메뉴 건너뛰기




Volumn 1778, Issue 3, 2008, Pages 670-691

Structural and functional associations of apical junctions with cytoskeleton

Author keywords

Actin cytoskeleton; Cadherin; Epithelial cell polarity; Nectin; Small G protein

Indexed keywords

ACTIN;

EID: 39849084350     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.12.014     Document Type: Review
Times cited : (134)

References (228)
  • 1
    • 33645963995 scopus 로고    scopus 로고
    • Claudins and epithelial paracellular transport
    • Van Itallie C.M., and Anderson J.M. Claudins and epithelial paracellular transport. Annu. Rev. Physiol. 68 (2006) 403-429
    • (2006) Annu. Rev. Physiol. , vol.68 , pp. 403-429
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 3
    • 7244219999 scopus 로고    scopus 로고
    • Establishment and characterization of cultured epithelial cells lacking expression of ZO-1
    • Umeda K., Matsui T., Nakayama M., Furuse K., Sasaki H., Furuse M., and Tsukita S. Establishment and characterization of cultured epithelial cells lacking expression of ZO-1. J. Biol. Chem. 279 (2004) 44785-44794
    • (2004) J. Biol. Chem. , vol.279 , pp. 44785-44794
    • Umeda, K.1    Matsui, T.2    Nakayama, M.3    Furuse, K.4    Sasaki, H.5    Furuse, M.6    Tsukita, S.7
  • 4
    • 0033168966 scopus 로고    scopus 로고
    • Occludin and claudins in tight-junction strands: leading or supporting players?
    • Tsukita S., and 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
    • 0032842426 scopus 로고    scopus 로고
    • Structural and signalling molecules come together at tight junctions
    • Tsukita S., Furuse M., and Itoh M. Structural and signalling molecules come together at tight junctions. Curr. Opin. Cell Biol. 11 (1999) 628-633
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 628-633
    • Tsukita, S.1    Furuse, M.2    Itoh, M.3
  • 6
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar M.G., and Palade G.E. Junctional complexes in various epithelia. J. Cell Biol. 17 (1963) 375-412
    • (1963) J. Cell Biol. , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 7
    • 0037032804 scopus 로고    scopus 로고
    • Composition and formation of intercellular junctions in epithelial cells
    • Knust E., and Bossinger O. Composition and formation of intercellular junctions in epithelial cells. Science 298 (2002) 1955-1959
    • (2002) Science , vol.298 , pp. 1955-1959
    • Knust, E.1    Bossinger, O.2
  • 9
    • 0034657319 scopus 로고    scopus 로고
    • Cadherin superfamily genes: functions, genomic organization, and neurologic diversity
    • Yagi T., and 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
  • 10
    • 23144442645 scopus 로고    scopus 로고
    • Regulation of cadherin-mediated adhesion in morphogenesis
    • Gumbiner B.M. Regulation of cadherin-mediated adhesion in morphogenesis. Nat. Rev., Mol. Cell Biol. 6 (2005) 622-634
    • (2005) Nat. Rev., Mol. Cell Biol. , vol.6 , pp. 622-634
    • Gumbiner, B.M.1
  • 11
    • 0037232646 scopus 로고    scopus 로고
    • Nectin and afadin: novel organizers of intercellular junctions
    • Takai Y., and 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
  • 12
    • 0141813527 scopus 로고    scopus 로고
    • Nectins and nectin-like molecules: roles in cell adhesion, migration, and polarization
    • Takai Y., Irie K., Shimizu K., Sakisaka T., and Ikeda W. Nectins and nectin-like molecules: roles in cell adhesion, migration, and polarization. Cancer Sci. 94 (2003) 655-667
    • (2003) Cancer Sci. , vol.94 , pp. 655-667
    • Takai, Y.1    Irie, K.2    Shimizu, K.3    Sakisaka, T.4    Ikeda, W.5
  • 14
    • 0034616002 scopus 로고    scopus 로고
    • Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities
    • Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M., Nishimura M., Tachibana K., Mizoguchi A., and Takai Y. Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities. J. Biol. Chem. 275 (2000) 10291-10299
    • (2000) J. Biol. Chem. , vol.275 , pp. 10291-10299
    • Satoh-Horikawa, K.1    Nakanishi, H.2    Takahashi, K.3    Miyahara, M.4    Nishimura, M.5    Tachibana, K.6    Mizoguchi, A.7    Takai, Y.8
  • 16
    • 14244268497 scopus 로고    scopus 로고
    • Separation force measurements reveal different types of modulation of E-cadherin-based adhesion by nectin-1 and -3
    • Martinez-Rico C., Pincet F., Perez E., Thiery J.P., Shimizu K., Takai Y., and Dufour S. Separation force measurements reveal different types of modulation of E-cadherin-based adhesion by nectin-1 and -3. J. Biol. Chem. 280 (2005) 4753-4760
    • (2005) J. Biol. Chem. , vol.280 , pp. 4753-4760
    • Martinez-Rico, C.1    Pincet, F.2    Perez, E.3    Thiery, J.P.4    Shimizu, K.5    Takai, Y.6    Dufour, S.7
  • 17
    • 0032498847 scopus 로고    scopus 로고
    • Cytoplasmic regulation of the movement of E-cadherin on the free cell surface as studied by optical tweezers and single particle tracking: corralling and tethering by the membrane skeleton
    • Sako Y., Nagafuchi A., Tsukita S., Takeichi M., and Kusumi A. Cytoplasmic regulation of the movement of E-cadherin on the free cell surface as studied by optical tweezers and single particle tracking: corralling and tethering by the membrane skeleton. J. Cell Biol. 140 (1998) 1227-1240
    • (1998) J. Cell Biol. , vol.140 , pp. 1227-1240
    • Sako, Y.1    Nagafuchi, A.2    Tsukita, S.3    Takeichi, M.4    Kusumi, A.5
  • 18
    • 11244352270 scopus 로고    scopus 로고
    • Force measurements in E-cadherin-mediated cell doublets reveal rapid adhesion strengthened by actin cytoskeleton remodeling through Rac and Cdc42
    • Chu Y.S., Thomas W.A., Eder O., Pincet F., Perez E., Thiery J.P., and Dufour S. Force measurements in E-cadherin-mediated cell doublets reveal rapid adhesion strengthened by actin cytoskeleton remodeling through Rac and Cdc42. J. Cell Biol. 167 (2004) 1183-1194
    • (2004) J. Cell Biol. , vol.167 , pp. 1183-1194
    • Chu, Y.S.1    Thomas, W.A.2    Eder, O.3    Pincet, F.4    Perez, E.5    Thiery, J.P.6    Dufour, S.7
  • 19
    • 0025752664 scopus 로고
    • The 102 kd cadherin-associated protein: similarity to vinculin and posttranscriptional regulation of expression
    • Nagafuchi A., Takeichi M., and Tsukita S. The 102 kd cadherin-associated protein: similarity to vinculin and posttranscriptional regulation of expression. Cell 65 (1991) 849-857
    • (1991) Cell , vol.65 , pp. 849-857
    • Nagafuchi, A.1    Takeichi, M.2    Tsukita, S.3
  • 21
    • 33947133738 scopus 로고    scopus 로고
    • The unique-5 and -6 motifs of ZO-1 regulate tight junction strand localization and scaffolding properties
    • Fanning A.S., Little B.P., Rahner C., Utepbergenov D., Walther Z., and Anderson J.M. The unique-5 and -6 motifs of ZO-1 regulate tight junction strand localization and scaffolding properties. Mol. Biol. Cell 18 (2007) 721-731
    • (2007) Mol. Biol. Cell , vol.18 , pp. 721-731
    • Fanning, A.S.1    Little, B.P.2    Rahner, C.3    Utepbergenov, D.4    Walther, Z.5    Anderson, J.M.6
  • 22
    • 1842390685 scopus 로고
    • Cell binding function of E-cadherin is regulated by the cytoplasmic domain
    • Nagafuchi A., and Takeichi M. Cell binding function of E-cadherin is regulated by the cytoplasmic domain. EMBO J. 7 (1988) 3679-3684
    • (1988) EMBO J. , vol.7 , pp. 3679-3684
    • Nagafuchi, A.1    Takeichi, M.2
  • 23
    • 0034695656 scopus 로고    scopus 로고
    • Directed actin polymerization is the driving force for epithelial cell-cell adhesion
    • Vasioukhin V., Bauer C., Yin M., and Fuchs E. Directed actin polymerization is the driving force for epithelial cell-cell adhesion. Cell 100 (2000) 209-219
    • (2000) Cell , vol.100 , pp. 209-219
    • Vasioukhin, V.1    Bauer, C.2    Yin, M.3    Fuchs, E.4
  • 26
    • 33745009493 scopus 로고    scopus 로고
    • Polychaetoid/ZO-1 is required for cell specification and rearrangement during Drosophila tracheal morphogenesis
    • Jung A.C., Ribeiro C., Michaut L., Certa U., and Affolter M. Polychaetoid/ZO-1 is required for cell specification and rearrangement during Drosophila tracheal morphogenesis. Curr. Biol. 16 (2006) 1224-1231
    • (2006) Curr. Biol. , vol.16 , pp. 1224-1231
    • Jung, A.C.1    Ribeiro, C.2    Michaut, L.3    Certa, U.4    Affolter, M.5
  • 27
    • 0035145414 scopus 로고    scopus 로고
    • Localization of the Drosophila MAGUK protein polychaetoid is controlled by alternative splicing
    • Wei X., and Ellis H.M. Localization of the Drosophila MAGUK protein polychaetoid is controlled by alternative splicing. Mech. Dev. 100 (2001) 217-231
    • (2001) Mech. Dev. , vol.100 , pp. 217-231
    • Wei, X.1    Ellis, H.M.2
  • 28
    • 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
  • 29
    • 0035479827 scopus 로고    scopus 로고
    • Molecular architecture of adherens junctions
    • Nagafuchi A. Molecular architecture of adherens junctions. Curr. Opin. Cell Biol. 13 (2001) 600-603
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 600-603
    • Nagafuchi, A.1
  • 30
    • 0037459077 scopus 로고    scopus 로고
    • Sticky business: orchestrating cellular signals at adherens junctions
    • Perez-Moreno M., Jamora C., and 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
  • 31
    • 0033535163 scopus 로고    scopus 로고
    • Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions
    • Mandai K., Nakanishi H., Satoh A., Takahashi K., Satoh K., Nishioka H., Mizoguchi A., and Takai Y. Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions. J. Cell Biol. 144 (1999) 1001-1017
    • (1999) J. Cell Biol. , vol.144 , pp. 1001-1017
    • Mandai, K.1    Nakanishi, H.2    Satoh, A.3    Takahashi, K.4    Satoh, K.5    Nishioka, H.6    Mizoguchi, A.7    Takai, Y.8
  • 32
    • 0037423380 scopus 로고    scopus 로고
    • ADIP, a novel afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions
    • Asada M., Irie K., Morimoto K., Yamada A., Ikeda W., Takeuchi M., and Takai Y. ADIP, a novel afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions. J. Biol. Chem. 278 (2003) 4103-4111
    • (2003) J. Biol. Chem. , vol.278 , pp. 4103-4111
    • Asada, M.1    Irie, K.2    Morimoto, K.3    Yamada, A.4    Ikeda, W.5    Takeuchi, M.6    Takai, Y.7
  • 33
    • 3242743242 scopus 로고    scopus 로고
    • Involvement of LMO7 in the association of two cell-cell adhesion molecules, nectin and E-cadherin, through afadin and alpha-actinin in epithelial cells
    • Ooshio T., Irie K., Morimoto K., Fukuhara A., Imai T., and Takai Y. Involvement of LMO7 in the association of two cell-cell adhesion molecules, nectin and E-cadherin, through afadin and alpha-actinin in epithelial cells. J. Biol. Chem. 279 (2004) 31365-31373
    • (2004) J. Biol. Chem. , vol.279 , pp. 31365-31373
    • Ooshio, T.1    Irie, K.2    Morimoto, K.3    Fukuhara, A.4    Imai, T.5    Takai, Y.6
  • 34
    • 33746363486 scopus 로고    scopus 로고
    • Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits
    • Bhattacharyya R.P., Remenyi A., Yeh B.J., and Lim W.A. Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits. Annu. Rev. Biochem. 75 (2006) 655-680
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 655-680
    • Bhattacharyya, R.P.1    Remenyi, A.2    Yeh, B.J.3    Lim, W.A.4
  • 37
    • 0037147288 scopus 로고    scopus 로고
    • Impaired trafficking of connexins in androgen-independent human prostate cancer cell lines and its mitigation by alpha-catenin
    • Govindarajan R., Zhao S., Song X.H., Guo R.J., Wheelock M., Johnson K.R., and Mehta P.P. Impaired trafficking of connexins in androgen-independent human prostate cancer cell lines and its mitigation by alpha-catenin. J. Biol. Chem. 277 (2002) 50087-50097
    • (2002) J. Biol. Chem. , vol.277 , pp. 50087-50097
    • Govindarajan, R.1    Zhao, S.2    Song, X.H.3    Guo, R.J.4    Wheelock, M.5    Johnson, K.R.6    Mehta, P.P.7
  • 38
    • 33644875413 scopus 로고    scopus 로고
    • Identification of regions of alpha-catenin required for desmosome organization in epithelial cells
    • Taniguchi T., Miyazaki M., Miyashita Y., Arima T., and Ozawa M. Identification of regions of alpha-catenin required for desmosome organization in epithelial cells. Int. J. Mol. Med. 16 (2005) 1003-1008
    • (2005) Int. J. Mol. Med. , vol.16 , pp. 1003-1008
    • Taniguchi, T.1    Miyazaki, M.2    Miyashita, Y.3    Arima, T.4    Ozawa, M.5
  • 39
    • 0030748548 scopus 로고    scopus 로고
    • Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments
    • Itoh M., Nagafuchi A., Moroi S., and Tsukita S. Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments. J. Cell Biol. Jul 138 (1997) 181-192
    • (1997) J. Cell Biol. Jul , vol.138 , pp. 181-192
    • Itoh, M.1    Nagafuchi, A.2    Moroi, S.3    Tsukita, S.4
  • 40
    • 0030724368 scopus 로고    scopus 로고
    • The Ras target AF-6 interacts with ZO-1 and serves as a peripheral component of tight junctions in epithelial cells
    • Yamamoto T., Harada N., Kano K., Taya S., Canaani E., Matsuura Y., Mizoguchi A., Ide C., and Kaibuchi K. The Ras target AF-6 interacts with ZO-1 and serves as a peripheral component of tight junctions in epithelial cells. J. Cell Biol. 139 (1997) 785-795
    • (1997) J. Cell Biol. , vol.139 , pp. 785-795
    • Yamamoto, T.1    Harada, N.2    Kano, K.3    Taya, S.4    Canaani, E.5    Matsuura, Y.6    Mizoguchi, A.7    Ide, C.8    Kaibuchi, K.9
  • 43
    • 3543148258 scopus 로고    scopus 로고
    • Alpha-catenin: at the junction of intercellular adhesion and actin dynamics
    • Kobielak A., and Fuchs E. Alpha-catenin: at the junction of intercellular adhesion and actin dynamics. Nat. Rev., Mol. Cell Biol. 5 (2004) 614-625
    • (2004) Nat. Rev., Mol. Cell Biol. , vol.5 , pp. 614-625
    • Kobielak, A.1    Fuchs, E.2
  • 44
    • 34250722594 scopus 로고    scopus 로고
    • p120-catenin regulates microtubule dynamics and cell migration in a cadherin-independent manner
    • Ichii T., and Takeichi M. p120-catenin regulates microtubule dynamics and cell migration in a cadherin-independent manner. Genes Cells 12 (2007) 827-839
    • (2007) Genes Cells , vol.12 , pp. 827-839
    • Ichii, T.1    Takeichi, M.2
  • 45
    • 1942503184 scopus 로고    scopus 로고
    • Gap junctions and connexin-interacting proteins
    • Giepmans B. Gap junctions and connexin-interacting proteins. Cardiovasc. Res. 62 (2004) 233-245
    • (2004) Cardiovasc. Res. , vol.62 , pp. 233-245
    • Giepmans, B.1
  • 46
    • 0031658385 scopus 로고    scopus 로고
    • Integrins, cadherins, and catenins: molecular cross-talk in cancer cells
    • Pignatelli M. Integrins, cadherins, and catenins: molecular cross-talk in cancer cells. J. Pathol. 186 (1998) 1-2
    • (1998) J. Pathol. , vol.186 , pp. 1-2
    • Pignatelli, M.1
  • 47
    • 4644328373 scopus 로고    scopus 로고
    • Dynamic cross-talk between cells and the extracellular matrix in the testis
    • Siu M.K., and Cheng C.Y. Dynamic cross-talk between cells and the extracellular matrix in the testis. Bioessays 26 (2004) 978-992
    • (2004) Bioessays , vol.26 , pp. 978-992
    • Siu, M.K.1    Cheng, C.Y.2
  • 48
    • 0037032828 scopus 로고    scopus 로고
    • Shaping the vertebrate body plan by polarized embryonic cell movements
    • Keller R. Shaping the vertebrate body plan by polarized embryonic cell movements. Science 298 (2002) 1950-1954
    • (2002) Science , vol.298 , pp. 1950-1954
    • Keller, R.1
  • 49
    • 0037428084 scopus 로고    scopus 로고
    • Tube morphogenesis: making and shaping biological tubes
    • Lubarsky B., and Krasnow M.A. Tube morphogenesis: making and shaping biological tubes. Cell 112 (2003) 19-28
    • (2003) Cell , vol.112 , pp. 19-28
    • Lubarsky, B.1    Krasnow, M.A.2
  • 50
    • 33847389353 scopus 로고    scopus 로고
    • Abelson kinase (Abl) and RhoGEF2 regulate actin organization during cell constriction in Drosophila
    • Fox D.T., and Peifer M. Abelson kinase (Abl) and RhoGEF2 regulate actin organization during cell constriction in Drosophila. Development 134 (2007) 567-578
    • (2007) Development , vol.134 , pp. 567-578
    • Fox, D.T.1    Peifer, M.2
  • 52
    • 0037033804 scopus 로고    scopus 로고
    • Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion
    • Calautti E., Grossi M., Mammucari C., Aoyama Y., Pirro M., Ono Y., Li J., and Dotto G.P. Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion. J. Cell Biol. 156 (2002) 137-148
    • (2002) J. Cell Biol. , vol.156 , pp. 137-148
    • Calautti, E.1    Grossi, M.2    Mammucari, C.3    Aoyama, Y.4    Pirro, M.5    Ono, Y.6    Li, J.7    Dotto, G.P.8
  • 53
    • 0038054266 scopus 로고    scopus 로고
    • Regulation by nectin of the velocity of the formation of adherens junctions and tight junctions
    • Honda T., Shimizu K., Fukuhara A., Irie K., and Takai Y. Regulation by nectin of the velocity of the formation of adherens junctions and tight junctions. Biochem. Biophys. Res. Commun. 306 (2003) 104-109
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 104-109
    • Honda, T.1    Shimizu, K.2    Fukuhara, A.3    Irie, K.4    Takai, Y.5
  • 54
    • 24344457031 scopus 로고    scopus 로고
    • Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis
    • Shen L., and Turner J.R. Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis. Mol. Bio. Cell 16 (2005) 3919-3936
    • (2005) Mol. Bio. Cell , vol.16 , pp. 3919-3936
    • Shen, L.1    Turner, J.R.2
  • 55
    • 33846847697 scopus 로고    scopus 로고
    • Rac-WAVE-mediated actin reorganization is required for organization and maintenance of cell-cell adhesion
    • Yamazaki D., Oikawa T., and Takenawa T. Rac-WAVE-mediated actin reorganization is required for organization and maintenance of cell-cell adhesion. J. Cell Sci. 120 (2007) 86-100
    • (2007) J. Cell Sci. , vol.120 , pp. 86-100
    • Yamazaki, D.1    Oikawa, T.2    Takenawa, T.3
  • 56
    • 0033403506 scopus 로고    scopus 로고
    • Establishment of the circumferential actin filament network is a prerequisite for localization of the cadherin-catenin complex in epithelial cells
    • Quinlan M.P., and Hyatt J.L. Establishment of the circumferential actin filament network is a prerequisite for localization of the cadherin-catenin complex in epithelial cells. Cell Growth. Differ. 10 (1999) 839-854
    • (1999) Cell Growth. Differ. , vol.10 , pp. 839-854
    • Quinlan, M.P.1    Hyatt, J.L.2
  • 57
    • 0027323552 scopus 로고
    • The product of the Drosophila segment polarity gene armadillo is part of a multi-protein complex resembling the vertebrate adherens junction
    • Peifer M. The product of the Drosophila segment polarity gene armadillo is part of a multi-protein complex resembling the vertebrate adherens junction. J. Cell Sci. 105 (1993) 993-1000
    • (1993) J. Cell Sci. , vol.105 , pp. 993-1000
    • Peifer, M.1
  • 58
    • 0030014526 scopus 로고    scopus 로고
    • Armadillo is required for adherens junction assembly, cell polarity, and morphogenesis during Drosophila embryogenesis
    • Cox R.T., Kirkpatrick C., and Peifer M. Armadillo is required for adherens junction assembly, cell polarity, and morphogenesis during Drosophila embryogenesis. J. Cell Biol. 134 (1996) 133-148
    • (1996) J. Cell Biol. , vol.134 , pp. 133-148
    • Cox, R.T.1    Kirkpatrick, C.2    Peifer, M.3
  • 59
    • 28344433073 scopus 로고    scopus 로고
    • Deconstructing the cadherin-catenin-actin complex
    • Yamada S., Pokutta S., Drees F., Weis W.I., and Nelson W.J. Deconstructing the cadherin-catenin-actin complex. Cell 123 (2005) 889-901
    • (2005) Cell , vol.123 , pp. 889-901
    • Yamada, S.1    Pokutta, S.2    Drees, F.3    Weis, W.I.4    Nelson, W.J.5
  • 60
    • 0032563564 scopus 로고    scopus 로고
    • Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein
    • Adams C.L., Chen Y.T., Smith S.J., and Nelson W.J. Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein. J. Cell Biol. 142 (1998) 1105-1119
    • (1998) J. Cell Biol. , vol.142 , pp. 1105-1119
    • Adams, C.L.1    Chen, Y.T.2    Smith, S.J.3    Nelson, W.J.4
  • 61
    • 0036696823 scopus 로고    scopus 로고
    • Spatio-temporal regulation of Rac1 localization and lamellipodia dynamics during epithelial cell-cell adhesion
    • Ehrlich J.S., Hansen M.D., and Nelson W.J. Spatio-temporal regulation of Rac1 localization and lamellipodia dynamics during epithelial cell-cell adhesion. Dev. Cell 3 (2002) 259-270
    • (2002) Dev. Cell , vol.3 , pp. 259-270
    • Ehrlich, J.S.1    Hansen, M.D.2    Nelson, W.J.3
  • 62
    • 0036746704 scopus 로고    scopus 로고
    • Actin cable dynamics and Rho/Rock orchestrate a polarized cytoskeletal architecture in the early steps of assembling a stratified epithelium
    • Vaezi A., Bauer C., Vasioukhin V., and Fuchs E. Actin cable dynamics and Rho/Rock orchestrate a polarized cytoskeletal architecture in the early steps of assembling a stratified epithelium. Dev. Cell 3 (2002) 367-381
    • (2002) Dev. Cell , vol.3 , pp. 367-381
    • Vaezi, A.1    Bauer, C.2    Vasioukhin, V.3    Fuchs, E.4
  • 63
    • 33846065117 scopus 로고    scopus 로고
    • Depletion of E-cadherin disrupts establishment but not maintenance of cell junctions in Madin-Darby canine kidney epithelial cells
    • Capaldo C.T., and Macara I.G. Depletion of E-cadherin disrupts establishment but not maintenance of cell junctions in Madin-Darby canine kidney epithelial cells. Mol. Biol. Cell 18 (2007) 189-200
    • (2007) Mol. Biol. Cell , vol.18 , pp. 189-200
    • Capaldo, C.T.1    Macara, I.G.2
  • 64
    • 4444253507 scopus 로고    scopus 로고
    • Requirement of the actin cytoskeleton for the association of nectins with other cell adhesion molecules at adherens and tight junctions in MDCK cells
    • Yamada A., Irie K., Fukuhara A., Ooshio T., and Takai Y. Requirement of the actin cytoskeleton for the association of nectins with other cell adhesion molecules at adherens and tight junctions in MDCK cells. Genes Cells 9 (2004) 843-855
    • (2004) Genes Cells , vol.9 , pp. 843-855
    • Yamada, A.1    Irie, K.2    Fukuhara, A.3    Ooshio, T.4    Takai, Y.5
  • 65
    • 33745269374 scopus 로고    scopus 로고
    • Zonula occludens-1 function in the assembly of tight junctions in Madin-Darby canine kidney epithelial cells
    • McNeil E., Capaldo C.T., and Macara I.G. Zonula occludens-1 function in the assembly of tight junctions in Madin-Darby canine kidney epithelial cells. Mol. Biol. Cell 17 (2006) 1922-1932
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1922-1932
    • McNeil, E.1    Capaldo, C.T.2    Macara, I.G.3
  • 66
    • 28344446744 scopus 로고    scopus 로고
    • Can 1000 reviews be wrong? Actin, alpha-catenin, and adherens junctions
    • Gates J., and Peifer M. Can 1000 reviews be wrong? Actin, alpha-catenin, and adherens junctions. Cell 123 (2005) 769-772
    • (2005) Cell , vol.123 , pp. 769-772
    • Gates, J.1    Peifer, M.2
  • 67
    • 33644748151 scopus 로고    scopus 로고
    • A break in the chain?
    • Burridge K. A break in the chain?. Nature 440 (2006) 38-39
    • (2006) Nature , vol.440 , pp. 38-39
    • Burridge, K.1
  • 69
    • 2642579936 scopus 로고    scopus 로고
    • Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex
    • Millard T.H., Sharp S.J., and Machesky L.M. Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex. Biochem. J. 380 (2004) 1-17
    • (2004) Biochem. J. , vol.380 , pp. 1-17
    • Millard, T.H.1    Sharp, S.J.2    Machesky, L.M.3
  • 71
  • 74
    • 0033965314 scopus 로고    scopus 로고
    • Control of actin assembly and disassembly at filament ends
    • Cooper J.A., and Schafer D.A. Control of actin assembly and disassembly at filament ends. Curr. Opin. Cell Biol. 12 (2000) 97-103
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 97-103
    • Cooper, J.A.1    Schafer, D.A.2
  • 75
    • 0033198879 scopus 로고    scopus 로고
    • Putting a new twist on actin: ADF/cofilins modulate actin dynamics
    • Bamburg J.R., McGough A., and Ono S. Putting a new twist on actin: ADF/cofilins modulate actin dynamics. Trends Cell Biol. 9 (1999) 364-370
    • (1999) Trends Cell Biol. , vol.9 , pp. 364-370
    • Bamburg, J.R.1    McGough, A.2    Ono, S.3
  • 76
    • 34547796327 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5 bisphosphate produced by PIP5KIgamma regulates gelsolin, actin assembly, and adhesion strength of N-cadherin junctions
    • El Sayegh T.Y., Arora P.D., Ling K., Laschinger C., Janmey P.A., Anderson R.A., and McCulloch C.A. Phosphatidylinositol-4,5 bisphosphate produced by PIP5KIgamma regulates gelsolin, actin assembly, and adhesion strength of N-cadherin junctions. Mol. Biol. Cell 18 (2007) 3026-3038
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3026-3038
    • El Sayegh, T.Y.1    Arora, P.D.2    Ling, K.3    Laschinger, C.4    Janmey, P.A.5    Anderson, R.A.6    McCulloch, C.A.7
  • 77
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard T.D., and Borisy G.G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112 (2003) 453-465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 78
  • 79
    • 0022390903 scopus 로고
    • Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling
    • Wang Y. Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J. Cell Biol. 101 (1985) 597-602
    • (1985) J. Cell Biol. , vol.101 , pp. 597-602
    • Wang, Y.1
  • 81
    • 34547571737 scopus 로고    scopus 로고
    • Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion
    • Yamada S., and Nelson W.J. Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion. J. Cell Biol. 178 (2007) 517-527
    • (2007) J. Cell Biol. , vol.178 , pp. 517-527
    • Yamada, S.1    Nelson, W.J.2
  • 82
    • 33847701706 scopus 로고    scopus 로고
    • Role of multiple bonds between the single cell adhesion molecules, nectin and cadherin, revealed by high sensitive force measurements
    • Tsukasaki Y., Kitamura K., Shimizu K., Iwane A.H., Takai Y., and Yanagida T. Role of multiple bonds between the single cell adhesion molecules, nectin and cadherin, revealed by high sensitive force measurements. J. Mol. Biol. 367 (2007) 996-1006
    • (2007) J. Mol. Biol. , vol.367 , pp. 996-1006
    • Tsukasaki, Y.1    Kitamura, K.2    Shimizu, K.3    Iwane, A.H.4    Takai, Y.5    Yanagida, T.6
  • 83
    • 33846309701 scopus 로고    scopus 로고
    • Integrins and the actin cytoskeleton
    • Delon I., and Brown N.H. Integrins and the actin cytoskeleton. Curr. Opin. Cell Biol. 19 (2007) 43-50
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 43-50
    • Delon, I.1    Brown, N.H.2
  • 84
    • 0027333420 scopus 로고
    • Life at the leading edge: the formation of cell protrusions
    • Condeelis J. Life at the leading edge: the formation of cell protrusions. Annu. Rev. Cell Biol. 9 (1993) 411-444
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 411-444
    • Condeelis, J.1
  • 85
    • 0030021649 scopus 로고    scopus 로고
    • Signal transduction and actin filament organization
    • Zigmond S.H. Signal transduction and actin filament organization. Curr. Opin. Cell Biol. 8 (1996) 66-73
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 66-73
    • Zigmond, S.H.1
  • 86
    • 34248227301 scopus 로고    scopus 로고
    • Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin monomers
    • Kiuchi T., Ohashi K., Kurita S., and Mizuno K. Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin monomers. J. Cell Biol. 177 (2007) 465-476
    • (2007) J. Cell Biol. , vol.177 , pp. 465-476
    • Kiuchi, T.1    Ohashi, K.2    Kurita, S.3    Mizuno, K.4
  • 87
    • 0022476930 scopus 로고
    • Probing the mechanism of incorporation of fluorescently labeled actin into stress fibers
    • Amato P.A., and Taylor D.L. Probing the mechanism of incorporation of fluorescently labeled actin into stress fibers. J. Cell Biol. 102 (1986) 1074-1084
    • (1986) J. Cell Biol. , vol.102 , pp. 1074-1084
    • Amato, P.A.1    Taylor, D.L.2
  • 88
    • 0025740949 scopus 로고
    • Actin microfilament dynamics in locomoting cells
    • Theriot J.A., and Mitchison T.J. Actin microfilament dynamics in locomoting cells. Nature 352 (1991) 126-131
    • (1991) Nature , vol.352 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 89
    • 0031660704 scopus 로고    scopus 로고
    • Simultaneous measurements of actin filament turnover, filament fraction, and monomer diffusion in endothelial cells
    • Mcgrath J.L., Tardy Y., Dewey Jr. C.F., Meister J.J., and Hartwig J.H. Simultaneous measurements of actin filament turnover, filament fraction, and monomer diffusion in endothelial cells. Biophys. J. 75 (1998) 2070-2078
    • (1998) Biophys. J. , vol.75 , pp. 2070-2078
    • Mcgrath, J.L.1    Tardy, Y.2    Dewey Jr., C.F.3    Meister, J.J.4    Hartwig, J.H.5
  • 90
    • 1342310742 scopus 로고    scopus 로고
    • Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables
    • Kobielak A., Pasolli H.A., and Fuchs E. Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables. Nat. Cell Biol. 6 (2004) 21-30
    • (2004) Nat. Cell Biol. , vol.6 , pp. 21-30
    • Kobielak, A.1    Pasolli, H.A.2    Fuchs, E.3
  • 92
    • 0037022538 scopus 로고    scopus 로고
    • Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts
    • Kovacs E.M., Goodwin M., Ali R.G., Paterson A.D., and Yap A.S. Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts. Curr. Biol. 12 (2002) 379-382
    • (2002) Curr. Biol. , vol.12 , pp. 379-382
    • Kovacs, E.M.1    Goodwin, M.2    Ali, R.G.3    Paterson, A.D.4    Yap, A.S.5
  • 93
    • 28344439885 scopus 로고    scopus 로고
    • Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly
    • Drees F., Pokutta S., Yamada S., Nelson W.J., and Weis W.I. Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. Cell 123 (2005) 903-915
    • (2005) Cell , vol.123 , pp. 903-915
    • Drees, F.1    Pokutta, S.2    Yamada, S.3    Nelson, W.J.4    Weis, W.I.5
  • 94
    • 0028087729 scopus 로고
    • The roles of catenins in the cadherin-mediated cell adhesion: functional analysis of E-cadherin-alpha catenin fusion molecules
    • Nagafuchi A., Ishihara S., and Tsukita S. The roles of catenins in the cadherin-mediated cell adhesion: functional analysis of E-cadherin-alpha catenin fusion molecules. J. Cell Biol. 127 (1994) 235-245
    • (1994) J. Cell Biol. , vol.127 , pp. 235-245
    • Nagafuchi, A.1    Ishihara, S.2    Tsukita, S.3
  • 95
    • 85058203804 scopus 로고    scopus 로고
    • Actin regulators I
    • Siripara A.D., and Welch M.D. Actin regulators I. Cell 128 (2007) 626
    • (2007) Cell , vol.128 , pp. 626
    • Siripara, A.D.1    Welch, M.D.2
  • 96
    • 85058203804 scopus 로고    scopus 로고
    • Actin regulators II
    • Siripara A.D., and Welch M.D. Actin regulators II. Cell 128 (2007) 1014
    • (2007) Cell , vol.128 , pp. 1014
    • Siripara, A.D.1    Welch, M.D.2
  • 98
    • 0035140977 scopus 로고    scopus 로고
    • Actin dynamics and cell-cell adhesion in epithelia
    • Vasioukhin V., and Fuchs E. Actin dynamics and cell-cell adhesion in epithelia. Curr. Opin. Cell Biol. 13 (2001) 76-84
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 76-84
    • Vasioukhin, V.1    Fuchs, E.2
  • 101
    • 33749037156 scopus 로고    scopus 로고
    • The ARP2/3 complex: an actin nucleator comes of age
    • Goley E.D., and Welch M.D. The ARP2/3 complex: an actin nucleator comes of age. Nat. Rev., Mol. Cell Biol. 7 (2006) 713-726
    • (2006) Nat. Rev., Mol. Cell Biol. , vol.7 , pp. 713-726
    • Goley, E.D.1    Welch, M.D.2
  • 102
    • 0036899582 scopus 로고    scopus 로고
    • The web and the rock: cell adhesion and the ARP2/3 complex
    • Kovacs E.M., and Yap A.S. The web and the rock: cell adhesion and the ARP2/3 complex. Dev. Cell 3 (2002) 760-761
    • (2002) Dev. Cell , vol.3 , pp. 760-761
    • Kovacs, E.M.1    Yap, A.S.2
  • 104
    • 6344258806 scopus 로고    scopus 로고
    • Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor
    • Goley E.D., Rodenbusch S.E., Martin A.C., and Welch M.D. Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor. Mol. Cell 16 (2004) 269-279
    • (2004) Mol. Cell , vol.16 , pp. 269-279
    • Goley, E.D.1    Rodenbusch, S.E.2    Martin, A.C.3    Welch, M.D.4
  • 106
    • 0037343053 scopus 로고    scopus 로고
    • A dynamin-cortactin-Arp2/3 complex mediates actin reorganization in growth factor-stimulated cells
    • Krueger E.W., Orth J.D., Cao H., and McNiven M.A. A dynamin-cortactin-Arp2/3 complex mediates actin reorganization in growth factor-stimulated cells. Mol. Biol. Cell 14 (2003) 1085-1096
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1085-1096
    • Krueger, E.W.1    Orth, J.D.2    Cao, H.3    McNiven, M.A.4
  • 107
    • 0027419589 scopus 로고
    • Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex
    • Wu H., and Parsons J.T. Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J. Cell Biol. 120 (1993) 1417-1426
    • (1993) J. Cell Biol. , vol.120 , pp. 1417-1426
    • Wu, H.1    Parsons, J.T.2
  • 108
    • 0035475450 scopus 로고    scopus 로고
    • Cortactin: coupling membrane dynamics to cortical actin assembly
    • Weed S.A., and Parsons J.T. Cortactin: coupling membrane dynamics to cortical actin assembly. Oncogene 20 (2001) 6418-6434
    • (2001) Oncogene , vol.20 , pp. 6418-6434
    • Weed, S.A.1    Parsons, J.T.2
  • 109
    • 0034597092 scopus 로고    scopus 로고
    • Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex
    • Weed S.A., Karginov A.V., Schafer D.A., Weaver A.M., Kinley A.W., Cooper J.A., and Parsons J.T. Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex. J. Cell Biol. 151 (2000) 29-40
    • (2000) J. Cell Biol. , vol.151 , pp. 29-40
    • Weed, S.A.1    Karginov, A.V.2    Schafer, D.A.3    Weaver, A.M.4    Kinley, A.W.5    Cooper, J.A.6    Parsons, J.T.7
  • 110
    • 0037810840 scopus 로고    scopus 로고
    • Dual regulation of neuronal morphogenesis by a delta-catenin-cortactin complex and Rho
    • Martinez M.C., Ochiishi T., Majewski M., and Kosik K.S. Dual regulation of neuronal morphogenesis by a delta-catenin-cortactin complex and Rho. J. Cell Biol. 162 (2003) 99-111
    • (2003) J. Cell Biol. , vol.162 , pp. 99-111
    • Martinez, M.C.1    Ochiishi, T.2    Majewski, M.3    Kosik, K.S.4
  • 114
    • 0037160142 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 291 enhances the ability of WASP to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich syndrome protein
    • Cory G.O., Garg R., Cramer R., and Ridley A.J. Phosphorylation of tyrosine 291 enhances the ability of WASP to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich syndrome protein. J. Biol. Chem. 277 (2002) 45115-45121
    • (2002) J. Biol. Chem. , vol.277 , pp. 45115-45121
    • Cory, G.O.1    Garg, R.2    Cramer, R.3    Ridley, A.J.4
  • 115
    • 0038392871 scopus 로고    scopus 로고
    • Contingent phosphorylation/dephosphorylation provides a mechanism of molecular memory in WASP
    • Torres E., and Rosen M.K. Contingent phosphorylation/dephosphorylation provides a mechanism of molecular memory in WASP. Mol. Cell 11 (2003) 1215-1227
    • (2003) Mol. Cell , vol.11 , pp. 1215-1227
    • Torres, E.1    Rosen, M.K.2
  • 116
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden S., Rohatgi R., Podtelejnikov A.V., Mann M., and Kirschner M.W. Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 418 (2002) 790-793
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 117
    • 33646763140 scopus 로고    scopus 로고
    • Optimization of WAVE2-complexinduced actin polymerization by membrane-bound IRSp53, PIP3, and Rac
    • Suetsugu S., Kurisu S., Oikawa T., Yamazaki D., Oda A., and Takenawa T. Optimization of WAVE2-complexinduced actin polymerization by membrane-bound IRSp53, PIP3, and Rac. J. Cell Biol. 173 (2006) 571-585
    • (2006) J. Cell Biol. , vol.173 , pp. 571-585
    • Suetsugu, S.1    Kurisu, S.2    Oikawa, T.3    Yamazaki, D.4    Oda, A.5    Takenawa, T.6
  • 118
    • 33845729059 scopus 로고    scopus 로고
    • The WASP-WAVE protein network: connecting the membrane to the cytoskeleton
    • Takenawa T., and Suetsugu S. The WASP-WAVE protein network: connecting the membrane to the cytoskeleton. Nat. Rev., Mol. Cell Biol. 8 (2007) 37-48
    • (2007) Nat. Rev., Mol. Cell Biol. , vol.8 , pp. 37-48
    • Takenawa, T.1    Suetsugu, S.2
  • 119
    • 20444426470 scopus 로고    scopus 로고
    • The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia
    • Schirenbeck A., Bretschneider T., Arasada R., Schleicher M., and Faix J. The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia. Nature Cell Biol. 7 (2005) 619-625
    • (2005) Nature Cell Biol. , vol.7 , pp. 619-625
    • Schirenbeck, A.1    Bretschneider, T.2    Arasada, R.3    Schleicher, M.4    Faix, J.5
  • 120
    • 34248154652 scopus 로고    scopus 로고
    • Mechanism and function of formins in the control of actin assembly
    • Goode B.L., and Eck M.J. Mechanism and function of formins in the control of actin assembly. Annu. Rev. Biochem. 76 (2007) 32.1-32.35
    • (2007) Annu. Rev. Biochem. , vol.76
    • Goode, B.L.1    Eck, M.J.2
  • 121
    • 14844288286 scopus 로고    scopus 로고
    • Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1
    • Li F., and Higgs H.N. Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1. J. Biol. Chem. 280 (2005) 6986-6992
    • (2005) J. Biol. Chem. , vol.280 , pp. 6986-6992
    • Li, F.1    Higgs, H.N.2
  • 122
    • 19544386803 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the interaction between Rho and mammalian Dia
    • Rose R., Weyand M., Lammers M., Ishizaki T., Ahmadian M.R., and Wittinghofer A. Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature 435 (2005) 513-518
    • (2005) Nature , vol.435 , pp. 513-518
    • Rose, R.1    Weyand, M.2    Lammers, M.3    Ishizaki, T.4    Ahmadian, M.R.5    Wittinghofer, A.6
  • 123
    • 28644442126 scopus 로고    scopus 로고
    • The regulation of mDia1 by autoinhibition and its release by Rho-GTP
    • Lammers M., Rose R., Scrima A., and Wittinghofer A. The regulation of mDia1 by autoinhibition and its release by Rho-GTP. EMBO J. 24 (2005) 4176-4187
    • (2005) EMBO J. , vol.24 , pp. 4176-4187
    • Lammers, M.1    Rose, R.2    Scrima, A.3    Wittinghofer, A.4
  • 124
    • 32044470440 scopus 로고    scopus 로고
    • Structure of the autoinhibitory switch in formin mDia1
    • Nezami A.G., Poy F., and Eck M.J. Structure of the autoinhibitory switch in formin mDia1. Structure 14 (2006) 257-263
    • (2006) Structure , vol.14 , pp. 257-263
    • Nezami, A.G.1    Poy, F.2    Eck, M.J.3
  • 125
    • 30844449003 scopus 로고    scopus 로고
    • Molecular details of formin-mediated actin assembly
    • Kovar D.R. Molecular details of formin-mediated actin assembly. Curr. Opin. Cell Biol. 18 (2006) 11-17
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 11-17
    • Kovar, D.R.1
  • 126
    • 0036086782 scopus 로고    scopus 로고
    • Looking over the edge: a new role for Ena/VASP proteins in lamellipodial dynamics
    • Sutherland J.D., and Way M. Looking over the edge: a new role for Ena/VASP proteins in lamellipodial dynamics. Dev. Cell 2 (2002) 692-694
    • (2002) Dev. Cell , vol.2 , pp. 692-694
    • Sutherland, J.D.1    Way, M.2
  • 132
    • 33644865002 scopus 로고    scopus 로고
    • Ena/VASP proteins can regulate distinct modes of actin organization at cadherin-adhesive contacts
    • Scott J.A., Shewan A.M., den Elzen N.R., Loureiro J.J., Gertler F.B., and Yap A.S. Ena/VASP proteins can regulate distinct modes of actin organization at cadherin-adhesive contacts. Mol. Biol. Cell 17 (2006) 1085-1095
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1085-1095
    • Scott, J.A.1    Shewan, A.M.2    den Elzen, N.R.3    Loureiro, J.J.4    Gertler, F.B.5    Yap, A.S.6
  • 133
    • 36849032329 scopus 로고    scopus 로고
    • Claudin-16 is directly phosphorylated by protein kinase a independently of a vasodilator-stimulated phosphoprotein-mediated pathway
    • Ikari A., Ito M., Okude C., Sawada H., Harada H., Degawa M., Sakai H., Takahashi T., Sugatani J., and Miwa M. Claudin-16 is directly phosphorylated by protein kinase a independently of a vasodilator-stimulated phosphoprotein-mediated pathway. J. Cell Physiol. 214 (2007) 221-229
    • (2007) J. Cell Physiol. , vol.214 , pp. 221-229
    • Ikari, A.1    Ito, M.2    Okude, C.3    Sawada, H.4    Harada, H.5    Degawa, M.6    Sakai, H.7    Takahashi, T.8    Sugatani, J.9    Miwa, M.10
  • 134
    • 39949083996 scopus 로고    scopus 로고
    • V. Niggli, J. Rossy, Ezrin/radixin/moesin: versatile controllers of signaling molecules and of the cortical cytoskeleton, Int. J. Biochem. Cell Biol. (in press).
    • V. Niggli, J. Rossy, Ezrin/radixin/moesin: versatile controllers of signaling molecules and of the cortical cytoskeleton, Int. J. Biochem. Cell Biol. (in press).
  • 136
    • 26244455734 scopus 로고    scopus 로고
    • Myosin 2 is a key Rho kinase target necessary for the local concentration of E-cadherin at cell-cell contacts
    • Shewan A.M., Maddugoda M., Kraemer A., Stehbens S.J., Verma S., Kovacs E.M., and Yap A.S. Myosin 2 is a key Rho kinase target necessary for the local concentration of E-cadherin at cell-cell contacts. Mol. Biol. Cell 16 (2005) 4531-4532
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4531-4532
    • Shewan, A.M.1    Maddugoda, M.2    Kraemer, A.3    Stehbens, S.J.4    Verma, S.5    Kovacs, E.M.6    Yap, A.S.7
  • 137
    • 33846019622 scopus 로고    scopus 로고
    • Two distinct modes of myosin assembly and dynamics during epithelial wound closure
    • Tamada M., Perez T.D., Nelson W.J., and Sheetz M.P. Two distinct modes of myosin assembly and dynamics during epithelial wound closure. J. Cell Biol. 176 (2007) 27-33
    • (2007) J. Cell Biol. , vol.176 , pp. 27-33
    • Tamada, M.1    Perez, T.D.2    Nelson, W.J.3    Sheetz, M.P.4
  • 138
    • 34547591456 scopus 로고    scopus 로고
    • Myosin VI and vinculin cooperate during the morphogenesis of cadherin cell-cell contacts in mammalian epithelial cells
    • Maddugoda M.P., Crampton M.S., Shewan A.M., and Yap A.S. Myosin VI and vinculin cooperate during the morphogenesis of cadherin cell-cell contacts in mammalian epithelial cells. J. Cell Biology 178 (2007) 529-540
    • (2007) J. Cell Biology , vol.178 , pp. 529-540
    • Maddugoda, M.P.1    Crampton, M.S.2    Shewan, A.M.3    Yap, A.S.4
  • 139
    • 0041758426 scopus 로고    scopus 로고
    • The formins: active scaffolds that remodel the cytoskeleton
    • Wallar B.J., and Alberts A.S. The formins: active scaffolds that remodel the cytoskeleton. Trends Cell Biol. 13 (2003) 435-446
    • (2003) Trends Cell Biol. , vol.13 , pp. 435-446
    • Wallar, B.J.1    Alberts, A.S.2
  • 141
    • 0036305635 scopus 로고    scopus 로고
    • ROCK and Dia have opposing effects on adherens junctions downstream of Rho
    • Sahai E., and Marshall C.J. ROCK and Dia have opposing effects on adherens junctions downstream of Rho. Nat. Cell Biol. 4 (2002) 408-415
    • (2002) Nat. Cell Biol. , vol.4 , pp. 408-415
    • Sahai, E.1    Marshall, C.J.2
  • 142
    • 0030785342 scopus 로고    scopus 로고
    • Rho-stimulated contractility contributes to the fibroblastic phenotype of Ras-transformed epithelial cells
    • Zhong C., Kinch M.S., and Burridge K. Rho-stimulated contractility contributes to the fibroblastic phenotype of Ras-transformed epithelial cells. Mol. Biol. Cell 8 (1997) 2329-2344
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2329-2344
    • Zhong, C.1    Kinch, M.S.2    Burridge, K.3
  • 143
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells
    • Takaishi K., Sasaki T., Kotani H., Nishioka H., and Takai Y. Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells. J. Cell Biol. 139 (1997) 1047-1059
    • (1997) J. Cell Biol. , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 144
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga V.M., Machesky L.M., Hall A., and Hotchin N.A. The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J. Cell Biol. 137 (1997) 1421-1431
    • (1997) J. Cell Biol. , vol.137 , pp. 1421-1431
    • Braga, V.M.1    Machesky, L.M.2    Hall, A.3    Hotchin, N.A.4
  • 145
    • 0033536245 scopus 로고    scopus 로고
    • Involvement of Cdc42 small G protein in cell-cell adhesion, migration and morphology of MDCK cells
    • Kodama A., Takaishi K., Nakano K., Nishioka H., and Takai Y. Involvement of Cdc42 small G protein in cell-cell adhesion, migration and morphology of MDCK cells. Oncogene 18 (1999) 3996-4006
    • (1999) Oncogene , vol.18 , pp. 3996-4006
    • Kodama, A.1    Takaishi, K.2    Nakano, K.3    Nishioka, H.4    Takai, Y.5
  • 146
    • 3242705077 scopus 로고    scopus 로고
    • RhoA, Rac1, and Cdc42 exert distinct effects on epithelial barrier via selective structural and biochemical modulation of junctional proteins and F-actin
    • Bruewer M., Hopkins A.M., Hobert M.E., Nusrat A., and Madara J.L. RhoA, Rac1, and Cdc42 exert distinct effects on epithelial barrier via selective structural and biochemical modulation of junctional proteins and F-actin. Am. J. Physiol. Cell Physiol. 287 (2004) C327-C335
    • (2004) Am. J. Physiol. Cell Physiol. , vol.287
    • Bruewer, M.1    Hopkins, A.M.2    Hobert, M.E.3    Nusrat, A.4    Madara, J.L.5
  • 149
    • 0037421188 scopus 로고    scopus 로고
    • Direct cadherin-activated cell signaling: a view from the plasma membrane
    • Yap A.S., and Kovacs E.M. Direct cadherin-activated cell signaling: a view from the plasma membrane. J. Cell Biol. 160 (2003) 11-16
    • (2003) J. Cell Biol. , vol.160 , pp. 11-16
    • Yap, A.S.1    Kovacs, E.M.2
  • 150
    • 1642462391 scopus 로고    scopus 로고
    • Lamellipodium extension and cadherin adhesion: two cell responses to cadherin activation relying on distinct signalling pathways
    • Gavard J., Lambert M., Grosheva I., Marthiens V., Irinopoulou T., Riou J.F., Bershadsky A., and Mege R.M. Lamellipodium extension and cadherin adhesion: two cell responses to cadherin activation relying on distinct signalling pathways. J. Cell Sci. 117 (2004) 257-270
    • (2004) J. Cell Sci. , vol.117 , pp. 257-270
    • Gavard, J.1    Lambert, M.2    Grosheva, I.3    Marthiens, V.4    Irinopoulou, T.5    Riou, J.F.6    Bershadsky, A.7    Mege, R.M.8
  • 151
    • 30044444270 scopus 로고    scopus 로고
    • Activation of Rac by cadherin through the c-Src-Rap1-phosphatidylinositol 3-kinase-Vav2 pathway
    • Fukuyama T., Ogita H., Kawakatsu T., Inagaki M., and Takai Y. Activation of Rac by cadherin through the c-Src-Rap1-phosphatidylinositol 3-kinase-Vav2 pathway. Oncogene 25 (2006) 8-19
    • (2006) Oncogene , vol.25 , pp. 8-19
    • Fukuyama, T.1    Ogita, H.2    Kawakatsu, T.3    Inagaki, M.4    Takai, Y.5
  • 152
    • 0032583205 scopus 로고    scopus 로고
    • Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase
    • Sander E.E., van Delft S., ten Klooster J.P., Reid T., van der Kammen R.A., Michiels F., and Collard J.G. Matrix-dependent Tiam1/Rac signaling 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
    • (1998) J. Cell Biol. , vol.143 , pp. 1385-1398
    • Sander, E.E.1    van Delft, S.2    ten Klooster, J.P.3    Reid, T.4    van der Kammen, R.A.5    Michiels, F.6    Collard, J.G.7
  • 154
    • 0037155159 scopus 로고    scopus 로고
    • E-cadherin homophilic ligation directly signals through Rac and phosphatidylinositol 3-kinase to regulate adhesive contacts
    • Kovacs E.M., Ali R.G., McCormack A.J., and Yap A.S. E-cadherin homophilic ligation directly signals through Rac and phosphatidylinositol 3-kinase to regulate adhesive contacts. J. Biol. Chem. 277 (2002) 6708-6718
    • (2002) J. Biol. Chem. , vol.277 , pp. 6708-6718
    • Kovacs, E.M.1    Ali, R.G.2    McCormack, A.J.3    Yap, A.S.4
  • 155
    • 0033606788 scopus 로고    scopus 로고
    • Signaling to actin dynamics
    • Machesky L.M., and Insall R.H. Signaling to actin dynamics. J. Cell Biol. 146 (1999) 267-272
    • (1999) J. Cell Biol. , vol.146 , pp. 267-272
    • Machesky, L.M.1    Insall, R.H.2
  • 156
    • 0346734251 scopus 로고    scopus 로고
    • SRC-induced disintegration of adherens junctions of Madin-Darby canine kidney cells is dependent on endocytosis of cadherin and antagonized by Tiam-1
    • Palovuori R., Sormunen R., and Eskelinen S. SRC-induced disintegration of adherens junctions of Madin-Darby canine kidney cells is dependent on endocytosis of cadherin and antagonized by Tiam-1. Lab. Invest. 83 (2003) 1901-1915
    • (2003) Lab. Invest. , vol.83 , pp. 1901-1915
    • Palovuori, R.1    Sormunen, R.2    Eskelinen, S.3
  • 157
    • 2942618768 scopus 로고    scopus 로고
    • A renaissance for SRC
    • Yeatman T.J. A renaissance for SRC. Nat. Rev. Cancer 4 (2004) 470-480
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 470-480
    • Yeatman, T.J.1
  • 158
    • 0142119854 scopus 로고    scopus 로고
    • Roles of the intercellular adhesion molecule nectin in intracellular signaling
    • Shimizu K., and Takai Y. Roles of the intercellular adhesion molecule nectin in intracellular signaling. J. Biochem. (Tokyo) 134 (2003) 631-636
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 631-636
    • Shimizu, K.1    Takai, Y.2
  • 159
    • 34249734651 scopus 로고    scopus 로고
    • Involvement of integrin-induced activation of protein kinase C in the formation of adherens junctions
    • Ozaki M., Ogita H., and Takai Y. Involvement of integrin-induced activation of protein kinase C in the formation of adherens junctions. Genes Cells 12 (2007) 651-662
    • (2007) Genes Cells , vol.12 , pp. 651-662
    • Ozaki, M.1    Ogita, H.2    Takai, Y.3
  • 162
    • 14044273991 scopus 로고    scopus 로고
    • Vav2 as a Rac-GDP/GTP exchange factor responsible for the nectin-induced, c-Src- and Cdc42-mediated activation of Rac
    • Kawakatsu T., Ogita H., Fukuhara T., Fukuyama T., Minami Y., Shimizu K., and Takai Y. Vav2 as a Rac-GDP/GTP exchange factor responsible for the nectin-induced, c-Src- and Cdc42-mediated activation of Rac. J. Biol. Chem. 280 (2005) 4940-4947
    • (2005) J. Biol. Chem. , vol.280 , pp. 4940-4947
    • Kawakatsu, T.1    Ogita, H.2    Fukuhara, T.3    Fukuyama, T.4    Minami, Y.5    Shimizu, K.6    Takai, Y.7
  • 163
    • 0038708352 scopus 로고    scopus 로고
    • Involvement of nectin in the localization of IQGAP1 at the cell-cell adhesion sites through the actin cytoskeleton in Madin-Darby canine kidney cells
    • Katata T., Irie K., Fukuhara A., Kawakatsu T., Yamada A., Shimizu K., and Takai Y. Involvement of nectin in the localization of IQGAP1 at the cell-cell adhesion sites through the actin cytoskeleton in Madin-Darby canine kidney cells. Oncogene 22 (2003) 2097-2109
    • (2003) Oncogene , vol.22 , pp. 2097-2109
    • Katata, T.1    Irie, K.2    Fukuhara, A.3    Kawakatsu, T.4    Yamada, A.5    Shimizu, K.6    Takai, Y.7
  • 164
    • 3342986329 scopus 로고    scopus 로고
    • Endocytosis of E-cadherin regulated by Rac and Cdc42 small G proteins through IQGAP1 and actin filaments
    • Izumi G., Sakisaka T., Baba T., Tanaka S., Morimoto K., and Takai Y. Endocytosis of E-cadherin regulated by Rac and Cdc42 small G proteins through IQGAP1 and actin filaments. J. Cell Biol. 166 (2004) 237-248
    • (2004) J. Cell Biol. , vol.166 , pp. 237-248
    • Izumi, G.1    Sakisaka, T.2    Baba, T.3    Tanaka, S.4    Morimoto, K.5    Takai, Y.6
  • 165
    • 0034254923 scopus 로고    scopus 로고
    • The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profiling
    • Boettner B., Govek E.E., Cross J., and Van Aelst L. The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profiling. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 9064-9069
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9064-9069
    • Boettner, B.1    Govek, E.E.2    Cross, J.3    Van Aelst, L.4
  • 166
    • 0034623082 scopus 로고    scopus 로고
    • Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1
    • Ebnet K., Schulz C.U., Meyer Zu Brickwedde M.K., Pendl G.G., and Vestweber D. Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1. J. Biol. Chem. 275 (2000) 27979-27988
    • (2000) J. Biol. Chem. , vol.275 , pp. 27979-27988
    • Ebnet, K.1    Schulz, C.U.2    Meyer Zu Brickwedde, M.K.3    Pendl, G.G.4    Vestweber, D.5
  • 167
    • 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
    • Takahashi K., Nakanishi H., Miyahara M., Mandai K., Satoh K., Satoh A., Nishioka H., Aoki J., Nomoto A., Mizoguchi A., and 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
    • (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    Aoki, J.8    Nomoto, A.9    Mizoguchi, A.10    Takai, Y.11
  • 168
    • 0242708621 scopus 로고    scopus 로고
    • A core function for p120-catenin in cadherin turnover
    • Davis M.A., Ireton R.C., and Reynolds A.B. A core function for p120-catenin in cadherin turnover. J. Cell Biol. 163 (2003) 525-534
    • (2003) J. Cell Biol. , vol.163 , pp. 525-534
    • Davis, M.A.1    Ireton, R.C.2    Reynolds, A.B.3
  • 169
    • 33646177309 scopus 로고    scopus 로고
    • Regulation of the assembly and adhesion activity of E-cadherin by nectin and afadin for the formation of adherens junctions in Madin-Darby canine kidney cells
    • Sato T., Fujita N., Yamada A., Ooshio T., Okamoto R., Irie K., and Takai Y. Regulation of the assembly and adhesion activity of E-cadherin by nectin and afadin for the formation of adherens junctions in Madin-Darby canine kidney cells. J. Biol. Chem. 281 (2006) 5288-5299
    • (2006) J. Biol. Chem. , vol.281 , pp. 5288-5299
    • Sato, T.1    Fujita, N.2    Yamada, A.3    Ooshio, T.4    Okamoto, R.5    Irie, K.6    Takai, Y.7
  • 170
    • 33846847701 scopus 로고    scopus 로고
    • Rap1: a key regulator in cell-cell junction formation
    • Kooistra M.R., Dube N., and Bos J.L. Rap1: a key regulator in cell-cell junction formation. J. Cell Sci. 120 (2007) 17-22
    • (2007) J. Cell Sci. , vol.120 , pp. 17-22
    • Kooistra, M.R.1    Dube, N.2    Bos, J.L.3
  • 172
    • 0024600222 scopus 로고
    • A Ras-related gene with transformation suppressor activity
    • Kitayama H., Sugimoto Y., Matsuzaki T., Ikawa Y., and Noda M. A Ras-related gene with transformation suppressor activity. Cell 56 (1989) 77-84
    • (1989) Cell , vol.56 , pp. 77-84
    • Kitayama, H.1    Sugimoto, Y.2    Matsuzaki, T.3    Ikawa, Y.4    Noda, M.5
  • 174
    • 31944446602 scopus 로고    scopus 로고
    • MAGI-1 is required for Rap1 activation upon cell-cell contact and for enhancement of vascular endothelial cadherin-mediated cell adhesion
    • Sakurai A., Fukuhara S., Yamagishi A., Sako K., Kamioka Y., Masuda M., Nakaoka Y., and Mochizuki N. MAGI-1 is required for Rap1 activation upon cell-cell contact and for enhancement of vascular endothelial cadherin-mediated cell adhesion. Mol. Biol. Cell 17 (2006) 966-976
    • (2006) Mol. Biol. Cell , vol.17 , pp. 966-976
    • Sakurai, A.1    Fukuhara, S.2    Yamagishi, A.3    Sako, K.4    Kamioka, Y.5    Masuda, M.6    Nakaoka, Y.7    Mochizuki, N.8
  • 176
    • 0034696822 scopus 로고    scopus 로고
    • MAGI-1 interacts with beta-catenin and is associated with cell-cell adhesion structures
    • Dobrosotskaya I.Y., and James G.L. MAGI-1 interacts with beta-catenin and is associated with cell-cell adhesion structures. Biochem. Biophys. Res. Commun. 270 (2000) 903-909
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 903-909
    • Dobrosotskaya, I.Y.1    James, G.L.2
  • 177
    • 0034485413 scopus 로고    scopus 로고
    • Membrane-associated guanylate kinase with inverted orientation (MAGI)-1/brain angiogenesis inhibitor 1-associated protein (BAP1) as a scaffolding molecule for Rap small G protein GDP/GTP exchange protein at tight junctions
    • Mino A., Ohtsuka T., Inoue E., and Takai Y. Membrane-associated guanylate kinase with inverted orientation (MAGI)-1/brain angiogenesis inhibitor 1-associated protein (BAP1) as a scaffolding molecule for Rap small G protein GDP/GTP exchange protein at tight junctions. Genes Cells 5 (2000) 1009-1016
    • (2000) Genes Cells , vol.5 , pp. 1009-1016
    • Mino, A.1    Ohtsuka, T.2    Inoue, E.3    Takai, Y.4
  • 179
    • 5444230311 scopus 로고    scopus 로고
    • Rap1 promotes cell spreading by localizing Rac guanine nucleotide exchange factors
    • Arthur W.T., Quilliam L.A., and Cooper J.A. Rap1 promotes cell spreading by localizing Rac guanine nucleotide exchange factors. J. Cell Biol. 167 (2004) 111-122
    • (2004) J. Cell Biol. , vol.167 , pp. 111-122
    • Arthur, W.T.1    Quilliam, L.A.2    Cooper, J.A.3
  • 180
    • 27844507514 scopus 로고    scopus 로고
    • E-cadherin endocytosis regulates the activity of Rap1: a traffic light GTPase at the crossroads between cadherin and integrin function
    • Balzac F., Avolio M., Degani S., Kaverina I., Torti M., Silengo L., Small J.V., and Retta S.F. E-cadherin endocytosis regulates the activity of Rap1: a traffic light GTPase at the crossroads between cadherin and integrin function. J. Cell Sci. 118 (2005) 4765-4783
    • (2005) J. Cell Sci. , vol.118 , pp. 4765-4783
    • Balzac, F.1    Avolio, M.2    Degani, S.3    Kaverina, I.4    Torti, M.5    Silengo, L.6    Small, J.V.7    Retta, S.F.8
  • 181
    • 4344594485 scopus 로고    scopus 로고
    • The sequential activity of the GTPases Rap1B and Cdc42 determines neuronal polarity
    • Schwamborn J.C., and Puschel A.W. The sequential activity of the GTPases Rap1B and Cdc42 determines neuronal polarity. Nat. Neurosci. 7 (2004) 923-929
    • (2004) Nat. Neurosci. , vol.7 , pp. 923-929
    • Schwamborn, J.C.1    Puschel, A.W.2
  • 182
    • 33645746316 scopus 로고    scopus 로고
    • The PAR-aPKC system: lessons in polarity
    • Suzuki A., and Ohno S. The PAR-aPKC system: lessons in polarity. J. Cell Sci. 119 (2006) 979-987
    • (2006) J. Cell Sci. , vol.119 , pp. 979-987
    • Suzuki, A.1    Ohno, S.2
  • 183
    • 24144444059 scopus 로고    scopus 로고
    • Epac1 regulates integrity of endothelial cell junctions through VE-cadherin
    • Kooistra M.R., Corada M., Dejana E., and Bos J.L. Epac1 regulates integrity of endothelial cell junctions through VE-cadherin. FEBS Lett. 579 (2005) 4966-4972
    • (2005) FEBS Lett. , vol.579 , pp. 4966-4972
    • Kooistra, M.R.1    Corada, M.2    Dejana, E.3    Bos, J.L.4
  • 184
    • 14944377651 scopus 로고    scopus 로고
    • Regulation of vascular endothelial barrier function by Epac, a cAMP-activated exchange factor for Rap GTPase
    • Cullere X., Shaw S.K., Andersson L., Hirahashi J., Luscinskas F.W., and Mayadas T.N. Regulation of vascular endothelial barrier function by Epac, a cAMP-activated exchange factor for Rap GTPase. Blood 105 (2005) 1950-1955
    • (2005) Blood , vol.105 , pp. 1950-1955
    • Cullere, X.1    Shaw, S.K.2    Andersson, L.3    Hirahashi, J.4    Luscinskas, F.W.5    Mayadas, T.N.6
  • 185
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • Edwards D.C., Sanders L.C., Bokoch G.M., and Gill G.N. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. 1 (1999) 253-259
    • (1999) Nat. Cell Biol. , vol.1 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 186
    • 0035002333 scopus 로고    scopus 로고
    • N-WASP, WAVE and Mena play different roles in the organization of actin cytoskeleton in lamellipodia
    • Nakagawa H., Miki H., Ito M., Ohashi K., Takenawa T., and Miyamoto S. N-WASP, WAVE and Mena play different roles in the organization of actin cytoskeleton in lamellipodia. J. Cell Sci. 114 (2001) 1555-1565
    • (2001) J. Cell Sci. , vol.114 , pp. 1555-1565
    • Nakagawa, H.1    Miki, H.2    Ito, M.3    Ohashi, K.4    Takenawa, T.5    Miyamoto, S.6
  • 187
    • 0036774217 scopus 로고    scopus 로고
    • Cell-cell adhesion and signaling
    • Braga V.M. Cell-cell adhesion and signaling. Curr. Opin. Cell Biol. 14 (2002) 546-556
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 546-556
    • Braga, V.M.1
  • 188
    • 0035902520 scopus 로고    scopus 로고
    • Contact interactions between epitheliocytes and fibroblasts: formation of heterotypic cadherin-containing adhesion sites is accompanied by local cytoskeletal reorganization
    • Omelchenko T., Fetisova E., Ivanova O., Bonder E.M., Feder H., Vasiliev J.M., and Gelfand I.M. Contact interactions between epitheliocytes and fibroblasts: formation of heterotypic cadherin-containing adhesion sites is accompanied by local cytoskeletal reorganization. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 8632-8637
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8632-8637
    • Omelchenko, T.1    Fetisova, E.2    Ivanova, O.3    Bonder, E.M.4    Feder, H.5    Vasiliev, J.M.6    Gelfand, I.M.7
  • 189
    • 0031696485 scopus 로고    scopus 로고
    • Translocation of cortactin to the cell periphery is mediated by the small GTPase Rac1
    • Weed S.A., Du Y., and Parsons J.T. Translocation of cortactin to the cell periphery is mediated by the small GTPase Rac1. J. Cell Sci. 111 (1998) 2433-2443
    • (1998) J. Cell Sci. , vol.111 , pp. 2433-2443
    • Weed, S.A.1    Du, Y.2    Parsons, J.T.3
  • 190
    • 30944433152 scopus 로고    scopus 로고
    • Regulated and polarized PtdIns(3,4,5)P3 accumulation is essential for apical membrane morphogenesis in photoreceptor epithelial cells
    • Pinal N., Goberdhan D.C., Collinson L., Fujita Y., Cox I.M., Wilson C., and Pichaud F. Regulated and polarized PtdIns(3,4,5)P3 accumulation is essential for apical membrane morphogenesis in photoreceptor epithelial cells. Curr. Biol. 16 (2006) 140-149
    • (2006) Curr. Biol. , vol.16 , pp. 140-149
    • Pinal, N.1    Goberdhan, D.C.2    Collinson, L.3    Fujita, Y.4    Cox, I.M.5    Wilson, C.6    Pichaud, F.7
  • 192
    • 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
  • 195
    • 25444486668 scopus 로고    scopus 로고
    • The Rac activator Tiam1 controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex
    • Mertens A.E., Rygiel T.P., Olivo C., van der Kammen R., and Collard J.G. The Rac activator Tiam1 controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex. J. Cell Biol. 170 (2005) 1029-1037
    • (2005) J. Cell Biol. , vol.170 , pp. 1029-1037
    • Mertens, A.E.1    Rygiel, T.P.2    Olivo, C.3    van der Kammen, R.4    Collard, J.G.5
  • 196
    • 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
    • Kawakatsu T., Shimizu K., Honda T., Fukuhara T., Hoshino T., and 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
    • (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
  • 197
    • 0034711219 scopus 로고    scopus 로고
    • E-cadherin-mediated cell-cell attachment activates Cdc42
    • Kim S.H., Li Z., and Sacks D.B. E-cadherin-mediated cell-cell attachment activates Cdc42. J. Biol. Chem. 275 (2000) 36999-37005
    • (2000) J. Biol. Chem. , vol.275 , pp. 36999-37005
    • Kim, S.H.1    Li, Z.2    Sacks, D.B.3
  • 198
    • 0035911955 scopus 로고    scopus 로고
    • Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures
    • Suzuki A., Yamanaka T., Hirose T., Manabe N., Mizuno K., Shimizu M., Akimoto K., Izumi Y., Ohnishi T., and Ohno S. Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures. J. Cell Biol. 152 (2001) 1183-1196
    • (2001) J. Cell Biol. , vol.152 , pp. 1183-1196
    • Suzuki, A.1    Yamanaka, T.2    Hirose, T.3    Manabe, N.4    Mizuno, K.5    Shimizu, M.6    Akimoto, K.7    Izumi, Y.8    Ohnishi, T.9    Ohno, S.10
  • 199
    • 33846270032 scopus 로고    scopus 로고
    • PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42
    • Martin-Belmonte F., Gassama A., Datta A., Yu W., Rescher U., Gerke V., and Mostov K. PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42. Cell 128 (2007) 383-397
    • (2007) Cell , vol.128 , pp. 383-397
    • Martin-Belmonte, F.1    Gassama, A.2    Datta, A.3    Yu, W.4    Rescher, U.5    Gerke, V.6    Mostov, K.7
  • 200
    • 14044255938 scopus 로고    scopus 로고
    • Involvement of the annexin II-S100A10 complex in the formation of E-cadherin-based adherens junctions in Madin-Darby canine kidney cells
    • Yamada A., Irie K., Hirota T., Ooshio T., Fukuhara A., and Takai Y. Involvement of the annexin II-S100A10 complex in the formation of E-cadherin-based adherens junctions in Madin-Darby canine kidney cells. J. Biol. Chem. 280 (2005) 6016-6027
    • (2005) J. Biol. Chem. , vol.280 , pp. 6016-6027
    • Yamada, A.1    Irie, K.2    Hirota, T.3    Ooshio, T.4    Fukuhara, A.5    Takai, Y.6
  • 201
    • 0035936807 scopus 로고    scopus 로고
    • Hyperproliferation and defects in epithelial polarity upon conditional ablation of alpha-catenin in skin
    • Vasioukhin V., Bauer C., Degenstein L., Wise B., and Fuchs E. Hyperproliferation and defects in epithelial polarity upon conditional ablation of alpha-catenin in skin. Cell 104 (2001) 605-617
    • (2001) Cell , vol.104 , pp. 605-617
    • Vasioukhin, V.1    Bauer, C.2    Degenstein, L.3    Wise, B.4    Fuchs, E.5
  • 202
    • 12544252343 scopus 로고    scopus 로고
    • beta-Catenin: a pivot between cell adhesion and Wnt signaling
    • Bienz M. beta-Catenin: a pivot between cell adhesion and Wnt signaling. Curr. Biol. 15 (2005) R64-R67
    • (2005) Curr. Biol. , vol.15
    • Bienz, M.1
  • 203
    • 1542347695 scopus 로고    scopus 로고
    • Convergence of Wnt, beta-catenin, and cadherin pathways
    • Nelson W.J., and Nusse R. Convergence of Wnt, beta-catenin, and cadherin pathways. Science 303 (2004) 1483-1487
    • (2004) Science , vol.303 , pp. 1483-1487
    • Nelson, W.J.1    Nusse, R.2
  • 204
    • 34250361104 scopus 로고    scopus 로고
    • E-Cadherin homophilic ligation inhibits cell growth and epidermal growth factor receptor signaling independently of other cell interactions
    • Perrais M., Chen X., Perez-Moreno M., and Gumbiner B.M. E-Cadherin homophilic ligation inhibits cell growth and epidermal growth factor receptor signaling independently of other cell interactions. Mol. Biol. Cell 18 (2007) 2013-2025
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2013-2025
    • Perrais, M.1    Chen, X.2    Perez-Moreno, M.3    Gumbiner, B.M.4
  • 205
    • 0034595219 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression
    • Balda M.S., and Matter K. The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression. EMBO J. 19 (2000) 2024-2033
    • (2000) EMBO J. , vol.19 , pp. 2024-2033
    • Balda, M.S.1    Matter, K.2
  • 206
    • 0037415643 scopus 로고    scopus 로고
    • The ZO-1 associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density
    • Balda M.S., Garrett M.D., and Matter K. The ZO-1 associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density. J. Cell Biol. 160 (2003) 423-432
    • (2003) J. Cell Biol. , vol.160 , pp. 423-432
    • Balda, M.S.1    Garrett, M.D.2    Matter, K.3
  • 207
    • 0023030826 scopus 로고
    • Identification of ZO-1, a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia
    • Stevenson B.R., Siliciano J.D., Mooseker M.S., and Goodenough D.A. Identification of ZO-1, a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J. Cell Biol. 103 (1986) 755-766
    • (1986) J. Cell Biol. , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3    Goodenough, D.A.4
  • 208
    • 0033180348 scopus 로고    scopus 로고
    • Protein modules as organizers of membrane structure
    • Fanning A.S., and Anderson J.M. Protein modules as organizers of membrane structure. Curr. Opin. Cell Biol. 11 (1999) 432-439
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 432-439
    • Fanning, A.S.1    Anderson, J.M.2
  • 209
    • 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
  • 210
    • 0034695461 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion
    • Raucher D., Stauffer T., Chen W., Shen K., Guo S., York J.D., Sheetz M.P., and Meyer T. Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion. Cell 100 (2000) 221-228
    • (2000) Cell , vol.100 , pp. 221-228
    • Raucher, D.1    Stauffer, T.2    Chen, W.3    Shen, K.4    Guo, S.5    York, J.D.6    Sheetz, M.P.7    Meyer, T.8
  • 212
    • 1542319943 scopus 로고    scopus 로고
    • Activation of type I phosphatidylinositol 4-phosphate 5-kinase isoforms by the Rho GTPases, RhoA, Rac1, and Cdc42
    • Weernink P.A., Meletiadis K., Hommeltenberg S., Hinz M., Ishihara H., Schmidt M., and Jakobs K.H. Activation of type I phosphatidylinositol 4-phosphate 5-kinase isoforms by the Rho GTPases, RhoA, Rac1, and Cdc42. J. Biol. Chem. 279 (2004) 7840-7849
    • (2004) J. Biol. Chem. , vol.279 , pp. 7840-7849
    • Weernink, P.A.1    Meletiadis, K.2    Hommeltenberg, S.3    Hinz, M.4    Ishihara, H.5    Schmidt, M.6    Jakobs, K.H.7
  • 213
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4,5-bisphosphate
    • Gilmore A.P., and Burridge K. Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4,5-bisphosphate. Nature 381 (1996) 531-535
    • (1996) Nature , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 214
    • 17344380140 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactin-actomyosin II complex and malignant transformation
    • He H., Watanabe T., Zhan X., Huang C., Schuuring E., Fukami K., Takenawa T., Kumar C.C., Simpson R.J., and Maruta H. Role of phosphatidylinositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactin-actomyosin II complex and malignant transformation. Mol. Cell Biol. 18 (1998) 3829-3837
    • (1998) Mol. Cell Biol. , vol.18 , pp. 3829-3837
    • He, H.1    Watanabe, T.2    Zhan, X.3    Huang, C.4    Schuuring, E.5    Fukami, K.6    Takenawa, T.7    Kumar, C.C.8    Simpson, R.J.9    Maruta, H.10
  • 215
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi R., Ma L., Miki H., Lopez M., Kirchhausen T., Takenawa T., and Kirschner M.W. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97 (1999) 221-231
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6    Kirschner, M.W.7
  • 216
    • 0038311944 scopus 로고    scopus 로고
    • Phosphoinositide regulation of the actin cytoskeleton
    • Yin H.L., and Janmey P.A. Phosphoinositide regulation of the actin cytoskeleton. Annu. Rev. Physiol. 65 (2003) 761-789
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 761-789
    • Yin, H.L.1    Janmey, P.A.2
  • 217
    • 0034983715 scopus 로고    scopus 로고
    • WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell movement
    • Takenawa T., and Miki H. WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell movement. J. Cell Sci. 114 (2001) 1801-1809
    • (2001) J. Cell Sci. , vol.114 , pp. 1801-1809
    • Takenawa, T.1    Miki, H.2
  • 218
    • 0033588990 scopus 로고    scopus 로고
    • Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility
    • Egile C., Loisel T.P., Laurent V., Li R., Pantaloni D., Sansonetti P.J., and Carlier M.F. Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 146 (1999) 1319-1332
    • (1999) J. Cell Biol. , vol.146 , pp. 1319-1332
    • Egile, C.1    Loisel, T.P.2    Laurent, V.3    Li, R.4    Pantaloni, D.5    Sansonetti, P.J.6    Carlier, M.F.7
  • 219
    • 0034619847 scopus 로고    scopus 로고
    • IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
    • Miki H., Yamaguchi H., Suetsugu S., and Takenawa T. IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature 408 (2000) 732-735
    • (2000) Nature , vol.408 , pp. 732-735
    • Miki, H.1    Yamaguchi, H.2    Suetsugu, S.3    Takenawa, T.4
  • 220
    • 0036293357 scopus 로고    scopus 로고
    • WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac
    • Miki H., and Takenawa T. WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac. Biochem. Biophys. Res. Commun. 293 (2002) 93-99
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 93-99
    • Miki, H.1    Takenawa, T.2
  • 221
    • 36549053109 scopus 로고    scopus 로고
    • Mammalian diaphanous-related formin Dia1 controls the organization of E-cadherin-mediated cell-cell junctions
    • Carramusa L., Ballestrem C., Zilberman Y., and Bershadsky A.D. Mammalian diaphanous-related formin Dia1 controls the organization of E-cadherin-mediated cell-cell junctions. J. Cell Sci. 120 (2007) 3870-3882
    • (2007) J. Cell Sci. , vol.120 , pp. 3870-3882
    • Carramusa, L.1    Ballestrem, C.2    Zilberman, Y.3    Bershadsky, A.D.4
  • 222
    • 0043202969 scopus 로고    scopus 로고
    • The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
    • Li F., and Higgs H.N. The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr. Biol. 13 (2003) 1335-1340
    • (2003) Curr. Biol. , vol.13 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 223
    • 20844439387 scopus 로고    scopus 로고
    • Structural basis of Rho GTPase-mediated activation of the formin mDia1
    • Otomo T., Otomo C., Tomchick D.R., Machius M., and Rosen M.K. Structural basis of Rho GTPase-mediated activation of the formin mDia1. Mol. Cell 18 (2005) 273-281
    • (2005) Mol. Cell , vol.18 , pp. 273-281
    • Otomo, T.1    Otomo, C.2    Tomchick, D.R.3    Machius, M.4    Rosen, M.K.5
  • 225
    • 13244267197 scopus 로고    scopus 로고
    • Recruitment of phosphoinositide 3-kinase defines a positive contribution of tyrosine kinase signaling to E-cadherin function
    • Pang J.H., Kraemer A., Stehbens S.J., Frame M.C., and Yap A.S. Recruitment of phosphoinositide 3-kinase defines a positive contribution of tyrosine kinase signaling to E-cadherin function. J. Biol. Chem. 280 (2005) 3043-3050
    • (2005) J. Biol. Chem. , vol.280 , pp. 3043-3050
    • Pang, J.H.1    Kraemer, A.2    Stehbens, S.J.3    Frame, M.C.4    Yap, A.S.5
  • 227
    • 33745863102 scopus 로고    scopus 로고
    • Interaction of integrin alpha(v)beta3 with nectin. Implication in cross-talk between cell-matrix and cell-cell junctions
    • Sakamoto Y., Ogita H., Hirota T., Kawakatsu T., Fukuyama T., Yasumi M., Kanzaki N., Ozaki M., and Takai Y. Interaction of integrin alpha(v)beta3 with nectin. Implication in cross-talk between cell-matrix and cell-cell junctions. J. Biol. Chem. 281 (2006) 19631-19644
    • (2006) J. Biol. Chem. , vol.281 , pp. 19631-19644
    • Sakamoto, Y.1    Ogita, H.2    Hirota, T.3    Kawakatsu, T.4    Fukuyama, T.5    Yasumi, M.6    Kanzaki, N.7    Ozaki, M.8    Takai, Y.9
  • 228
    • 38049188053 scopus 로고    scopus 로고
    • Involvement of nectin in inactivation of integrin alpha vbeta 3 after the establishment of cell-cell adhesion
    • Sakamoto Y., Ogita H., Komura H., and Takai Y. Involvement of nectin in inactivation of integrin alpha vbeta 3 after the establishment of cell-cell adhesion. J. Biol. Chem. 283 (2008) 496-505
    • (2008) J. Biol. Chem. , vol.283 , pp. 496-505
    • Sakamoto, Y.1    Ogita, H.2    Komura, H.3    Takai, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.