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Volumn 11, Issue 5, 1999, Pages 561-566

Mechanism of cell-cell adhesion complex assembly

Author keywords

[No Author keywords available]

Indexed keywords

CADHERIN; CELL ADHESION MOLECULE; CELL SURFACE RECEPTOR;

EID: 0032842425     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)00021-6     Document Type: Review
Times cited : (88)

References (71)
  • 1
    • 0027771776 scopus 로고
    • Cytoskeletal architecture and epithelial differentiation: Molecular determinants of cell interaction and cytoskeletal filament anchorage
    • Schafer S, Troyanovsky SM, Heid HW, Eschkind LG, Koch PJ, Franke WW Cytoskeletal architecture and epithelial differentiation: molecular determinants of cell interaction and cytoskeletal filament anchorage. CR Acad Sci III. 316:1993;1316-1323.
    • (1993) CR Acad Sci III , vol.316 , pp. 1316-1323
    • Schafer, S.1    Troyanovsky, S.M.2    Heid, H.W.3    Eschkind, L.G.4    Koch, P.J.5    Franke, W.W.6
  • 2
    • 0031440104 scopus 로고    scopus 로고
    • Molecular and functional analysis of cadherin-based adherens junctions
    • Yap AS, Brieher WM, Gumbiner BM Molecular and functional analysis of cadherin-based adherens junctions. Annu Rev Cell Dev Biol. 13:1997;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
  • 3
    • 0032440448 scopus 로고    scopus 로고
    • The tight junction: Morphology to molecules
    • Stevenson BR, Keon BH The tight junction: morphology to molecules. Annu Rev Cell Dev Biol. 14:1998;89-109.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 89-109
    • Stevenson, B.R.1    Keon, B.H.2
  • 4
  • 5
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complex
    • Yamada KM, Geiger B Molecular interactions in cell adhesion complex. Curr Opin Cell Biol. 9:1997;76-85.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 76-85
    • Yamada, K.M.1    Geiger, B.2
  • 6
    • 0028093281 scopus 로고
    • Conformational changes of the recombinant extracellular domain of E-cadherin upon calcium binding
    • Pokutta S, Herrenknecht K, Kemler R, Engel J Conformational changes of the recombinant extracellular domain of E-cadherin upon calcium binding. Eur J Biochem. 223:1994;1019-1026.
    • (1994) Eur J Biochem , vol.223 , pp. 1019-1026
    • Pokutta, S.1    Herrenknecht, K.2    Kemler, R.3    Engel, J.4
  • 7
    • 0033582334 scopus 로고    scopus 로고
    • Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands
    • This work demonstrates the existence of a novel family of transmembrane adhesion receptors, claudins, mediating formation of tight junction strands in various tissues.
    • Morita K, Furuse M, Fujimoto K, Tsukita S Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci USA. 96:1999;511-516. This work demonstrates the existence of a novel family of transmembrane adhesion receptors, claudins, mediating formation of tight junction strands in various tissues.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3    Tsukita, S.4
  • 8
    • 0025239290 scopus 로고
    • Localization of specificity determining sites in cadherin cell adhesion molecules
    • Nose A, Tsuji K, Takeichi M Localization of specificity determining sites in cadherin cell adhesion molecules. Cell. 61:1990;147-155.
    • (1990) Cell , vol.61 , pp. 147-155
    • Nose, A.1    Tsuji, K.2    Takeichi, M.3
  • 9
    • 0029980542 scopus 로고    scopus 로고
    • Structural basis of calcium-induced E-cadherin rigidification and dimerization
    • Nagar B, Overduin M, Ikura M, Rini JM Structural basis of calcium-induced E-cadherin rigidification and dimerization. Nature. 380:1996;360-364.
    • (1996) Nature , vol.380 , pp. 360-364
    • Nagar, B.1    Overduin, M.2    Ikura, M.3    Rini, J.M.4
  • 11
    • 0032102397 scopus 로고    scopus 로고
    • Structure-function analysis of cell adhesion by Neural (N-) cadherin
    • Tamura K, Shan W-S, Hendrickson WA, Colman DR, Shapiro L Structure-function analysis of cell adhesion by Neural (N-) cadherin. Neuron. 20:1998;1153-1163.
    • (1998) Neuron , vol.20 , pp. 1153-1163
    • Tamura, K.1    Shan, W.-S.2    Hendrickson, W.A.3    Colman, D.R.4    Shapiro, L.5
  • 13
    • 0033106491 scopus 로고    scopus 로고
    • Homophilic adhesion by cadherins
    • This is a comprehensive review of the molecular structure of cadherins with emphasis on possible mechanisms and functions of lateral cadherin dimers.
    • Koch AW, Bozic D, Pertz O, Engel J Homophilic adhesion by cadherins. Curr Opin Struct Biol. 9:1999;275-281. This is a comprehensive review of the molecular structure of cadherins with emphasis on possible mechanisms and functions of lateral cadherin dimers.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 275-281
    • Koch, A.W.1    Bozic, D.2    Pertz, O.3    Engel, J.4
  • 14
    • 0025238409 scopus 로고
    • Identification of a cadherin cell adhesion recognition sequence
    • Blaschuk OW, Sullivan R, David S, Pouliot Y Identification of a cadherin cell adhesion recognition sequence. Dev Biol. 139:1990;227-229.
    • (1990) Dev Biol , vol.139 , pp. 227-229
    • Blaschuk, O.W.1    Sullivan, R.2    David, S.3    Pouliot, Y.4
  • 15
    • 0000836705 scopus 로고    scopus 로고
    • Inhibition of adhesion and induction of epithelial cell invasion by HAV-containing E-cadherin-specific peptides
    • Noë V, Willems J, Vandekerckhove Van Roy F, Bruyneel E, Mareel M Inhibition of adhesion and induction of epithelial cell invasion by HAV-containing E-cadherin-specific peptides. J Cell Sci. 112:1998;127-135.
    • (1998) J Cell Sci , vol.112 , pp. 127-135
    • Noë, V.1    Willems, J.2    Vandekerckhove Van Roy, F.3    Bruyneel, E.4    Mareel, M.5
  • 16
    • 0033597125 scopus 로고    scopus 로고
    • Biochemical characterization and functional analysis of two type II classic cadherins, cadherin-6 and -14, and comparison with E-cadherin
    • Shimoyama Y, Takeda H, Yoshihara S, Kitajima M, Hirohashi S Biochemical characterization and functional analysis of two type II classic cadherins, cadherin-6 and -14, and comparison with E-cadherin. J Biol Chem. 274:1999;11987-11994.
    • (1999) J Biol Chem , vol.274 , pp. 11987-11994
    • Shimoyama, Y.1    Takeda, H.2    Yoshihara, S.3    Kitajima, M.4    Hirohashi, S.5
  • 17
    • 0031852523 scopus 로고    scopus 로고
    • Adhesive but not lateral E-cadherin complexes require calcium and catenins for their formation
    • Chitaev NA, Troyanovsky SM Adhesive but not lateral E-cadherin complexes require calcium and catenins for their formation. J Cell Biol. 142:1998;837-846.
    • (1998) J Cell Biol , vol.142 , pp. 837-846
    • Chitaev, N.A.1    Troyanovsky, S.M.2
  • 18
    • 0028273266 scopus 로고
    • Cytoskeletal involvement in the modulation of cell-cell junctions by protein kinase inhibitor H-7
    • Citi S, Volberg T, Bershadsky AD, Denisenko N, Geiger B Cytoskeletal involvement in the modulation of cell-cell junctions by protein kinase inhibitor H-7. J Cell Sci. 107:1994;683-692.
    • (1994) J Cell Sci , vol.107 , pp. 683-692
    • Citi, S.1    Volberg, T.2    Bershadsky, A.D.3    Denisenko, N.4    Geiger, B.5
  • 19
    • 0029998613 scopus 로고    scopus 로고
    • Lateral dimerization is required for the homophilic binding activity of C-cadherin
    • Brieher WM, Yap AS, Gumbiner BM Lateral dimerization is required for the homophilic binding activity of C-cadherin. J Cell Biol. 135:1996;487-496.
    • (1996) J Cell Biol , vol.135 , pp. 487-496
    • Brieher, W.M.1    Yap, A.S.2    Gumbiner, B.M.3
  • 20
    • 0030842356 scopus 로고    scopus 로고
    • Calcium binding and homoassociation of E-cadherin domains
    • Koch AW, Pokutta S, Lustig A, Engel J Calcium binding and homoassociation of E-cadherin domains. Biochemistry. 36:1997;7697-7705.
    • (1997) Biochemistry , vol.36 , pp. 7697-7705
    • Koch, A.W.1    Pokutta, S.2    Lustig, A.3    Engel, J.4
  • 21
    • 0032953786 scopus 로고    scopus 로고
    • E-cadherin functions as a cis dimer at the cell-cell adhesive interface in vivo
    • Takeda H, Yutaka S, Nagafuchi A, Hirohashi S E-cadherin functions as a cis dimer at the cell-cell adhesive interface in vivo. Nat Struct Biol. 6:1999;310-312.
    • (1999) Nat Struct Biol , vol.6 , pp. 310-312
    • Takeda, H.1    Yutaka, S.2    Nagafuchi, A.3    Hirohashi, S.4
  • 22
    • 0025651841 scopus 로고
    • A possible new adhesive site in the cell-adhesion molecule uvomorulin
    • Ozawa M, Hoschützky H, Herrenknecht K, Kemler R A possible new adhesive site in the cell-adhesion molecule uvomorulin. Mech Dev. 33:1991;49-56.
    • (1991) Mech Dev , vol.33 , pp. 49-56
    • Ozawa, M.1    Hoschützky, H.2    Herrenknecht, K.3    Kemler, R.4
  • 23
    • 0033601768 scopus 로고    scopus 로고
    • Analysis of C-cadherin regulation during tissue morphogenesis with an activating antibody
    • This paper describes production and characterization of the novel monoclonal antibody AA5 against Xenopus C-cadherin. This antibody has unique potential to enhance the cell adhesion activity of cadherins.
    • Zhong Y, Brieher WM, Gumbiner BM Analysis of C-cadherin regulation during tissue morphogenesis with an activating antibody. J Cell Biol. 144:1999;351-359. This paper describes production and characterization of the novel monoclonal antibody AA5 against Xenopus C-cadherin. This antibody has unique potential to enhance the cell adhesion activity of cadherins.
    • (1999) J Cell Biol , vol.144 , pp. 351-359
    • Zhong, Y.1    Brieher, W.M.2    Gumbiner, B.M.3
  • 25
    • 0033519211 scopus 로고    scopus 로고
    • Nectin/PRR: An immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with afadin, a PDZ domain-containing protein
    • This study demonstrates that adhesion proteins of the immunoglobulin superfamily can be co-clustered with cadherins via interactions with MAGUK proteins.
    • Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Nomoto A, Mizoguchi A, Takai Y Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with afadin, a PDZ domain-containing protein. J Cell Biol. 145:1999;539-549. This study demonstrates that adhesion proteins of the immunoglobulin superfamily can be co-clustered with cadherins via interactions with MAGUK proteins.
    • (1999) J Cell Biol , vol.145 , pp. 539-549
    • Takahashi, K.1    Nakanishi, H.2    Miyahara, M.3    Mandai, K.4    Satoh, K.5    Satoh, A.6    Nishioka, H.7    Nomoto, A.8    Mizoguchi, A.9    Takai, Y.10
  • 26
    • 0032555935 scopus 로고    scopus 로고
    • The membrane-proximal region of the E-cadherin cytoplasmic domain prevents dimerization and negatively regulates adhesion activity
    • Ozawa M, Kemler R The membrane-proximal region of the E-cadherin cytoplasmic domain prevents dimerization and negatively regulates adhesion activity. J Cell Biol. 142:1998;1605-1613.
    • (1998) J Cell Biol , vol.142 , pp. 1605-1613
    • Ozawa, M.1    Kemler, R.2
  • 27
    • 0031149109 scopus 로고    scopus 로고
    • Lateral clustering of the adhesive ectodomain: A fundamental determinant of cadherin function
    • Yap AS, Brieher WM, Pruschy M, Gumbiner BM Lateral clustering of the adhesive ectodomain: a fundamental determinant of cadherin function. Curr Biol. 7:1997;308-315.
    • (1997) Curr Biol , vol.7 , pp. 308-315
    • Yap, A.S.1    Brieher, W.M.2    Pruschy, M.3    Gumbiner, B.M.4
  • 29
    • 0027938682 scopus 로고
    • A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated
    • Stappert J, Kemler R A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated. Cell Adhesion Commun. 2:1994;319-327.
    • (1994) Cell Adhesion Commun , vol.2 , pp. 319-327
    • Stappert, J.1    Kemler, R.2
  • 30
    • 0029752762 scopus 로고    scopus 로고
    • Drosophila α-catenin and E-cadherin bind to distinct regions of Drosophila armadillo
    • Pai LM, Kirkpatrick C, Blanton J, Oda H, Takeichi M, Peifer M Drosophila α-catenin and E-cadherin bind to distinct regions of Drosophila armadillo. J Biol Chem. 271:1996;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
  • 31
    • 0032531218 scopus 로고    scopus 로고
    • Modulation of cell-cell adherens junctions by surface clustering of the N-cadherin cytoplasmic tail
    • The data in this paper demonstrate that the intracellular junctional plaque has the capacity to recruit cadherins via intracellular proteins.
    • Katz BZ, Levenberg S, Yamada KM, Geiger B Modulation of cell-cell adherens junctions by surface clustering of the N-cadherin cytoplasmic tail. Exp Cell Res. 243:1998;415-424. The data in this paper demonstrate that the intracellular junctional plaque has the capacity to recruit cadherins via intracellular proteins.
    • (1998) Exp Cell Res , vol.243 , pp. 415-424
    • Katz, B.Z.1    Levenberg, S.2    Yamada, K.M.3    Geiger, B.4
  • 32
    • 0033058556 scopus 로고    scopus 로고
    • Cadherin function in junctional complex rearrangement and posttranslational control of cadherin expression
    • Troxell ML, Chen Y-T, Cobb N, Nelson WJ, Marrs JA Cadherin function in junctional complex rearrangement and posttranslational control of cadherin expression. Am J Physiol. 45:1999;C404-C418.
    • (1999) Am J Physiol , vol.45
    • Troxell, M.L.1    Chen, Y.-T.2    Cobb, N.3    Nelson, W.J.4    Marrs, J.A.5
  • 33
    • 0027457601 scopus 로고
    • Disruption of epithelial cell-cell adhesion by exogenous expression of a mutated nonfunctional N-cadherin
    • Fujimori T, Takeichi M Disruption of epithelial cell-cell adhesion by exogenous expression of a mutated nonfunctional N-cadherin. Mol Biol Cell. 4:1993;37-47.
    • (1993) Mol Biol Cell , vol.4 , pp. 37-47
    • Fujimori, T.1    Takeichi, M.2
  • 34
    • 0033014334 scopus 로고    scopus 로고
    • Mechanism of extracellular domain-deleted dominant negative cadherins
    • Nieman MT, Kim JB, Johnson KR, Wheelock MJ Mechanism of extracellular domain-deleted dominant negative cadherins. J Cell Sci. 112:1999;1621-1632.
    • (1999) J Cell Sci , vol.112 , pp. 1621-1632
    • Nieman, M.T.1    Kim, J.B.2    Johnson, K.R.3    Wheelock, M.J.4
  • 35
    • 0026602806 scopus 로고
    • Regulation of embryonic cell adhesion by the cadherin cytoplasmic domain
    • Kintner C Regulation of embryonic cell adhesion by the cadherin cytoplasmic domain. Cell. 69:1992;225-236.
    • (1992) Cell , vol.69 , pp. 225-236
    • Kintner, C.1
  • 36
    • 0031754774 scopus 로고    scopus 로고
    • The armadillo family of structural proteins
    • Hatzfeld M The armadillo family of structural proteins. Int Rev Cytol. 186:1999;179-224.
    • (1999) Int Rev Cytol , vol.186 , pp. 179-224
    • Hatzfeld, M.1
  • 37
    • 0033519239 scopus 로고    scopus 로고
    • ctn acts as an inhibitory regulator of cadherin function in colon carcinoma cells
    • ctn acts as an inhibitory regulator of cadherin function in colon carcinoma cells. J Cell Biol. 145:1999;551-562.
    • (1999) J Cell Biol , vol.145 , pp. 551-562
    • Aono, S.1    Nakagawa, S.2    Reynolds, A.B.3    Takeichi, M.4
  • 38
    • 0030926845 scopus 로고    scopus 로고
    • Characterization of the interactions of α-catenin with α-actinin and β-catenin/plakoglobin
    • Nieset JE, Redfield AR, Knudsen JF, Johnson KR, Wheelock MJ Characterization of the interactions of α-catenin with α-actinin and β-catenin/plakoglobin. J Cell Sci. 110:1997;1013-1022.
    • (1997) J Cell Sci , vol.110 , pp. 1013-1022
    • Nieset, J.E.1    Redfield, A.R.2    Knudsen, J.F.3    Johnson, K.R.4    Wheelock, M.J.5
  • 39
    • 0033594088 scopus 로고    scopus 로고
    • Functional domains of α-catenin required for the strong state of cadherin-based cell adhesion
    • This study identified functional domains of α-catenin required for cadherin-mediated cell-cell adhesion.
    • Imamura Y, Itoh M, Maeno Y, Tsukita S, Nagafuchi A Functional domains of α-catenin required for the strong state of cadherin-based cell adhesion. J Cell Biol. 144:1999;1311-1322. This study identified functional domains of α-catenin required for cadherin-mediated cell-cell adhesion.
    • (1999) J Cell Biol , vol.144 , pp. 1311-1322
    • Imamura, Y.1    Itoh, M.2    Maeno, Y.3    Tsukita, S.4    Nagafuchi, A.5
  • 40
    • 0032482254 scopus 로고    scopus 로고
    • Vinculin is part of the cadherin-catenin junctional complex: Complex formation between α-catenin and vinculin
    • Weiss EE, Kroemker M, Rudiger A-H, Jockusch BM, Rudiger M Vinculin is part of the cadherin-catenin junctional complex: complex formation between α-catenin and vinculin. J Cell Biol. 141:1998;755-764.
    • (1998) J Cell Biol , vol.141 , pp. 755-764
    • Weiss, E.E.1    Kroemker, M.2    Rudiger, A.-H.3    Jockusch, B.M.4    Rudiger, M.5
  • 41
    • 15644363085 scopus 로고    scopus 로고
    • α-catenin vinculin interaction functions to organize the apical junctional complex in epithelial cells
    • This paper provides the first clear evidence for common mechanisms of the adherens and tight junctions assembly. The data demonstrated that expression of α-catenin in α-catenin-negative tumor cells normalizes tight junctions. The vinculin-binding domain of α-catenin was required for this effect.
    • Wataba-Uchida M, Uchida N, Imammura Y, Nagafuchi A α-catenin vinculin interaction functions to organize the apical junctional complex in epithelial cells. J Cell Biol. 142:1998;847-857. This paper provides the first clear evidence for common mechanisms of the adherens and tight junctions assembly. The data demonstrated that expression of α-catenin in α-catenin-negative tumor cells normalizes tight junctions. The vinculin-binding domain of α-catenin was required for this effect.
    • (1998) J Cell Biol , vol.142 , pp. 847-857
    • Wataba-Uchida, M.1    Uchida, N.2    Imammura, Y.3    Nagafuchi, A.4
  • 42
    • 0032469949 scopus 로고    scopus 로고
    • A mutation in α-catenin disrupts adhesion in clone A cells without perturbing its actin and β-catenin binding activity
    • Roe S, Koslov E, Rimm DL A mutation in α-catenin disrupts adhesion in clone A cells without perturbing its actin and β-catenin binding activity. Cell Adhes Commun. 5:1998;283-296.
    • (1998) Cell Adhes Commun , vol.5 , pp. 283-296
    • Roe, S.1    Koslov, E.2    Rimm, D.L.3
  • 43
    • 0032491404 scopus 로고    scopus 로고
    • Identification of the region of α-catenin that plays an essential role in cadherin-mediated cell adhesion
    • ••], this study examines α-catenin sequence requirements for cell-cell adhesion.
    • ••], this study examines α-catenin sequence requirements for cell-cell adhesion.
    • (1998) J Biol Chem , vol.273 , pp. 29524-29529
    • Ozawa, M.1
  • 44
    • 0031692261 scopus 로고    scopus 로고
    • Cytomechanics of cadherin-mediated cell-cell adhesion
    • This is a very well written current review about the role of actomyosin-generated tension in cadherins clustering.
    • Adams CL, Nelson WJ Cytomechanics of cadherin-mediated cell-cell adhesion. Curr Opin Cell Biol. 10:1998;572-577. This is a very well written current review about the role of actomyosin-generated tension in cadherins clustering.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 572-577
    • Adams, C.L.1    Nelson, W.J.2
  • 45
    • 0033605347 scopus 로고    scopus 로고
    • Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and α-catenin
    • Itoh M, Morita K, Tsukita S Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and α-catenin. J Biol Chem. 274:1999;5981-5986.
    • (1999) J Biol Chem , vol.274 , pp. 5981-5986
    • Itoh, M.1    Morita, K.2    Tsukita, S.3
  • 46
    • 0033601948 scopus 로고    scopus 로고
    • Different behavior of I-afadin and neurabin II during the formation and destruction of cell-cell adherens junctions
    • Sakisaka T, Nakanishi H, Takahashi K, Mandai K, Miyahara M, Satoh A, Takaishi K, Takai Y Different behavior of I-afadin and neurabin II during the formation and destruction of cell-cell adherens junctions. Oncogene. 18:1999;1609-1617.
    • (1999) Oncogene , vol.18 , pp. 1609-1617
    • Sakisaka, T.1    Nakanishi, H.2    Takahashi, K.3    Mandai, K.4    Miyahara, M.5    Satoh, A.6    Takaishi, K.7    Takai, Y.8
  • 47
    • 0030748548 scopus 로고    scopus 로고
    • Involvement of ZO-1 in cadherin-based adhesion through its binding to α-catenin and actin filaments
    • Itoh M, Nagafuchi A, Moroi S, Tsukita S Involvement of ZO-1 in cadherin-based adhesion through its binding to α-catenin and actin filaments. J Cell Biol. 138:1997;181-192.
    • (1997) J Cell Biol , vol.138 , pp. 181-192
    • Itoh, M.1    Nagafuchi, A.2    Moroi, S.3    Tsukita, S.4
  • 48
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • This study provides evidence that ZO-1 protein associates with the transmembrane tight junction protein occludin via a specific domain located at its amino-terminal half and with actin filaments via its carboxy-terminal domain; furthermore, it was shown that the PDZ2 domain of ZO-1 is required for heterodimerization of ZO-1 with ZO-2. The data suggest that ZO-1 may link tight junction proteins to the cortical actin cytoskeleton.
    • Fanning AS, Jameson BJ, Jasaitis LA, Anderson JM The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J Biol Chem. 273:1998;29745-29753. This study provides evidence that ZO-1 protein associates with the transmembrane tight junction protein occludin via a specific domain located at its amino-terminal half and with actin filaments via its carboxy-terminal domain; furthermore, it was shown that the PDZ2 domain of ZO-1 is required for heterodimerization of ZO-1 with ZO-2. The data suggest that ZO-1 may link tight junction proteins to the cortical actin cytoskeleton.
    • (1998) J Biol Chem , vol.273 , pp. 29745-29753
    • Fanning, A.S.1    Jameson, B.J.2    Jasaitis, L.A.3    Anderson, J.M.4
  • 49
    • 0032491603 scopus 로고    scopus 로고
    • Cortactin associates with the cell-cell junction protein ZO-1 in both Drosophila and mouse
    • Katsube T, Takahisa M, Ueda R, Hashimoto N, Kobayashi M, Togashi S Cortactin associates with the cell-cell junction protein ZO-1 in both Drosophila and mouse. J Biol Chem. 273:1998;29672-29677.
    • (1998) J Biol Chem , vol.273 , pp. 29672-29677
    • Katsube, T.1    Takahisa, M.2    Ueda, R.3    Hashimoto, N.4    Kobayashi, M.5    Togashi, S.6
  • 50
    • 0031436412 scopus 로고    scopus 로고
    • Vinculin is associated with E-cadherin adhesion complex
    • Hazan RB, Kang L, Roe S, Borgen PI, Rimm DL Vinculin is associated with E-cadherin adhesion complex. J Biol Chem. 272:1997;32448-32453.
    • (1997) J Biol Chem , vol.272 , pp. 32448-32453
    • Hazan, R.B.1    Kang, L.2    Roe, S.3    Borgen, P.I.4    Rimm, D.L.5
  • 51
    • 0032100705 scopus 로고    scopus 로고
    • Defining the interactions between intermediate filaments and desmosomes
    • Smith EA, Fuchs E Defining the interactions between intermediate filaments and desmosomes. J Cell Biol. 141:1998;1229-1241.
    • (1998) J Cell Biol , vol.141 , pp. 1229-1241
    • Smith, E.A.1    Fuchs, E.2
  • 52
    • 0029847068 scopus 로고    scopus 로고
    • Breaking the connections: Displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly
    • Bornslaeger EA, Corcoran CM, Stappenbeck TS, Green KJ Breaking the connections: displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly. J Cell Biol. 134:1996;985-1001.
    • (1996) J Cell Biol , vol.134 , pp. 985-1001
    • Bornslaeger, E.A.1    Corcoran, C.M.2    Stappenbeck, T.S.3    Green, K.J.4
  • 53
    • 0028153267 scopus 로고
    • Identification of amino acid sequence motifs in the desmosomal glycoprotein, desmocollin, that are required for plakoglobin binding and plaque formation
    • Troyanovsky SM, Troyanovsky RB, Eshkind LG, Leube RL, Franke WW Identification of amino acid sequence motifs in the desmosomal glycoprotein, desmocollin, that are required for plakoglobin binding and plaque formation. Proc Natl Acad Sci USA. 91:1994;10790-10794.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10790-10794
    • Troyanovsky, S.M.1    Troyanovsky, R.B.2    Eshkind, L.G.3    Leube, R.L.4    Franke, W.W.5
  • 54
    • 0030479469 scopus 로고    scopus 로고
    • Cadherin binding sites of plakoglobin: Localization, specificity and role in targeting to adhering junctions
    • Troyanovsky RB, Chitaev NA, Troyanovsky SM Cadherin binding sites of plakoglobin: localization, specificity and role in targeting to adhering junctions. J Cell Sci. 109:1996;3069-3078.
    • (1996) J Cell Sci , vol.109 , pp. 3069-3078
    • Troyanovsky, R.B.1    Chitaev, N.A.2    Troyanovsky, S.M.3
  • 55
    • 20644437528 scopus 로고    scopus 로고
    • Desmoplakin is required early in development for assembly of desmosomes and cytoskeletal linkage
    • This provides genetic evidence that desmoplakin plays a critical function not only in anchoring intermediate filaments to desmosomes but also in desmosome assembly.
    • Galliciano GI, Kouklis P, Bauer C, Yin M, Vasioukhin V, Degenstain L, Fuchs E Desmoplakin is required early in development for assembly of desmosomes and cytoskeletal linkage. J Cell Biol. 143:1998;2009-2022. This provides genetic evidence that desmoplakin plays a critical function not only in anchoring intermediate filaments to desmosomes but also in desmosome assembly.
    • (1998) J Cell Biol , vol.143 , pp. 2009-2022
    • Galliciano, G.I.1    Kouklis, P.2    Bauer, C.3    Yin, M.4    Vasioukhin, V.5    Degenstain, L.6    Fuchs, E.7
  • 56
    • 0031771007 scopus 로고    scopus 로고
    • VE-cadherin and desmoplakin are assembled into dermal microvascular endothelial intercellular junctions: A pivotal role for plakoglobin in the recruitment of desmoplakin to intercellular junctions
    • Kowalczyk AP, Navarro P, Dejana E, Bornslaeger EA, Green KJ, Kopp DS, Borgward JE VE-cadherin and desmoplakin are assembled into dermal microvascular endothelial intercellular junctions: a pivotal role for plakoglobin in the recruitment of desmoplakin to intercellular junctions. J Cell Sci. 111:1998;3045-3057.
    • (1998) J Cell Sci , vol.111 , pp. 3045-3057
    • Kowalczyk, A.P.1    Navarro, P.2    Dejana, E.3    Bornslaeger, E.A.4    Green, K.J.5    Kopp, D.S.6    Borgward, J.E.7
  • 57
    • 0030579159 scopus 로고    scopus 로고
    • Gap junction formation between cultured embryonic lens cells is inhibited by antibody to N-cadherin
    • Frenzel EM, Johnson RG Gap junction formation between cultured embryonic lens cells is inhibited by antibody to N-cadherin. Dev Biol. 179:1996;1-16.
    • (1996) Dev Biol , vol.179 , pp. 1-16
    • Frenzel, E.M.1    Johnson, R.G.2
  • 58
    • 0024095524 scopus 로고
    • The role of cell adhesive molecule uvomorulin in the formation and maintenance of the epithelial junctional complex
    • Gumbiner B, Stevenson B, Grimaldi A The role of cell adhesive molecule uvomorulin in the formation and maintenance of the epithelial junctional complex. J Cell Biol. 107:1988;1575-1578.
    • (1988) J Cell Biol , vol.107 , pp. 1575-1578
    • Gumbiner, B.1    Stevenson, B.2    Grimaldi, A.3
  • 60
    • 0030610386 scopus 로고    scopus 로고
    • Cell-junctional and cytoskeletal organization in mouse blastocysts lacking E-cadherin
    • Ohsungi M, Larue L, Schwarz H, Kemler R Cell-junctional and cytoskeletal organization in mouse blastocysts lacking E-cadherin. Dev Biol. 185:1997;261-271.
    • (1997) Dev Biol , vol.185 , pp. 261-271
    • Ohsungi, M.1    Larue, L.2    Schwarz, H.3    Kemler, R.4
  • 61
    • 13144252170 scopus 로고    scopus 로고
    • The gap junction protein connexin-43 interacts with the second PDZ domain of the zona occludens-1 protein
    • Giepmans BN, Moolenaar WH The gap junction protein connexin-43 interacts with the second PDZ domain of the zona occludens-1 protein. Curr Biol. 8:1998;931-934.
    • (1998) Curr Biol , vol.8 , pp. 931-934
    • Giepmans, B.N.1    Moolenaar, W.H.2
  • 62
    • 0032557460 scopus 로고    scopus 로고
    • Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes
    • Toyofuku T, Yabuki M, Otsu K, Kuzuya T, Hori M, Tada M Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes. J Biol Chem. 273:1998;12725-12731.
    • (1998) J Biol Chem , vol.273 , pp. 12725-12731
    • Toyofuku, T.1    Yabuki, M.2    Otsu, K.3    Kuzuya, T.4    Hori, M.5    Tada, M.6
  • 63
    • 0027468175 scopus 로고
    • Contributions of cytoplasmic domains of desmosomal cadherins to desmosome assembly and intermediate filament anchorage
    • Troyanovsky SM, Eshkind LG, Troyanovsky RB, Leube RE, Franke WW Contributions of cytoplasmic domains of desmosomal cadherins to desmosome assembly and intermediate filament anchorage. Cell. 72:1993;561-574.
    • (1993) Cell , vol.72 , pp. 561-574
    • Troyanovsky, S.M.1    Eshkind, L.G.2    Troyanovsky, R.B.3    Leube, R.E.4    Franke, W.W.5
  • 67
  • 68
    • 0032493903 scopus 로고    scopus 로고
    • Role of IQGAP1, a target of the small GTPases Cdc42 and Rac1, in regulation of E-cadherin-mediated cell-cell adhesion
    • This study shows one of the mechanisms by which Rho-like GTPases regulate assembly of the cadherin-catenin complex.
    • Kuroda S, Fukata M, Nakagawa M, Fujii K, Nakamura T, Ookuda T, Izawa I, Nagase T, Nomura N, Tani Het al. Role of IQGAP1, a target of the small GTPases Cdc42 and Rac1, in regulation of E-cadherin-mediated cell-cell adhesion. Science. 281:1998;832-835. This study shows one of the mechanisms by which Rho-like GTPases regulate assembly of the cadherin-catenin complex.
    • (1998) Science , vol.281 , pp. 832-835
    • Kuroda, S.1    Fukata, M.2    Nakagawa, M.3    Fujii, K.4    Nakamura, T.5    Ookuda, T.6    Izawa, I.7    Nagase, T.8    Nomura, N.9    Tani, H.10
  • 69
    • 0032583205 scopus 로고    scopus 로고
    • Matrix-dependent Tiam1/Rac signalling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase
    • An important study showing that the effect of Rac (Rho-like GTPase) on cell-cell adhesion is cell-type specific. A constitutively active form of Rac increases epithelial cell-cell adhesion on fibronectin, while promoting cell-cell dissociation on collagens.
    • Sander EE, van Delft S, tem Klooster JP, Reid T, van der Kammen RA, Michiels F, Collard JD Matrix-dependent Tiam1/Rac signalling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase. J Cell Biol. 143:1998;1385-1398. An important study showing that the effect of Rac (Rho-like GTPase) on cell-cell adhesion is cell-type specific. A constitutively active form of Rac increases epithelial cell-cell adhesion on fibronectin, while promoting cell-cell dissociation on collagens.
    • (1998) J Cell Biol , vol.143 , pp. 1385-1398
    • Sander, E.E.1    Van Delft, S.2    Tem Klooster, J.P.3    Reid, T.4    Van Der Kammen, R.A.5    Michiels, F.6    Collard, J.D.7
  • 70
    • 0031971198 scopus 로고    scopus 로고
    • Modulation of hepatocyte growth factor-induced scattering of HT29 colon carcinoma cells. Involvement of the MAPK pathway
    • Herrera R Modulation of hepatocyte growth factor-induced scattering of HT29 colon carcinoma cells. Involvement of the MAPK pathway. J Cell Sci. 111:1998;1039-1049.
    • (1998) J Cell Sci , vol.111 , pp. 1039-1049
    • Herrera, R.1
  • 71
    • 0031829163 scopus 로고    scopus 로고
    • Activation of both MAP kinase and phosphatidylinositide 3-kinase by Ras is required for hepatocyte growth factor/scatter factor-induced adherens junction disassembly
    • Potempa S, Ridley AJ Activation of both MAP kinase and phosphatidylinositide 3-kinase by Ras is required for hepatocyte growth factor/scatter factor-induced adherens junction disassembly. Moll Biol Cell. 9:1998;2185-2200.
    • (1998) Moll Biol Cell , vol.9 , pp. 2185-2200
    • Potempa, S.1    Ridley, A.J.2


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