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Volumn 60, Issue , 2014, Pages 111-135

The cytoskeleton and classical cadherin adhesions

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EID: 84934876375     PISSN: 03060225     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-94-007-4186-7_6     Document Type: Article
Times cited : (17)

References (154)
  • 1
    • 38349138921 scopus 로고    scopus 로고
    • EPLIN mediates linkage of the cadherin-catenin complex to F-actin and stabilizes the circumferential actin belt
    • Abe K, Takeichi M (2008) EPLIN mediates linkage of the cadherin-catenin complex to F-actin and stabilizes the circumferential actin belt. Proc Natl Acad Sci U S A 105: 13-19.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 13-19
    • Abe, K.1    Takeichi, M.2
  • 3
    • 59849100330 scopus 로고    scopus 로고
    • Touch, grasp, deliver and control: Functional crosstalk between microtubules and cell adhesions
    • Akhmanova A, Stehbens SJ, Yap AS (2009) Touch, grasp, deliver and control: functional crosstalk between microtubules and cell adhesions. Traffic 10: 268-274.
    • (2009) Traffic , vol.10 , pp. 268-274
    • Akhmanova, A.1    Stehbens, S.J.2    Yap, A.S.3
  • 4
    • 0035910096 scopus 로고    scopus 로고
    • Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy
    • Amann KJ, Pollard TD (2001) Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy. Proc Natl Acad Sci U S A 98: 15009-15013.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 15009-15013
    • Amann, K.J.1    Pollard, T.D.2
  • 5
    • 0029892844 scopus 로고    scopus 로고
    • Mechanism for transition from initial to stable cell-cell adhesion: Kinetic analysis of E-cadherin-mediated adhesion using a quantitative adhesion assay
    • Angres B, Barth A, Nelson WJ (1996) Mechanism for transition from initial to stable cell-cell adhesion: Kinetic analysis of E-cadherin-mediated adhesion using a quantitative adhesion assay. J Cell Biol 134: 549-557.
    • (1996) J Cell Biol , vol.134 , pp. 549-557
    • Angres, B.1    Barth, A.2    Nelson, W.J.3
  • 6
    • 0028238580 scopus 로고
    • Spatial and temporal relationships between cadherins and PECAM-1 in cell-cell junctions of human endothelial-cells
    • Ayalon O, Sabanai H, Lampugnani MG, Dejana E, Geiger B (1994) Spatial and temporal relationships between cadherins and PECAM-1 in cell-cell junctions of human endothelial-cells. J Cell Biol 126: 247-258.
    • (1994) J Cell Biol , vol.126 , pp. 247-258
    • Ayalon, O.1    Sabanai, H.2    Lampugnani, M.G.3    Dejana, E.4    Geiger, B.5
  • 8
    • 79955508089 scopus 로고    scopus 로고
    • Dynamics of adherens junctions in epithelial establishment, maintenance, and remodeling
    • Baum B, Georgiou M (2011) Dynamics of adherens junctions in epithelial establishment, maintenance, and remodeling. J Cell Biol 192: 907-917.
    • (2011) J Cell Biol , vol.192 , pp. 907-917
    • Baum, B.1    Georgiou, M.2
  • 9
    • 0034785272 scopus 로고    scopus 로고
    • Spatial control of the actin cytoskeleton in Drosophila epithelial cells
    • Baum B, Perrimon N (2001) Spatial control of the actin cytoskeleton in Drosophila epithelial cells. Nat Cell Biol 3: 883-890.
    • (2001) Nat Cell Biol , vol.3 , pp. 883-890
    • Baum, B.1    Perrimon, N.2
  • 10
    • 43949120138 scopus 로고    scopus 로고
    • Follow the monomer
    • Bear JE (2008) Follow the monomer. Cell 133: 765-767.
    • (2008) Cell , vol.133 , pp. 765-767
    • Bear, J.E.1
  • 12
    • 80051700779 scopus 로고    scopus 로고
    • Arp2/3 promotes junction formation and maintenance in the Caenorhabditis elegans intestine by regulating membrane association of apical proteins
    • Bernadskaya YY, Patel FB, Hsu H-T, Soto MC (2011) Arp2/3 promotes junction formation and maintenance in the Caenorhabditis elegans intestine by regulating membrane association of apical proteins. Mol Biol Cell 22: 2886-2899.
    • (2011) Mol Biol Cell , vol.22 , pp. 2886-2899
    • Bernadskaya, Y.Y.1    Patel, F.B.2    Hsu, H.-T.3    Soto, M.C.4
  • 13
    • 2942587231 scopus 로고    scopus 로고
    • Myosin-dependent junction remodelling controls planar cell intercalation and axis elongation
    • Bertet C, Sulak L, Lecuit T (2004) Myosin-dependent junction remodelling controls planar cell intercalation and axis elongation. Nature 429: 667-671.
    • (2004) Nature , vol.429 , pp. 667-671
    • Bertet, C.1    Sulak, L.2    Lecuit, T.3
  • 15
    • 24644519086 scopus 로고    scopus 로고
    • The challenges of abundance: Epithelial junctions and small GTPase signalling
    • Braga VMM, Yap AS (2005) The challenges of abundance: epithelial junctions and small GTPase signalling. Curr Opin Cell Biol 17: 466-474.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 466-474
    • Braga, V.M.M.1    Yap, A.S.2
  • 16
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases rho and rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga VMM, Machesky LM, Hall A, Hotchin NA (1997) The small GTPases rho and rac are required for the establishment of cadherin-dependent cell-cell contacts. J Cell Biol 137: 1421-1431.
    • (1997) J Cell Biol , vol.137 , pp. 1421-1431
    • Braga, V.M.M.1    Machesky, L.M.2    Hall, A.3    Hotchin, N.A.4
  • 17
    • 4143146438 scopus 로고    scopus 로고
    • The ins and outs of E-cadherin trafficking
    • Bryant DM, Stow JL (2004) The ins and outs of E-cadherin trafficking. Trends Cell Biol 14: 427-434.
    • (2004) Trends Cell Biol , vol.14 , pp. 427-434
    • Bryant, D.M.1    Stow, J.L.2
  • 18
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: Cellular control of actin assembly
    • Campellone KG, Welch MD (2010) A nucleator arms race: cellular control of actin assembly. Nat Rev Mol Cell Biol 11: 237-251.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 19
    • 79151482119 scopus 로고    scopus 로고
    • Vinculin, an adapter protein in control of cell adhesion signalling
    • Carisey A, Ballestrem C (2011) Vinculin, an adapter protein in control of cell adhesion signalling. Eur J Cell Biol 90: 157-163.
    • (2011) Eur J Cell Biol , vol.90 , pp. 157-163
    • Carisey, A.1    Ballestrem, C.2
  • 20
    • 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, Bershadsky AD (2007) Mammalian diaphanous-related formin Dia1 controls the organization of E-cadherin-mediated cell-cell junctions. J Cell Sci 120: 3870-3882.
    • (2007) J Cell Sci , vol.120 , pp. 3870-3882
    • Carramusa, L.1    Ballestrem, C.2    Zilberman, Y.3    Bershadsky, A.D.4
  • 21
    • 44849115958 scopus 로고    scopus 로고
    • A two-tiered mechanism for stabilization and immobilization of E-cadherin
    • Cavey M, Rauzi M, Lenne PF, Lecuit T (2008) A two-tiered mechanism for stabilization and immobilization of E-cadherin. Nature 453: 751-U2.
    • (2008) Nature , vol.453 , pp. 751-752
    • Cavey, M.1    Rauzi, M.2    Lenne, P.F.3    Lecuit, T.4
  • 22
  • 23
    • 72949110575 scopus 로고    scopus 로고
    • Unleashing formins to remodel the actin and microtubule cytoskeletons
    • Chesarone MA, DuPage AG, Goode BL (2010) Unleashing formins to remodel the actin and microtubule cytoskeletons. Nat Rev Mol Cell Biol 11: 62-74.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 62-74
    • Chesarone, M.A.1    DuPage, A.G.2    Goode, B.L.3
  • 24
    • 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 YS, Thomas WA, Eder O, Pincet F, Perez E, Thiery JP, Dufour S (2004) Force measurements in E-cadherin-mediated cell doublets reveal rapid adhesion strengthened by actin cytoskeleton remodeling through Rac and Cdc42. J Cell Biol 167: 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
  • 25
    • 0032489838 scopus 로고    scopus 로고
    • A putative catenin-cadherin system mediates morphogenesis of the Caenorhabditis elegans embryo
    • Costa M, Raich W, Agbunag C, Leung B, Hardin J, Priess JR (1998) A putative catenin-cadherin system mediates morphogenesis of the Caenorhabditis elegans embryo. J Cell Biol 141: 297-308.
    • (1998) J Cell Biol , vol.141 , pp. 297-308
    • Costa, M.1    Raich, W.2    Agbunag, C.3    Leung, B.4    Hardin, J.5    Priess, J.R.6
  • 28
    • 69949106214 scopus 로고    scopus 로고
    • Cadherin adhesion receptors orient the mitotic spindle during symmetric cell division in mammalian epithelia
    • den Elzen N, Buttery CV, Maddugoda MP, Ren G, Yap AS (2009) Cadherin adhesion receptors orient the mitotic spindle during symmetric cell division in mammalian epithelia. Mol Biol Cell 20: 3740-3750.
    • (2009) Mol Biol Cell , vol.20 , pp. 3740-3750
    • den Elzen, N.1    Buttery, C.V.2    Maddugoda, M.P.3    Ren, G.4    Yap, A.S.5
  • 29
    • 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 WJ, Weis WI (2005) Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. Cell 123: 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
  • 30
    • 0022993466 scopus 로고
    • Elongation of actin-filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules
    • Drenckhahn D, Pollard TD (1986) Elongation of actin-filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules. J Biol Chem 261: 2754-2758.
    • (1986) J Biol Chem , vol.261 , pp. 2754-2758
    • Drenckhahn, D.1    Pollard, T.D.2
  • 33
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar MG, Palade GE (1963) Junctional complexes in various epithelia. J Cell Biol 17: 375-412.
    • (1963) J Cell Biol , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 36
    • 0036052866 scopus 로고    scopus 로고
    • Myosin VI is required for E-cadherin-mediated border cell migration
    • Geisbrecht ER, Montell DJ (2002) Myosin VI is required for E-cadherin-mediated border cell migration. Nat Cell Biol 4: 616-620.
    • (2002) Nat Cell Biol , vol.4 , pp. 616-620
    • Geisbrecht, E.R.1    Montell, D.J.2
  • 37
    • 55249111248 scopus 로고    scopus 로고
    • Cdc42, Par6, and aPKC Regulate Arp2/3-mediated endocytosis to control local adherens junction stability
    • Georgiou M, Marinari E, Burden J, Baum B (2008) Cdc42, Par6, and aPKC Regulate Arp2/3-mediated endocytosis to control local adherens junction stability. Curr Biol 18: 1631-1638.
    • (2008) Curr Biol , vol.18 , pp. 1631-1638
    • Georgiou, M.1    Marinari, E.2    Burden, J.3    Baum, B.4
  • 39
    • 33749037156 scopus 로고    scopus 로고
    • The ARP2/3 complex: An actin nucleator comes of age
    • Goley ED, Welch MD (2006) The ARP2/3 complex: an actin nucleator comes of age. Nat Rev Mol Cell Biol 7: 713-726.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 713-726
    • Goley, E.D.1    Welch, M.D.2
  • 40
    • 78049521359 scopus 로고    scopus 로고
    • VASP is a processive actin polymerase that requires monomeric actin for barbed end association
    • Hansen SD, Mullins RD (2010) VASP is a processive actin polymerase that requires monomeric actin for barbed end association. J Cell Biol 191: 571-584.
    • (2010) J Cell Biol , vol.191 , pp. 571-584
    • Hansen, S.D.1    Mullins, R.D.2
  • 41
    • 1542344034 scopus 로고    scopus 로고
    • Novel kelch-like protein, KLEIP, is involved in actin assembly at cell-cell contact sites of Madin-Darby canine kidney cells
    • Hara T, Ishida H, Raziuddin R, Dorkhom S, Kamijo K, Miki T (2004) Novel kelch-like protein, KLEIP, is involved in actin assembly at cell-cell contact sites of Madin-Darby canine kidney cells. Mol Biol Cell 15: 1172-1184.
    • (2004) Mol Biol Cell , vol.15 , pp. 1172-1184
    • Hara, T.1    Ishida, H.2    Raziuddin, R.3    Dorkhom, S.4    Kamijo, K.5    Miki, T.6
  • 42
    • 24144443830 scopus 로고    scopus 로고
    • The positioning and segregation of apical cues during epithelial polarity establishment in Drosophila
    • Harris TJC, Peifer M (2005) The positioning and segregation of apical cues during epithelial polarity establishment in Drosophila. J Cell Biol 170: 813-823.
    • (2005) J Cell Biol , vol.170 , pp. 813-823
    • Harris, T.J.C.1    Peifer, M.2
  • 45
    • 0032702259 scopus 로고    scopus 로고
    • Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins
    • Higgs HN, Pollard TD (1999) Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins. J Biol Chem 274: 32531-32534.
    • (1999) J Biol Chem , vol.274 , pp. 32531-32534
    • Higgs, H.N.1    Pollard, T.D.2
  • 46
    • 77955057786 scopus 로고    scopus 로고
    • Molecules, mechanisms, and cellular roles of clathrinindependent endocytosis
    • Howes MT, Mayor S, Parton RG (2010) Molecules, mechanisms, and cellular roles of clathrinindependent endocytosis. Curr Opin Cell Biol 22: 519-527.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 519-527
    • Howes, M.T.1    Mayor, S.2    Parton, R.G.3
  • 47
    • 70249116807 scopus 로고    scopus 로고
    • Actin dynamics at the leading edge: From simple machinery to complex networks
    • Insall RH, Machesky LM (2009) Actin dynamics at the leading edge: From simple machinery to complex networks. Dev Cell 17: 310-322.
    • (2009) Dev Cell , vol.17 , pp. 310-322
    • Insall, R.H.1    Machesky, L.M.2
  • 48
    • 0021027198 scopus 로고
    • Vinculin phosphorylation by the Src kinase-Interaction of vinculin with phospholipid-vesicles
    • Ito S, Werth DK, Richert ND, Pastan I (1983) Vinculin phosphorylation by the Src kinase-Interaction of vinculin with phospholipid-vesicles. J Biol Chem 258: 4626-4631.
    • (1983) J Biol Chem , vol.258 , pp. 4626-4631
    • Ito, S.1    Werth, D.K.2    Richert, N.D.3    Pastan, I.4
  • 49
    • 19644382735 scopus 로고    scopus 로고
    • Differential roles for actin polymerization and a myosin II motor in assembly of the epithelial apical junctional complex
    • Ivanov AI, Hunt D, Utech M, Nusrat A, Parkos CA (2005) Differential roles for actin polymerization and a myosin II motor in assembly of the epithelial apical junctional complex. Mol Biol Cell 16: 2636-2650.
    • (2005) Mol Biol Cell , vol.16 , pp. 2636-2650
    • Ivanov, A.I.1    Hunt, D.2    Utech, M.3    Nusrat, A.4    Parkos, C.A.5
  • 50
    • 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, Takai Y (2004) Endocytosis of E-cadherin regulated by Rac and Cdc42 small G proteins through IQGAP1 and actin filaments. J Cell Biol 166: 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
  • 51
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrin-mediated endocytosis
    • Kaksonen M, Toret CP, Drubin DG. (2006) Harnessing actin dynamics for clathrin-mediated endocytosis. Nat Rev Mol Cell Biol 7: 404-414.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 404-414
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 52
    • 33845888826 scopus 로고    scopus 로고
    • Basal-to-apical cadherin flow at cell junctions
    • Kametani Y, Takeichi M (2007) Basal-to-apical cadherin flow at cell junctions. Nat Cell Biol 9: 92-U118.
    • (2007) Nat Cell Biol , vol.9 , pp. 92-118
    • Kametani, Y.1    Takeichi, M.2
  • 53
    • 0028979956 scopus 로고
    • Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin
    • Knudsen KA, Soler AP, Johnson KR, Wheelock MJ (1995) Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin. J Cell Biol 130: 67-77.
    • (1995) J Cell Biol , vol.130 , pp. 67-77
    • Knudsen, K.A.1    Soler, A.P.2    Johnson, K.R.3    Wheelock, M.J.4
  • 54
    • 1342310742 scopus 로고    scopus 로고
    • Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables
    • Kobielak A, Pasolli HA, Fuchs E (2004) Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables. Nat Cell Biol 6: 21-U2.
    • (2004) Nat Cell Biol , vol.6 , pp. 21-22
    • Kobielak, A.1    Pasolli, H.A.2    Fuchs, E.3
  • 55
    • 0037155159 scopus 로고    scopus 로고
    • E-cadherin homophilic ligation directly signals through Rac and phosphatidylinositol 3-kinase to regulate adhesive contacts
    • Kovacs EM, Ali RG, McCormack AJ, Yap AS (2002a) E-cadherin homophilic ligation directly signals through Rac and phosphatidylinositol 3-kinase to regulate adhesive contacts. J Biol Chem 277: 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
  • 56
    • 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 EM, Goodwin M, Ali RG, Paterson AD, Yap AS (2002b) Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts. Curr Biol 12: 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
  • 57
    • 79960984867 scopus 로고    scopus 로고
    • N-WASP regulates the epithelial junctional actin cytoskeleton through a non-canonical post-nucleation pathway
    • Kovacs EM, Verma S, Ali RG, Ratheesh A, Hamilton NA, Akhmanova A, Yap AS (2011) N-WASP regulates the epithelial junctional actin cytoskeleton through a non-canonical post-nucleation pathway. Nat Cell Biol 13: 934-U400.
    • (2011) Nat Cell Biol , vol.13 , pp. 400-934
    • Kovacs, E.M.1    Verma, S.2    Ali, R.G.3    Ratheesh, A.4    Hamilton, N.A.5    Akhmanova, A.6    Yap, A.S.7
  • 58
    • 30844449003 scopus 로고    scopus 로고
    • Molecular details of formin-mediated actin assembly
    • Kovar DR (2006) Molecular details of formin-mediated actin assembly. Curr Opin Cell Biol 18: 11-17.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 11-17
    • Kovar, D.R.1
  • 59
    • 10344234183 scopus 로고    scopus 로고
    • Progressing actin: SFormin as a processive elongation machine
    • Kovar DR, Pollard TD (2004) Progressing actin: sFormin as a processive elongation machine. Nat Cell Biol 6: 1158-1159.
    • (2004) Nat Cell Biol , vol.6 , pp. 1158-1159
    • Kovar, D.R.1    Pollard, T.D.2
  • 60
    • 33947310595 scopus 로고    scopus 로고
    • Rac is a dominant regulator of cadherin-directed actin assembly that is activated by adhesive ligation independently of Tiam1
    • Kraemer A, Goodwin M, Verma S, Yap AS, Ali RG (2007) Rac is a dominant regulator of cadherin-directed actin assembly that is activated by adhesive ligation independently of Tiam1. Am J Physiol Cell Physiol 292: C1061-C1069.
    • (2007) Am J Physiol Cell Physiol , vol.292 , pp. 1061-1069
    • Kraemer, A.1    Goodwin, M.2    Verma, S.3    Yap, A.S.4    Ali, R.G.5
  • 64
    • 0037193462 scopus 로고    scopus 로고
    • Dynamics of ligand-induced, Rac1-dependent anchoring of cadherins to the actin cytoskeleton
    • Lambert M, Choquet D, Mege RM (2002) Dynamics of ligand-induced, Rac1-dependent anchoring of cadherins to the actin cytoskeleton. J Cell Biol 157: 469-479.
    • (2002) J Cell Biol , vol.157 , pp. 469-479
    • Lambert, M.1    Choquet, D.2    Mege, R.M.3
  • 65
    • 77954410997 scopus 로고    scopus 로고
    • Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner
    • le Duc Q, Shi Q, Blonk I, Sonnenberg A, Wang N, Leckband D, de Rooij J (2010) Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner. J Cell Biol 189: 1107-1115.
    • (2010) J Cell Biol , vol.189 , pp. 1107-1115
    • le Duc, Q.1    Shi, Q.2    Blonk, I.3    Sonnenberg, A.4    Wang, N.5    Leckband, D.6    de Rooij, J.7
  • 66
    • 55249104474 scopus 로고    scopus 로고
    • Drosophila Cip4 and WASp define a branch of the Cdc42-Par6-aPKC pathway
    • Leibfried A, Fricke R, Morgan M, Bogdan S, Bellaiche Y (2008) Drosophila Cip4 and WASp define a branch of the Cdc42-Par6-aPKC pathway. Curr Biol 18: 1639-1648.
    • (2008) Curr Biol , vol.18 , pp. 1639-1648
    • Leibfried, A.1    Fricke, R.2    Morgan, M.3    Bogdan, S.4    Bellaiche, Y.5
  • 67
    • 0043202969 scopus 로고    scopus 로고
    • The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
    • Li F, Higgs HN (2003) The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr Biol 13: 1335-1340.
    • (2003) Curr Biol , vol.13 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 68
    • 34250888843 scopus 로고    scopus 로고
    • Microtubules tethered at epithelial cell junctions by dynein facilitate efficient junction assembly
    • Ligon LA, Holzbaur ELF (2007) Microtubules tethered at epithelial cell junctions by dynein facilitate efficient junction assembly. Traffic 8: 808-819.
    • (2007) Traffic , vol.8 , pp. 808-819
    • Ligon, L.A.1    Holzbaur, E.L.F.2
  • 69
    • 0034795209 scopus 로고    scopus 로고
    • Dynein binds to beta-catenin and may tether microtubules at adherens junctions
    • Ligon LA, Karki S, Tokito M, Holzbaur ELF (2001) Dynein binds to beta-catenin and may tether microtubules at adherens junctions. Nat Cell Biol 3: 913-917.
    • (2001) Nat Cell Biol , vol.3 , pp. 913-917
    • Ligon, L.A.1    Karki, S.2    Tokito, M.3    Holzbaur, E.L.F.4
  • 72
    • 34547591456 scopus 로고    scopus 로고
    • Myosin VI and vinculin cooperate during the morphogenesis of cadherin cell-cell contacts in mammalian epithelial cells
    • Maddugoda MP, Crampton MS, Shewan AM, Yap AS (2007) Myosin VI and vinculin cooperate during the morphogenesis of cadherin cell-cell contacts in mammalian epithelial cells. J Cell Biol 178: 529-540.
    • (2007) J Cell Biol , vol.178 , pp. 529-540
    • Maddugoda, M.P.1    Crampton, M.S.2    Shewan, A.M.3    Yap, A.S.4
  • 73
    • 79952814622 scopus 로고    scopus 로고
    • Hepatocyte growth factor acutely perturbs actin filament anchorage at the epithelial zonula adherens
    • Mangold S, Wu SK, Norwood SJ, Collins BM, Hamilton NA, Thorn P, Yap AS (2011) Hepatocyte growth factor acutely perturbs actin filament anchorage at the epithelial zonula adherens. Curr Biol 21: 503-507.
    • (2011) Curr Biol , vol.21 , pp. 503-507
    • Mangold, S.1    Wu, S.K.2    Norwood, S.J.3    Collins, B.M.4    Hamilton, N.A.5    Thorn, P.6    Yap, A.S.7
  • 74
    • 58749084302 scopus 로고    scopus 로고
    • Pulsed contractions of an actin-myosin network drive apical constriction
    • Martin AC, Kaschube M, Wieschaus EF (2009) Pulsed contractions of an actin-myosin network drive apical constriction. Nature 457: 495-U11.
    • (2009) Nature , vol.457 , pp. 411-495
    • Martin, A.C.1    Kaschube, M.2    Wieschaus, E.F.3
  • 78
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis
    • Mayor S, Pagano RE (2007) Pathways of clathrin-independent endocytosis. Nat Rev Mol Cell Biol 8: 603-612.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 603-612
    • Mayor, S.1    Pagano, R.E.2
  • 79
    • 66349112566 scopus 로고    scopus 로고
    • Independent cadherin-catenin and Bazooka clusters interact to assemble adherens junctions
    • McGill MA, McKinley RFA, Harris TJC (2009) Independent cadherin-catenin and Bazooka clusters interact to assemble adherens junctions. J Cell Biol 185: 787-796.
    • (2009) J Cell Biol , vol.185 , pp. 787-796
    • McGill, M.A.1    McKinley, R.F.A.2    Harris, T.J.C.3
  • 80
    • 78650224472 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase activity is necessary for E-Cadherinactivated src signaling
    • McLachlan RW, Yap AS (2011) Protein tyrosine phosphatase activity is necessary for E-Cadherinactivated src signaling. Cytoskeleton 68: 32-43.
    • (2011) Cytoskeleton , vol.68 , pp. 32-43
    • McLachlan, R.W.1    Yap, A.S.2
  • 82
    • 77649271537 scopus 로고    scopus 로고
    • The role of formins in filopodia formation
    • Mellor H (2010) The role of formins in filopodia formation. Biochim Biophys Acta Mol Cell Res 1803: 191-200.
    • (2010) Biochim Biophys Acta Mol Cell Res , vol.1803 , pp. 191-200
    • Mellor, H.1
  • 83
    • 56349123945 scopus 로고    scopus 로고
    • Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts
    • Meng W, Mushika Y, Ichii T, Takeichi M (2008) Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts. Cell 135: 948-959.
    • (2008) Cell , vol.135 , pp. 948-959
    • Meng, W.1    Mushika, Y.2    Ichii, T.3    Takeichi, M.4
  • 84
    • 79960718426 scopus 로고    scopus 로고
    • Building distinct actin filament networks review in a common cytoplasm
    • Michelot A, Drubin DG (2011) Building distinct actin filament networks review in a common cytoplasm. Curr Biol 21: R560-R569.
    • (2011) Curr Biol , vol.21 , pp. 560-569
    • Michelot, A.1    Drubin, D.G.2
  • 85
    • 0031952518 scopus 로고    scopus 로고
    • Induction of filopodium formation by a WASPrelated actin-depolymerizing protein N-WASP
    • Miki H, Sasaki T, Takai Y, Takenawa T (1998) Induction of filopodium formation by a WASPrelated actin-depolymerizing protein N-WASP. Nature 391: 93-96.
    • (1998) Nature , vol.391 , pp. 93-96
    • Miki, H.1    Sasaki, T.2    Takai, Y.3    Takenawa, T.4
  • 86
    • 0034465924 scopus 로고    scopus 로고
    • Ultrastructure of the zonula adherens revealed by rapid-freeze deep-etching
    • Miyaguchi K (2000) Ultrastructure of the zonula adherens revealed by rapid-freeze deep-etching. J Struct Biol 132: 169-178.
    • (2000) J Struct Biol , vol.132 , pp. 169-178
    • Miyaguchi, K.1
  • 87
    • 33746038584 scopus 로고    scopus 로고
    • Actomyosin tension is required for correct recruitment of adherens junction components and zonula occludens formation
    • Miyake Y, Inoue N, Nishimura K, Kinoshita N, Hosoya H, Yonemura S (2006) Actomyosin tension is required for correct recruitment of adherens junction components and zonula occludens formation. Exp Cell Res 312: 1637-1650.
    • (2006) Exp Cell Res , vol.312 , pp. 1637-1650
    • Miyake, Y.1    Inoue, N.2    Nishimura, K.3    Kinoshita, N.4    Hosoya, H.5    Yonemura, S.6
  • 88
    • 0014945041 scopus 로고
    • Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments
    • Moore PB, Huxley HE, Derosier DJ (1970) Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J Mol Biol 50: 279-295.
    • (1970) J Mol Biol , vol.50 , pp. 279-295
    • Moore, P.B.1    Huxley, H.E.2    Derosier, D.J.3
  • 89
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins RD, Heuser JA, Pollard TD (1998) The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc Natl Acad Sci U S A 95: 6181-6186.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 90
    • 1842390685 scopus 로고
    • Cell binding function of E-cadherin is regulated by the cytoplasmic domain
    • Nagafuchi A, Takeichi M (1988) Cell binding function of E-cadherin is regulated by the cytoplasmic domain. Embo J 7: 3679-3684.
    • (1988) Embo J , vol.7 , pp. 3679-3684
    • Nagafuchi, A.1    Takeichi, M.2
  • 91
    • 0024755646 scopus 로고
    • Transmembrane control of cadherin-mediated cell-adhesion-A 94 KDa protein functionally associated with a specific region of the cytoplasmic domain of E-cadherin
    • Nagafuchi A, Takeichi M (1989) Transmembrane control of cadherin-mediated cell-adhesion-A 94 KDa protein functionally associated with a specific region of the cytoplasmic domain of E-cadherin. Cell Regul 1: 37-44.
    • (1989) Cell Regul , vol.1 , pp. 37-44
    • Nagafuchi, A.1    Takeichi, M.2
  • 92
    • 0028087729 scopus 로고
    • The roles of catenins in the cadherin-mediated celladhesion-functional-analysis of E-cadherin-alpha catenin fusion molecules
    • Nagafuchi A, Ishihara S, Tsukita S (1994) The roles of catenins in the cadherin-mediated celladhesion-functional-analysis of E-cadherin-alpha catenin fusion molecules. J Cell Biol 127: 235-245.
    • (1994) J Cell Biol , vol.127 , pp. 235-245
    • Nagafuchi, A.1    Ishihara, S.2    Tsukita, S.3
  • 93
    • 32044470440 scopus 로고    scopus 로고
    • Structure of the autoinhibitory switch in formin mDia1
    • Nezami AG, Poy F, Eck MJ (2006) Structure of the autoinhibitory switch in formin mDia1. Struct 14: 257-263.
    • (2006) Struct , vol.14 , pp. 257-263
    • Nezami, A.G.1    Poy, F.2    Eck, M.J.3
  • 94
    • 79955642014 scopus 로고    scopus 로고
    • Tissue organization by Cadherin adhesion molecules: Dynamic molecular and cellular mechanisms of morphogenetic regulation
    • Niessen CM, Leckband D, Yap AS (2011) Tissue organization by Cadherin adhesion molecules: Dynamic molecular and cellular mechanisms of morphogenetic regulation. Physiol Rev 91: 691-731.
    • (2011) Physiol Rev , vol.91 , pp. 691-731
    • Niessen, C.M.1    Leckband, D.2    Yap, A.S.3
  • 96
    • 33847295719 scopus 로고    scopus 로고
    • Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics
    • Jeon KW (ed)
    • Ono S (2007) Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics. In: Jeon KW (ed) International Review of Cytology-a Survey of Cell Biology, vol 258, pp 1-82.
    • (2007) International Review of Cytology-a Survey of Cell Biology , vol.258 , pp. 1-82
    • Ono, S.1
  • 97
    • 33749548025 scopus 로고    scopus 로고
    • Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial cells
    • Otani T, Ichii T, Aono S, Takeichi M (2006) Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial cells. J Cell Biol 175: 135-146.
    • (2006) J Cell Biol , vol.175 , pp. 135-146
    • Otani, T.1    Ichii, T.2    Aono, S.3    Takeichi, M.4
  • 98
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • Otomo T, Tomchick DR, Otomo C, Panchal SC, Machius M, Rosen MK (2005) Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433: 488-494.
    • (2005) Nature , vol.433 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Machius, M.5    Rosen, M.K.6
  • 99
    • 0025651841 scopus 로고
    • A possible new adhesive site in the cell-adhesion molecule uvomorulin
    • Ozawa M, Hoschutzky H, Herrenknecht K, Kemler R (1990) A possible new adhesive site in the cell-adhesion molecule uvomorulin. Mec Dev 33: 49-56.
    • (1990) Mec Dev , vol.33 , pp. 49-56
    • Ozawa, M.1    Hoschutzky, H.2    Herrenknecht, K.3    Kemler, R.4
  • 100
    • 77953637330 scopus 로고    scopus 로고
    • Physical mechanisms of signal integration by WASP family proteins
    • Kornberg RD (ed)
    • Padrick SB, Rosen MK (2010) Physical mechanisms of signal integration by WASP family proteins. In: Kornberg RD (ed) Annual review of biochemistry, vol 79, pp 707-735.
    • (2010) Annual review of biochemistry , vol.79 , pp. 707-735
    • Padrick, S.B.1    Rosen, M.K.2
  • 102
    • 76649113736 scopus 로고    scopus 로고
    • Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin
    • Peng X, Cuff LE, Lawton CD, DeMali KA (2010) Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin. J Cell Sci 123: 567-577.
    • (2010) J Cell Sci , vol.123 , pp. 567-577
    • Peng, X.1    Cuff, L.E.2    Lawton, C.D.3    DeMali, K.A.4
  • 103
    • 0036535898 scopus 로고    scopus 로고
    • The cytoplasmic face of cell contact sites
    • Pokutta S, Weis WI (2002) The cytoplasmic face of cell contact sites. Curr Opin Struct Biol 12: 255-262.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 255-262
    • Pokutta, S.1    Weis, W.I.2
  • 104
    • 0033895234 scopus 로고    scopus 로고
    • Molecular mechanisms controlling actin filament dynamics in nonmuscle cells
    • Pollard TD, Blanchoin L, Mullins RD (2000) Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annu Rev Biophys Biomol Struct 29: 545-576.
    • (2000) Annu Rev Biophys Biomol Struct , vol.29 , pp. 545-576
    • Pollard, T.D.1    Blanchoin, L.2    Mullins, R.D.3
  • 105
    • 69549114949 scopus 로고    scopus 로고
    • WASP and SCAR/WAVE proteins: The drivers of actin assembly
    • Pollitt AY, Insall RH (2009) WASP and SCAR/WAVE proteins: The drivers of actin assembly. J Cell Sci 122: 2575-2578.
    • (2009) J Cell Sci , vol.122 , pp. 2575-2578
    • Pollitt, A.Y.1    Insall, R.H.2
  • 106
    • 70349422245 scopus 로고    scopus 로고
    • Cortactin: Coordinating adhesion and the actin cytoskeleton at cellular protrusions
    • Ren G, Crampton MS, Yap AS (2009a) Cortactin: Coordinating adhesion and the actin cytoskeleton at cellular protrusions. Cell Motil Cytoskeleton 66: 865-873.
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 865-873
    • Ren, G.1    Crampton, M.S.2    Yap, A.S.3
  • 107
    • 67650527139 scopus 로고    scopus 로고
    • Cortactin is a functional target of E-cadherin-activated src family kinases in MCF7 epithelial monolayers
    • Ren G, Helwani FM, Verma S, McLachlan RW, Weed SA, Yap AS (2009b) Cortactin is a functional target of E-cadherin-activated src family kinases in MCF7 epithelial monolayers. J Biol Chem 284: 18913-18922.
    • (2009) J Biol Chem , vol.284 , pp. 18913-18922
    • Ren, G.1    Helwani, F.M.2    Verma, S.3    McLachlan, R.W.4    Weed, S.A.5    Yap, A.S.6
  • 108
    • 0028981208 scopus 로고
    • Alpha(1)(E)-catenin is an actinbinding and actin-bundling protein mediating the attachment of F-actin to the membrane adhesion complex
    • Rimm DL, Koslov ER, Kebriaei P, Cianci CD, Morrow JS (1995) Alpha(1)(E)-catenin is an actinbinding and actin-bundling protein mediating the attachment of F-actin to the membrane adhesion complex. Proc Natl Acad Sci U S A 92: 8813-8817.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8813-8817
    • Rimm, D.L.1    Koslov, E.R.2    Kebriaei, P.3    Cianci, C.D.4    Morrow, J.S.5
  • 109
    • 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 MR, Wittinghofer A (2005) Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature 435: 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
  • 110
    • 78049296901 scopus 로고    scopus 로고
    • WASH, WHAMM and JMY: Regulation of Arp2/3 complex and beyond
    • Rottner K, Haenisch J, Campellone KG (2010) WASH, WHAMM and JMY: Regulation of Arp2/3 complex and beyond. Trends Cell Biol 20: 650-661.
    • (2010) Trends Cell Biol , vol.20 , pp. 650-661
    • Rottner, K.1    Haenisch, J.2    Campellone, K.G.3
  • 112
    • 0036305635 scopus 로고    scopus 로고
    • ROCK and Dia have opposing effects on adherens junctions downstream of Rho
    • Sahai E, Marshall CJ (2002) ROCK and Dia have opposing effects on adherens junctions downstream of Rho. Nat Cell Biol 4: 408-415.
    • (2002) Nat Cell Biol , vol.4 , pp. 408-415
    • Sahai, E.1    Marshall, C.J.2
  • 113
    • 67650472867 scopus 로고    scopus 로고
    • The Drosophila afadin homologue Canoe regulates linkage of the actin cytoskeleton to adherens junctions during apical constriction
    • Sawyer JK, Harris NJ, Slep KC, Gaul U, Peifer M (2009) The Drosophila afadin homologue Canoe regulates linkage of the actin cytoskeleton to adherens junctions during apical constriction. J Cell Biol 186: 57-73.
    • (2009) J Cell Biol , vol.186 , pp. 57-73
    • Sawyer, J.K.1    Harris, N.J.2    Slep, K.C.3    Gaul, U.4    Peifer, M.5
  • 115
    • 79960296387 scopus 로고    scopus 로고
    • A contractile actomyosin network linked to adherens junctions by Canoe/afadin helps drive convergent extension
    • Sawyer JK, Choi W, Jung K-C, He L, Harris NJ, Peifer M (2011) A contractile actomyosin network linked to adherens junctions by Canoe/afadin helps drive convergent extension. Mol Biol Cell 22: 2491-2508.
    • (2011) Mol Biol Cell , vol.22 , pp. 2491-2508
    • Sawyer, J.K.1    Choi, W.2    Jung, K.-C.3    He, L.4    Harris, N.J.5    Peifer, M.6
  • 116
    • 0035142828 scopus 로고    scopus 로고
    • Microtubules don and doff their caps: Dynamic attachments at plus and minus ends
    • Schroer TA (2001) Microtubules don and doff their caps: dynamic attachments at plus and minus ends. Curr Opin Cell Biol 13: 92-96.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 92-96
    • Schroer, T.A.1
  • 117
    • 79952598024 scopus 로고    scopus 로고
    • Integrins and extracellular matrix in mechanotransduction
    • Schwartz MA (2010) Integrins and extracellular matrix in mechanotransduction. Cold Spring Harb Perspect Biol 2: a005066.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Schwartz, M.A.1
  • 118
    • 50849083158 scopus 로고    scopus 로고
    • Cell adhesion receptors in mechanotransduction
    • Schwartz MA, DeSimone DW (2008) Cell adhesion receptors in mechanotransduction. Curr Opin Cell Biol 20: 551-556.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 551-556
    • Schwartz, M.A.1    DeSimone, D.W.2
  • 119
    • 33644865002 scopus 로고    scopus 로고
    • Ena/VASP proteins can regulate distinct modes of actin organization at cadherin-adhesive contacts
    • Scott JA, Shewan AM, den Elzen NR, Loureiro JJ, Gertler FB, Yap AS (2006) Ena/VASP proteins can regulate distinct modes of actin organization at cadherin-adhesive contacts. Mol Biol Cell 17: 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
  • 120
    • 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 AM, Maddugoda M, Kraemer A, Stehbens SJ, Verma S, Kovacs EM, Yap AS (2005) Myosin 2 is a key Rho kinase target necessary for the local concentration of E-cadherin at cell-cell contacts. Mol Biol Cell 16: 4531-4542.
    • (2005) Mol Biol Cell , vol.16 , pp. 4531-4542
    • 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
  • 122
    • 77954414080 scopus 로고    scopus 로고
    • Neighborly relations: Cadherins and mechanotransduction
    • Smutny M, Yap AS (2010) Neighborly relations: Cadherins and mechanotransduction. J Cell Biol 189: 1075-1077.
    • (2010) J Cell Biol , vol.189 , pp. 1075-1077
    • Smutny, M.1    Yap, A.S.2
  • 124
    • 79960681051 scopus 로고    scopus 로고
    • Multicomponent analysis of junctional movements regulated by Myosin II isoforms at the epithelial zonula adherens
    • Smutny M, Wu SK, Gomez GA, MangoldS, Yap AS, Hamilton NA (2011) Multicomponent analysis of junctional movements regulated by Myosin II isoforms at the epithelial zonula adherens. Plos One 6: e22458.
    • (2011) Plos One , vol.6
    • Smutny, M.1    Wu, S.K.2    Gomez, G.A.3    Mangold, S.4    Yap, A.S.5    Hamilton, N.A.6
  • 127
    • 80052614857 scopus 로고    scopus 로고
    • Mechanosensitive EPLIN-dependent remodeling of adherens junctions regulates epithelial reshaping
    • Taguchi K, Ishiuchi T, Takeichi M (2011) Mechanosensitive EPLIN-dependent remodeling of adherens junctions regulates epithelial reshaping. J Cell Biol 194: 643-656.
    • (2011) J Cell Biol , vol.194 , pp. 643-656
    • Taguchi, K.1    Ishiuchi, T.2    Takeichi, M.3
  • 128
    • 0028176572 scopus 로고
    • The development of cellular junctions in the Drosophila embryo
    • Tepass U, Hartenstein V (1994) The development of cellular junctions in the Drosophila embryo. Dev Biology 161: 563-96.
    • (1994) Dev Biology , vol.161 , pp. 563-596
    • Tepass, U.1    Hartenstein, V.2
  • 130
    • 77951977342 scopus 로고    scopus 로고
    • Electron tomography reveals unbranched networks of actin filaments in lamellipodia
    • Urban E, Jacob S, Nemethova M, Resch GP, Small JV (2010) Electron tomography reveals unbranched networks of actin filaments in lamellipodia. Nat Cell Biol 12: 429-U36.
    • (2010) Nat Cell Biol , vol.12 , pp. 429-436
    • Urban, E.1    Jacob, S.2    Nemethova, M.3    Resch, G.P.4    Small, J.V.5
  • 132
    • 0034695656 scopus 로고    scopus 로고
    • Directed actin polymerization is the driving force for epithelial cell-cell adhesion
    • Vasioukhin V, Bauer C, Yin M, Fuchs E (2000) Directed actin polymerization is the driving force for epithelial cell-cell adhesion. Cell 100: 209-219.
    • (2000) Cell , vol.100 , pp. 209-219
    • Vasioukhin, V.1    Bauer, C.2    Yin, M.3    Fuchs, E.4
  • 135
    • 0041758426 scopus 로고    scopus 로고
    • The formins: Active scaffolds that remodel the cytoskeleton
    • Wallar BJ, Alberts AS (2003) The formins: active scaffolds that remodel the cytoskeleton. Trends Cell Biol 13: 435-446.
    • (2003) Trends Cell Biol , vol.13 , pp. 435-446
    • Wallar, B.J.1    Alberts, A.S.2
  • 136
    • 0028129695 scopus 로고
    • Induction of polarized cell-cell association and retardation of growth by activation of the E-cadherin catenin adhesion system in a dispersed carcinoma line
    • Watabe M, Nagafuchi A, Tsukita S, Takeichi M (1994) Induction of polarized cell-cell association and retardation of growth by activation of the E-cadherin catenin adhesion system in a dispersed carcinoma line. J Cell Biol 127: 247-256.
    • (1994) J Cell Biol , vol.127 , pp. 247-256
    • Watabe, M.1    Nagafuchi, A.2    Tsukita, S.3    Takeichi, M.4
  • 138
    • 0033915956 scopus 로고    scopus 로고
    • Feedback interactions between cell-cell adherens junctions and cytoskeletal dynamics in Newt lung epithelial cells
    • Waterman-Storer CM, Salmon WC, Salmon ED (2000) Feedback interactions between cell-cell adherens junctions and cytoskeletal dynamics in Newt lung epithelial cells. Mol Biol Cell 11: 2471-2483.
    • (2000) Mol Biol Cell , vol.11 , pp. 2471-2483
    • Waterman-Storer, C.M.1    Salmon, W.C.2    Salmon, E.D.3
  • 141
    • 0028363603 scopus 로고
    • Dnase-1 increases the rate-constant of depolymerization at the pointed (-) end of actin filament
    • Weber A, Pennise CR, Pring M (1994) Dnase-1 increases the rate-constant of depolymerization at the pointed (-) end of actin filament. Biochem 33: 4780-4786.
    • (1994) Biochem , vol.33 , pp. 4780-4786
    • Weber, A.1    Pennise, C.R.2    Pring, M.3
  • 142
    • 0031696485 scopus 로고    scopus 로고
    • Translocation of cortactin to the cell periphery is mediated by the small GTPase Rac1
    • Weed SA, Du YR, Parsons JT (1998) Translocation of cortactin to the cell periphery is mediated by the small GTPase Rac1. J Cell SciSci 111: 2433-2443.
    • (1998) J Cell SciSci , vol.111 , pp. 2433-2443
    • Weed, S.A.1    Du, Y.R.2    Parsons, J.T.3
  • 143
    • 33845380864 scopus 로고    scopus 로고
    • Re-solving the cadherin-catenin-actin conundrum
    • Weis WI, Nelson WJ (2006) Re-solving the cadherin-catenin-actin conundrum. J Biol Chem 281: 35593-35597.
    • (2006) J Biol Chem , vol.281 , pp. 35593-35597
    • Weis, W.I.1    Nelson, W.J.2
  • 144
    • 0032482254 scopus 로고    scopus 로고
    • Vinculin is part of the cadherin-catenin junctional complex: Complex formation between alpha-catenin and vinculin
    • Weiss EE, Kroemker M, Rudiger AH, Jockusch BM, Rudiger M (1998) Vinculin is part of the cadherin-catenin junctional complex: Complex formation between alpha-catenin and vinculin. J Cell Biol 141: 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
  • 146
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture
    • Xu YW, Moseley JB, Sagot I, Poy F, Pellman D, Goode BL, Eck MJ (2004) Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell 116: 711-723.
    • (2004) Cell , vol.116 , pp. 711-723
    • Xu, Y.W.1    Moseley, J.B.2    Sagot, I.3    Poy, F.4    Pellman, D.5    Goode, B.L.6    Eck, M.J.7
  • 147
    • 34547571737 scopus 로고    scopus 로고
    • Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion
    • Yamada S, Nelson WJ (2007) Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion. J Cell Biol 178: 517-527.
    • (2007) J Cell Biol , vol.178 , pp. 517-527
    • Yamada, S.1    Nelson, W.J.2
  • 148
  • 149
    • 33846847697 scopus 로고    scopus 로고
    • Rac-WAVE-mediated actin reorganization is required for organization and maintenance of cell-cell adhesion
    • Yamazaki D, Oikawa T, Takenawa T (2007) Rac-WAVE-mediated actin reorganization is required for organization and maintenance of cell-cell adhesion. J Cell Sci 120: 86-100.
    • (2007) J Cell Sci , vol.120 , pp. 86-100
    • Yamazaki, D.1    Oikawa, T.2    Takenawa, T.3
  • 150
    • 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 (1997) Lateral clustering of the adhesive ectodomain: A fundamental determinant of cadherin function. Curr Biol 7: 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
  • 151
    • 0032482201 scopus 로고    scopus 로고
    • The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p129(ctn)
    • Yap AS, Niessen CM, Gumbiner BM (1998) The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p129(ctn). J Cell Biol 141: 779-789.
    • (1998) J Cell Biol , vol.141 , pp. 779-789
    • Yap, A.S.1    Niessen, C.M.2    Gumbiner, B.M.3
  • 152
    • 0028821093 scopus 로고
    • Cell-to-cell adherens junction formation and actin filament organization-similarities and differences between non-polarized fibroblasts and polarized epithelial-cells
    • Yonemura S, Itoh M, Nagafuchi A, Tsukita S (1995) Cell-to-cell adherens junction formation and actin filament organization-similarities and differences between non-polarized fibroblasts and polarized epithelial-cells. J Cell Sci 108: 127-142.
    • (1995) J Cell Sci , vol.108 , pp. 127-142
    • Yonemura, S.1    Itoh, M.2    Nagafuchi, A.3    Tsukita, S.4
  • 153
    • 77953123743 scopus 로고    scopus 로고
    • Alpha-catenin as a tension transducer that induces adherens junction development
    • Yonemura S, Wada Y, Watanabe T, Nagafuchi A, Shibata M (2010) Alpha-catenin as a tension transducer that induces adherens junction development. Nat Cell Biol 12: 533-542.
    • (2010) Nat Cell Biol , vol.12 , pp. 533-542
    • Yonemura, S.1    Wada, Y.2    Watanabe, T.3    Nagafuchi, A.4    Shibata, M.5


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