    Weissig, H.4    Kemler, R.5    Hoschuetzky, H.6
  • 2
    • 0030000980 scopus 로고    scopus 로고
    • Cadherin-catenin complex: Protein interactions and their implications for cadherin function
    • Aberle, H., H. Schwartz, and R. Kemler. 1996. Cadherin-catenin complex: protein interactions and their implications for cadherin function. J. Cell. Biochem. 61:514-523.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 514-523
    • Aberle, H.1    Schwartz, H.2    Kemler, R.3
  • 3
    • 0031026047 scopus 로고    scopus 로고
    • Hepatocyte growth factor alters the polarity of Madin-Darby canine kidney cell monolayers
    • Balkovetz, D.F., A.L. Pollack, and K.E. Mostov. 1997. Hepatocyte growth factor alters the polarity of Madin-Darby canine kidney cell monolayers. J. Biol. Chem. 272:3471-3477.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3471-3477
    • Balkovetz, D.F.1    Pollack, A.L.2    Mostov, K.E.3
  • 4
    • 0342327346 scopus 로고    scopus 로고
    • Cadherins, catenins and APC protein: Interplay between cytoskeletal complexes and signaling pathways
    • Barth, A.I., I.S. Nathke, and W.J. Nelson. 1997a. Cadherins, catenins and APC protein: interplay between cytoskeletal complexes and signaling pathways. Curr. Opin. Cell Biol. 9:683-690.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 683-690
    • Barth, A.I.1    Nathke, I.S.2    Nelson, W.J.3
  • 5
    • 0030614352 scopus 로고    scopus 로고
    • 2-terminal deletion of beta-catenin results in stable colocalization of mutant beta-catenin with adenomatous polyposis coli protein and altered MDCK cell adhesion
    • 2-terminal deletion of beta-catenin results in stable colocalization of mutant beta-catenin with adenomatous polyposis coli protein and altered MDCK cell adhesion. J. Cell Biol. 136:693-706.
    • (1997) J. Cell Biol. , vol.136 , pp. 693-706
    • Barth, A.I.1    Pollack, A.L.2    Altschuler, Y.3    Mostov, K.E.4    Nelson, W.J.5
  • 6
    • 0029998613 scopus 로고    scopus 로고
    • Lateral dimerization is required for the homophilic binding activity of C-cadherin
    • Brieher, W.M., A.S. Yap, and B.M. Gumbiner. 1996. Lateral dimerization is required for the homophilic binding activity of C-cadherin. J. Cell Biol. 135: 487-496.
    • (1996) J. Cell Biol. , vol.135 , pp. 487-496
    • Brieher, W.M.1    Yap, A.S.2    Gumbiner, B.M.3
  • 8
    • 0029102071 scopus 로고
    • The tyrosine kinase substrate p120cas binds directly to F-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin
    • Daniel, J.M. and A.B. Reynolds. 1995. The tyrosine kinase substrate p120cas binds directly to F-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin. Mol. Cell. Biol. 15:4819-4824.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4819-4824
    • Daniel, J.M.1    Reynolds, A.B.2
  • 9
    • 0031259778 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and cadherin/catenin function
    • Daniel, J.M., and A.B. Reynolds. 1997. Tyrosine phosphorylation and cadherin/catenin function. Bioessays. 19:883-891.
    • (1997) Bioessays , vol.19 , pp. 883-891
    • Daniel, J.M.1    Reynolds, A.B.2
  • 10
    • 0028954815 scopus 로고
    • Embryonic axis induction by the armadillo repeat domain of beta-catenin: Evidence for intracellular signaling
    • Funayama, N., F. Fagotto, P. McCrea, and B.M. Gumbiner. 1995. Embryonic axis induction by the armadillo repeat domain of beta-catenin: evidence for intracellular signaling. J. Cell Biol. 128:959-968.
    • (1995) J. Cell Biol. , vol.128 , pp. 959-968
    • Funayama, N.1    Fagotto, F.2    McCrea, P.3    Gumbiner, B.M.4
  • 11
    • 0029859086 scopus 로고    scopus 로고
    • Cloning and characterization of a new armadillo family member. P0071, associated with the functional plaque-evidence for a subfamily of closely related proteins
    • Hatzfeld, M., and C. Nachtsheim. 1996. Cloning and characterization of a new armadillo family member. P0071, associated with the functional plaque-evidence for a subfamily of closely related proteins. J. Cell Sci. 109:2767-2778.
    • (1996) J. Cell Sci. , vol.109 , pp. 2767-2778
    • Hatzfeld, M.1    Nachtsheim, C.2
  • 13
    • 0014977557 scopus 로고
    • Cell proliferation in the neural tube: An electron microscopic and Golgi analysis in the mouse cerebral vesicle
    • Hinds, J.W. and T.L. Ruffett. 1971. Cell proliferation in the neural tube: an electron microscopic and Golgi analysis in the mouse cerebral vesicle. Z. Zellforch. Mikrosk. Anat. 115:226-264.
    • (1971) Z. Zellforch. Mikrosk. Anat. , vol.115 , pp. 226-264
    • Hinds, J.W.1    Ruffett, T.L.2
  • 14
    • 0028170977 scopus 로고
    • Beta-catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor
    • Hoschuetzky, H., H. Aberle, and R. Kemler. 1994. Beta-catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor. J. Cell Biol. 127:1375-1380.
    • (1994) J. Cell Biol. , vol.127 , pp. 1375-1380
    • Hoschuetzky, H.1    Aberle, H.2    Kemler, R.3
  • 15
    • 0031035703 scopus 로고    scopus 로고
    • Mouse disabled (mDab1): A Src binding protein implicated in neuronal development
    • Howell, B.W., F.B. Gertler, and J.A. Cooper. 1997a. Mouse disabled (mDab1): a Src binding protein implicated in neuronal development. EMBO (Eur. Mol. Biol. Organ.) J. 16:121-132.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 121-132
    • Howell, B.W.1    Gertler, F.B.2    Cooper, J.A.3
  • 16
    • 0030704354 scopus 로고    scopus 로고
    • Neuronal position in the developing brain is regulated by mouse disabled-1
    • Howell, B.W., R. Hawkes, P. Soriano, and J.A. Cooper. 1997b. Neuronal position in the developing brain is regulated by mouse disabled-1. Nature. 389: 733-737.
    • (1997) Nature , vol.389 , pp. 733-737
    • Howell, B.W.1    Hawkes, R.2    Soriano, P.3    Cooper, J.A.4
  • 17
    • 0029040123 scopus 로고
    • Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex
    • Jou, T., D. Steward, J. Stappert, W. Nelson, and J. Marrs. 1995. Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex. Proc. Natl. Acad. Sci. USA. 92:5067-5071.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5067-5071
    • Jou, T.1    Steward, D.2    Stappert, J.3    Nelson, W.4    Marrs, J.5
  • 18
    • 0021716406 scopus 로고
    • A short amino acid sequence able to specify nuclear location
    • Kalderon, D., B.L. Roberts, W.D. Richardson, and A.E. Smith. 1984. A short amino acid sequence able to specify nuclear location. Cell. 39:499-509.
    • (1984) Cell , vol.39 , pp. 499-509
    • Kalderon, D.1    Roberts, B.L.2    Richardson, W.D.3    Smith, A.E.4
  • 19
    • 0023917828 scopus 로고
    • 1 75,000 as an accessory desmosomal plaque protein in stratified and complex epithelia
    • 1 75,000 as an accessory desmosomal plaque protein in stratified and complex epithelia. J. Cell Biol. 106:1679-1691.
    • (1988) J. Cell Biol. , vol.106 , pp. 1679-1691
    • Kapprell, H.P.1    Owaribe, K.2    Franke, W.W.3
  • 20
    • 0029116143 scopus 로고
    • Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia
    • Kinch, M.S., G.H. Clark, C.J. Der, and K. Burridge. 1995. Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia. J. Cell Biol. 130:461-471.
    • (1995) J. Cell Biol. , vol.130 , pp. 461-471
    • Kinch, M.S.1    Clark, G.H.2    Der, C.J.3    Burridge, K.4
  • 21
    • 0028979956 scopus 로고
    • Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin
    • Knudsen, K.A., A.P. Soler, K.R. Johnson, and M.J. Wheelock. 1995. Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin J. Cell Biol. 130:67-77.
    • (1995) J. Cell Biol. , vol.130 , pp. 67-77
    • Knudsen, K.A.1    Soler, A.P.2    Johnson, K.R.3    Wheelock, M.J.4
  • 23
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • Kozak, M. 1986. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell. 44:283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 24
    • 0031867842 scopus 로고    scopus 로고
    • Basal extracellular signal-regulated kinase activity modulates cell-cell and cell-matrix interactions
    • Lu, Q., M. Paredesm J. Zhangm and K. Kosik. 1998. Basal extracellular signal-regulated kinase activity modulates cell-cell and cell-matrix interactions. Mol. Cell. Biol. 18:3257-3265.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3257-3265
    • Lu, Q.1    Paredesm, M.2    Zhangm, J.3    Kosik, K.4
  • 25
    • 0029935329 scopus 로고    scopus 로고
    • Cadherin cell adhesion molecules in differentiation and embryogenesis
    • Marrs, J.A., and W.J. Nelson. 1996. Cadherin cell adhesion molecules in differentiation and embryogenesis. Int. Rev. Cytol. 165:159-205.
    • (1996) Int. Rev. Cytol. , vol.165 , pp. 159-205
    • Marrs, J.A.1    Nelson, W.J.2
  • 26
    • 0028318203 scopus 로고
    • Interactions of the cytoplasmic domain of the desmosomal cadherin Dsg1 with plakoglobin
    • Mathur, M., L. Goodwin, and P. Cowin. 1994. Interactions of the cytoplasmic domain of the desmosomal cadherin Dsg1 with plakoglobin. J. Biol. Chem. 269:14075-14080.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14075-14080
    • Mathur, M.1    Goodwin, L.2    Cowin, P.3
  • 27
    • 0029825414 scopus 로고    scopus 로고
    • Plakophilins 2a and 2b: Constitutive proteins of dual location in the karyoplasm and the desmosomal plaque
    • Mertens, C., C. Kuhn, and W.W. Franke. 1996. Plakophilins 2a and 2b: constitutive proteins of dual location in the karyoplasm and the desmosomal plaque. J. Cell Biol. 135:1009-1025.
    • (1996) J. Cell Biol. , vol.135 , pp. 1009-1025
    • Mertens, C.1    Kuhn, C.2    Franke, W.W.3
  • 28
    • 1842390685 scopus 로고    scopus 로고
    • Cell binding function of E-cadherin is regulated by the cytoplasmic domain
    • Nagafuchi, A., and M. Takeichi. 1998. Cell binding function of E-cadherin is regulated by the cytoplasmic domain. EMBO (Eur. Mol. Biol. Organ.) J. 7:3679-3684.
    • (1998) EMBO (Eur. Mol. Biol. Organ.) J. , vol.7 , pp. 3679-3684
    • Nagafuchi, A.1    Takeichi, M.2
  • 29
    • 0030926845 scopus 로고    scopus 로고
    • Characterization of the interactions of alpha-catenin with alpha-actinin and beta-catenin/plakoglobin
    • Nieset, J.E., A.R. Redfield, F. Jin, K.A. Knudsen, K.R. Johnson, and M.J. Wheelock. 1997. Characterization of the interactions of alpha-catenin with alpha-actinin and beta-catenin/plakoglobin. J. Cell Sci. 110:1013-1022.
    • (1997) J. Cell Sci. , vol.110 , pp. 1013-1022
    • Nieset, J.E.1    Redfield, A.R.2    Jin, F.3    Knudsen, K.A.4    Johnson, K.R.5    Wheelock, M.J.6
  • 30
    • 0029768676 scopus 로고    scopus 로고
    • An in vivo structure-function study of armadillo, the beta-catenin homologue, reveals both separate and overlapping regions of the protein required for cell adhesion and for wingless signaling
    • Orsulic, S., and M. Peifer. 1996. An in vivo structure-function study of armadillo, the beta-catenin homologue, reveals both separate and overlapping regions of the protein required for cell adhesion and for wingless signaling. J. Cell Biol. 134:1283-1300.
    • (1996) J. Cell Biol. , vol.134 , pp. 1283-1300
    • Orsulic, S.1    Peifer, M.2
  • 31
    • 0032555935 scopus 로고    scopus 로고
    • The membrane-proximal region of the E-cadherin cytoplasmic domain prevents dimerization and negatively regulates adhesion activity
    • Ozawa, M., and R. Kemler. 1998. The membrane-proximal region of the E-cadherin cytoplasmic domain prevents dimerization and negatively regulates adhesion activity. J. Cell Biol. 142:1605-1613.
    • (1998) J. Cell Biol. , vol.142 , pp. 1605-1613
    • Ozawa, M.1    Kemler, R.2
  • 32
    • 0024451982 scopus 로고
    • The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species
    • Ozawa, M., H. Baribault, and R. Kemler. 1989. The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species. EMBO (Eur. Mol. Biol. Organ.) J. 8:1711-1717.
    • (1989) EMBO (Eur. Mol. Biol. Organ.) J. , vol.8 , pp. 1711-1717
    • Ozawa, M.1    Baribault, H.2    Kemler, R.3
  • 33
    • 0030850642 scopus 로고    scopus 로고
    • Identification and localization of a neurally expressed member of the plakoglobin/armadillo multigene family
    • Paffenholz, R., and W.W. Franke. 1997. Identification and localization of a neurally expressed member of the plakoglobin/armadillo multigene family. Differentiation. 61:293-304.
    • (1997) Differentiation , vol.61 , pp. 293-304
    • Paffenholz, R.1    Franke, W.W.2
  • 34
    • 0029752762 scopus 로고    scopus 로고
    • Drosophila alpha-catenin and E-cadherin bind to distinct regions of Drosophila Armadillo
    • Pai, L.M., C. Kirkpatrick, J. Blanton, H. Oda, M. Takeichi, and M. Peifer. 1996. Drosophila alpha-catenin and E-cadherin bind to distinct regions of Drosophila Armadillo. J. Biol. Chem. 271:32411-32420.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32411-32420
    • Pai, L.M.1    Kirkpatrick, C.2    Blanton, J.3    Oda, H.4    Takeichi, M.5    Peifer, M.6
  • 35
    • 0030844356 scopus 로고    scopus 로고
    • Negative regulation of Armadillo, a Wingless effector in Drosophila
    • Pai, L.M., S. Orsulic, A. Bejsovec, and M. Peifer. 1997. Negative regulation of Armadillo, a Wingless effector in Drosophila. Development (Camb.) 124: 2255-2266.
    • (1997) Development (Camb.) , vol.124 , pp. 2255-2266
    • Pai, L.M.1    Orsulic, S.2    Bejsovec, A.3    Peifer, M.4
  • 36
    • 0028266975 scopus 로고
    • A repeating amino acid motif shared by proteins with diverse cellular roles
    • Peifer, M., S. Berg, and A.B. Reynolds. 1994. A repeating amino acid motif shared by proteins with diverse cellular roles. Cell. 76:789-791.
    • (1994) Cell , vol.76 , pp. 789-791
    • Peifer, M.1    Berg, S.2    Reynolds, A.B.3
  • 38
    • 0030923749 scopus 로고    scopus 로고
    • Dynamics of beta-catenin interactions with APC protein regulate epithelial tubulogenesis
    • Pollack, A.L., A.I.M. Barth, Y. Altschuler, W.J. Nelson, and K.E. Mostov. 1997. Dynamics of beta-catenin interactions with APC protein regulate epithelial tubulogenesis. J. Cell Biol. 137:1651-1662.
    • (1997) J. Cell Biol. , vol.137 , pp. 1651-1662
    • Pollack, A.L.1    Barth, A.I.M.2    Altschuler, Y.3    Nelson, W.J.4    Mostov, K.E.5
  • 40
    • 0028019276 scopus 로고
    • Identification of a new catenin: The tyrosine kinase substrate p120cas associates with E-cadherin complexes
    • Reynolds, A.B., J. Daniel, P.D. McCrea, M.J. Wheelock, J. Wu, and Z. Zhang. 1994. Identification of a new catenin: the tyrosine kinase substrate p120cas associates with E-cadherin complexes. Mol. Cell. Biol. 14:8333-8342.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8333-8342
    • Reynolds, A.B.1    Daniel, J.2    McCrea, P.D.3    Wheelock, M.J.4    Wu, J.5    Zhang, Z.6
  • 41
    • 0029665589 scopus 로고    scopus 로고
    • The novel catenin p120cas binds classical cadherins and induces an unusual morphological phenotype in NIH3T3 fibroblasts
    • Reynolds, A.B., J.M. Daniel, Y.Y. Mo, J. Wu, and Z. Zhang. 1996. The novel catenin p120cas binds classical cadherins and induces an unusual morphological phenotype in NIH3T3 fibroblasts. Exp. Cell Res. 225:328-337.
    • (1996) Exp. Cell Res. , vol.225 , pp. 328-337
    • Reynolds, A.B.1    Daniel, J.M.2    Mo, Y.Y.3    Wu, J.4    Zhang, Z.5
  • 42
    • 0024488978 scopus 로고
    • Molecular analysis of the armadillo locus: Uniformly distributed transcripts and a protein with novel internal repeats are associated with a Drosophila segment polarity gene
    • Riggleman, B., E. Wieschaus, and P. Schedl. 1989. Molecular analysis of the armadillo locus: uniformly distributed transcripts and a protein with novel internal repeats are associated with a Drosophila segment polarity gene. Genes Dev. 3:96-113.
    • (1989) Genes Dev. , vol.3 , pp. 96-113
    • Riggleman, B.1    Wieschaus, E.2    Schedl, P.3
  • 43
    • 0028981208 scopus 로고
    • Alpha 1 (E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex
    • Rimm, D.L., E.R. Koslov, P. Kebraiaci, C.D. Cianci, and J.S. Morrow. 1995. Alpha 1 (E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex. Proc. Natl. Acad. Sci. USA. 92:8813-8817.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8813-8817
    • Rimm, D.L.1    Koslov, E.R.2    Kebraiaci, P.3    Cianci, C.D.4    Morrow, J.S.5
  • 44
    • 0028564863 scopus 로고
    • Scatter factor and the e-met receptor: A paradigm for mesenchymal/epithelial interaction
    • Rosen, E.M., S.K. Nigam, and I.D. Goldberg. 1994. Scatter factor and the e-met receptor: a paradigm for mesenchymal/epithelial interaction. J. Cell Biol. 127:1783-1787.
    • (1994) J. Cell Biol. , vol.127 , pp. 1783-1787
    • Rosen, E.M.1    Nigam, S.K.2    Goldberg, I.D.3
  • 45
    • 0029664368 scopus 로고    scopus 로고
    • Binding of GSK3 beta to the APC-beta-catenin complex and regulation of complex assembly
    • Rubinfeld, B., I. Albert, E. Porfiri, C. Fiol, S. Munemitsu, and P. Polakis. 1996. Binding of GSK3 beta to the APC-beta-catenin complex and regulation of complex assembly. Science. 272:1023-1026.
    • (1996) Science , vol.272 , pp. 1023-1026
    • Rubinfeld, B.1    Albert, I.2    Porfiri, E.3    Fiol, C.4    Munemitsu, S.5    Polakis, P.6
  • 49
    • 0029757471 scopus 로고    scopus 로고
    • Dominant negative inhibition of the association between beta-catenin and c-erbB-2 by N-terminally deleted beta-catenin suppresses the invasion and metastasis of cancer cells
    • Shibata, T., A. Ochiai, Y. Kanai, S. Akimoto, M. Gotoh, N. Yasui, R. Machinami, and S. Hirohashi. 1996. Dominant negative inhibition of the association between beta-catenin and c-erbB-2 by N-terminally deleted beta-catenin suppresses the invasion and metastasis of cancer cells. Oncogene. 13: 883-889.
    • (1996) Oncogene , vol.13 , pp. 883-889
    • Shibata, T.1    Ochiai, A.2    Kanai, Y.3    Akimoto, S.4    Gotoh, M.5    Yasui, N.6    Machinami, R.7    Hirohashi, S.8
  • 50
    • 0018186897 scopus 로고
    • The development of the cerebral cortex in the embryonic mouse: An electron microscopic serial section analysis
    • Shoukimas, G.M., and J.W. Hinds. 1978. The development of the cerebral cortex in the embryonic mouse: an electron microscopic serial section analysis. J. Comp. Neurol. 179:795-830.
    • (1978) J. Comp. Neurol. , vol.179 , pp. 795-830
    • Shoukimas, G.M.1    Hinds, J.W.2
  • 52
    • 0029116142 scopus 로고
    • p120, a p120-related protein (p100), and the cadherin/catenin complex
    • Staddon, J.M., C. Smales, C. Schulze, F. Esch, and L.L. Rubin. 1995. p120, a p120-related protein (p100), and the cadherin/catenin complex. J. Cell Biol. 130:369-381.
    • (1995) J. Cell Biol. , vol.130 , pp. 369-381
    • Staddon, J.M.1    Smales, C.2    Schulze, C.3    Esch, F.4    Rubin, L.L.5
  • 53
    • 0025894092 scopus 로고
    • Cadherin cell adhesion receptors as a morphogenetic regulator
    • Takeichi, M. 1991. Cadherin cell adhesion receptors as a morphogenetic regulator. Science. 251:1451-1455.
    • (1991) Science , vol.251 , pp. 1451-1455
    • Takeichi, M.1
  • 54
    • 0029160437 scopus 로고
    • Morphogenetic roles of classic cadherins
    • Takeichi, M. 1995. Morphogenetic roles of classic cadherins. Curr. Opin. Cell Biol. 7:619-627.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 619-627
    • Takeichi, M.1
  • 55
    • 0029776445 scopus 로고    scopus 로고
    • Beta-catenin associates with the actin-bundling protein fascin in a noncadherin complex
    • Tao, Y.S., R.A. Edwards, B. Tubb, S. Wang, J. Bryan, and P.D. McCrea. 1996. Beta-catenin associates with the actin-bundling protein fascin in a noncadherin complex. J. Cell Biol. 134:1271-1281.
    • (1996) J. Cell Biol. , vol.134 , pp. 1271-1281
    • Tao, Y.S.1    Edwards, R.A.2    Tubb, B.3    Wang, S.4    Bryan, J.5    McCrea, P.D.6
  • 56
    • 0032568797 scopus 로고    scopus 로고
    • The cadherin superfamily at the synapse: More members, more missions
    • Uemura, T. 1998. The cadherin superfamily at the synapse: more members, more missions. Cell. 93:1095-1098.
    • (1998) Cell , vol.93 , pp. 1095-1098
    • Uemura, T.1
  • 59
    • 0031440104 scopus 로고    scopus 로고
    • Molecular and functional analysis of cadherin-based adherens junctions
    • Yap, A.S., W.M. Brieher, and B.M. Gumbiner. 1997. Molecular and functional analysis of cadherin-based adherens junctions. Annu. Rev. Cell Dev. Biol. 13: 119-146.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 119-146
    • Yap, A.S.1    Brieher, W.M.2    Gumbiner, B.M.3
  • 60
    • 0032482201 scopus 로고    scopus 로고
    • The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p120
    • Yap, A.S., C.M. Niessen, and B.M. Gumbiner. 1998. The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p120. J. Cell Biol. 141:779-789.
    • (1998) J. Cell Biol. , vol.141 , pp. 779-789
    • Yap, A.S.1    Niessen, C.M.2    Gumbiner, B.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.