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Volumn 196, Issue 1, 2012, Pages 115-130

α-Actinin-4/FSGS1 is required for Arp2/3-dependent actin assembly at the adherens junction

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; ALPHA ACTININ 4; CADHERIN; CELL PROTEIN; FOCAL SEGMENTAL GLOMERULOSCLEROSIS 1 PROTEIN; UNCLASSIFIED DRUG;

EID: 84856716925     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201103116     Document Type: Article
Times cited : (133)

References (76)
  • 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., M. Takeichi. 2008. EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt. Proc. Natl. Acad. Sci. USA. 105:13-19. http://dx.doi.org/10.1073/pnas.0710504105
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 13-19
    • Abe, K.1    Takeichi, M.2
  • 2
    • 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., Y.T. Chen, S.J. Smith, W.J. Nelson. 1998. Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein. J. Cell Biol. 142:1105-1119. http://dx.doi.org/10.1083/jcb.142.4.1105
    • (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
  • 3
    • 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., A. Barth, W.J. Nelson. 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. http://dx.doi.org/10.1083/jcb.134.2.549
    • (1996) J. Cell Biol. , vol.134 , pp. 549-557
    • Angres, B.1    Barth, A.2    Nelson, W.J.3
  • 4
    • 7444239796 scopus 로고    scopus 로고
    • Magic touch: How does cell-cell adhesion trigger actin assembly?
    • Bershadsky, A. 2004. Magic touch: How does cell-cell adhesion trigger actin assembly? Trends Cell Biol. 14:589-593. http://dx.doi.org/10.1016/j.tcb.2004.09.009
    • (2004) Trends Cell Biol , vol.14 , pp. 589-593
    • Bershadsky, A.1
  • 5
    • 2142654946 scopus 로고    scopus 로고
    • Fascin-mediated propulsion of Listeria monocytogenes independent of frequent nucleation by the Arp2/3 complex
    • Brieher, W.M., M. Coughlin, T.J. Mitchison. 2004. Fascin-mediated propulsion of Listeria monocytogenes independent of frequent nucleation by the Arp2/3 complex. J. Cell Biol. 165:233-242. http://dx.doi.org/10.1083/jcb.200311040
    • (2004) J. Cell Biol. , vol.165 , pp. 233-242
    • Brieher, W.M.1    Coughlin, M.2    Mitchison, T.J.3
  • 6
    • 33750365532 scopus 로고    scopus 로고
    • Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin
    • Brieher, W.M., H.Y. Kueh, B.A. Ballif, T.J. Mitchison. 2006. Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, Aip1. J. Cell Biol. 175:315-324. http://dx.doi.org/10.1083/jcb.200603149
    • (2006) Aip1. J. Cell Biol. , vol.175 , pp. 315-324
    • Brieher, W.M.1    Kueh, H.Y.2    Ballif, B.A.3    Mitchison, T.J.4
  • 7
    • 0027435176 scopus 로고
    • Localization and dynamics of nonfilamentous actin in cultured cells
    • Cao, L.G., D.J. Fishkind, Y.L. Wang. 1993. Localization and dynamics of nonfilamentous actin in cultured cells. J. Cell Biol. 123:173-181. http://dx.doi.org/10.1083/jcb.123.1.173
    • (1993) J. Cell Biol. , vol.123 , pp. 173-181
    • Cao, L.G.1    Fishkind, D.J.2    Wang, Y.L.3
  • 8
    • 36549053109 scopus 로고    scopus 로고
    • Mammalian diaphanous-related formin Dia1 controls the organization of E-cadherinmediated cell-cell junctions
    • Carramusa, L., C. Ballestrem, Y. Zilberman, A.D. Bershadsky. 2007. Mammalian diaphanous-related formin Dia1 controls the organization of E-cadherinmediated cell-cell junctions. J. Cell Sci. 120:3870-3882. http://dx.doi.org/10.1242/jcs.014365
    • (2007) J. Cell Sci. , vol.120 , pp. 3870-3882
    • Carramusa, L.1    Ballestrem, C.2    Zilberman, Y.3    Bershadsky, A.D.4
  • 10
    • 44849115958 scopus 로고    scopus 로고
    • A two-tiered mechanism for stabilization and immobilization of E-cadherin
    • Cavey, M., M. Rauzi, P.F. Lenne, T. Lecuit. 2008. A two-tiered mechanism for stabilization and immobilization of E-cadherin. Nature. 453:751-756. http://dx.doi.org/10.1038/nature06953
    • (2008) Nature , vol.453 , pp. 751-756
    • Cavey, M.1    Rauzi, M.2    Lenne, P.F.3    Lecuit, T.4
  • 11
    • 33750701767 scopus 로고    scopus 로고
    • Reassembly of contractile actin cortex in cell blebs
    • Charras, G.T., C.K. Hu, M. Coughlin, T.J. Mitchison. 2006. Reassembly of contractile actin cortex in cell blebs. J. Cell Biol. 175:477-490. http://dx.doi.org/10.1083/jcb.200602085
    • (2006) J. Cell Biol. , vol.175 , pp. 477-490
    • Charras, G.T.1    Hu, C.K.2    Coughlin, M.3    Mitchison, T.J.4
  • 12
    • 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., W.A. Thomas, O. Eder, F. Pincet, E. Perez, J.P. Thiery, S. Dufour. 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. http://dx.doi.org/10.1083/jcb.200403043
    • (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
  • 13
    • 0037049555 scopus 로고    scopus 로고
    • Recruitment of the Arp2/3 complex to vinculin: Coupling membrane protrusion to matrix adhesion
    • DeMali, K.A., C.A. Barlow, K. Burridge. 2002. Recruitment of the Arp2/3 complex to vinculin: Coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159:881-891. http://dx.doi.org/10.1083/jcb.200206043
    • (2002) J. Cell Biol. , vol.159 , pp. 881-891
    • DeMali, K.A.1    Barlow, C.A.2    Burridge, K.3
  • 14
    • 0022536576 scopus 로고
    • Identification of actin-, alpha-actinin-, and vinculin-containing plaques at the lateral membrane of epithelial cells
    • Drenckhahn, D., H. Franz. 1986. Identification of actin-, alpha-actinin-, and vinculin-containing plaques at the lateral membrane of epithelial cells. J. Cell Biol. 102:1843-1852. http://dx.doi.org/10.1083/jcb.102.5.1843
    • (1986) J. Cell Biol. , vol.102 , pp. 1843-1852
    • Drenckhahn, D.1    Franz, H.2
  • 15
    • 7944237936 scopus 로고    scopus 로고
    • The many faces of filamin: A versatile molecular scaffold for cell motility and signalling
    • Feng, Y., C.A. Walsh. 2004. The many faces of filamin: A versatile molecular scaffold for cell motility and signalling. Nat. Cell Biol. 6:1034-1038. http://dx.doi.org/10.1038/ncb1104-1034
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1034-1038
    • Feng, Y.1    Walsh, C.A.2
  • 16
    • 0019320646 scopus 로고
    • Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin
    • Flanagan, M.D., S. Lin. 1980. Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin. J. Biol. Chem. 255:835-838.
    • (1980) J. Biol. Chem. , vol.255 , pp. 835-838
    • Flanagan, M.D.1    Lin, S.2
  • 17
    • 0024095187 scopus 로고
    • Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone
    • Forscher, P., S.J. Smith. 1988. Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone. J. Cell Biol. 107:1505-1516. http://dx.doi.org/10.1083/jcb.107.4.1505
    • (1988) J. Cell Biol. , vol.107 , pp. 1505-1516
    • Forscher, P.1    Smith, S.J.2
  • 18
    • 77952938686 scopus 로고    scopus 로고
    • Discovering the molecular components of intercellular junctions-a historical view
    • Franke, W.W. 2009. Discovering the molecular components of intercellular junctions-a historical view. Cold Spring Harb. Perspect. Biol. 1:a003061. http://dx.doi.org/10.1101/cshperspect.a003061
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1
    • Franke, W.W.1
  • 19
    • 68349128540 scopus 로고    scopus 로고
    • The junctions that don't fit the scheme: Special symmetrical cell-cell junctions of their own kind
    • Franke, W.W., S. Rickelt, M. Barth, S. Pieperhoff. 2009. The junctions that don't fit the scheme: Special symmetrical cell-cell junctions of their own kind. Cell Tissue Res. 338:1-17. http://dx.doi.org/10.1007/s00441-009-0849-z
    • (2009) Cell Tissue Res , vol.338 , pp. 1-17
    • Franke, W.W.1    Rickelt, S.2    Barth, M.3    Pieperhoff, S.4
  • 20
    • 0035947772 scopus 로고    scopus 로고
    • E-cadherin suppresses cellular transformation by inhibiting β-catenin signaling in an adhesionindependent manner
    • Gottardi, C.J., E. Wong, B.M. Gumbiner. 2001. E-cadherin suppresses cellular transformation by inhibiting β-catenin signaling in an adhesionindependent manner. J. Cell Biol. 153:1049-1060. http://dx.doi.org/10.1083/jcb.153.5.1049
    • (2001) J. Cell Biol. , vol.153 , pp. 1049-1060
    • Gottardi, C.J.1    Wong, E.2    Gumbiner, B.M.3
  • 21
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner, B.M. 1996. Cell adhesion: The molecular basis of tissue architecture and morphogenesis. Cell. 84:345-357. http://dx.doi.org/10.1016/S0092-8674(00)81279-9
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 22
    • 23144442645 scopus 로고    scopus 로고
    • Regulation of cadherin-mediated adhesion in morphogenesis
    • Gumbiner, B.M. 2005. Regulation of cadherin-mediated adhesion in morphogenesis. Nat. Rev. Mol. Cell Biol. 6:622-634. http://dx.doi.org/10.1038/nrm1699
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 622-634
    • Gumbiner, B.M.1
  • 23
    • 59149085104 scopus 로고    scopus 로고
    • Regulated adhesion as a driving force of gastrulation movements
    • Hammerschmidt, M., D. Wedlich. 2008. Regulated adhesion as a driving force of gastrulation movements. Development. 135:3625-3641. http://dx.doi.org/10.1242/dev.015701
    • (2008) Development , vol.135 , pp. 3625-3641
    • Hammerschmidt, M.1    Wedlich, D.2
  • 24
    • 0032502669 scopus 로고    scopus 로고
    • The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton
    • Hazan, R.B., L. Norton. 1998. The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton. J. Biol. Chem. 273:9078-9084. http://dx.doi.org/10.1074/jbc.273.15.9078
    • (1998) J. Biol. Chem. , vol.273 , pp. 9078-9084
    • Hazan, R.B.1    Norton, L.2
  • 25
    • 0026596306 scopus 로고
    • Analysis of the actinbinding domain of alpha-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain
    • Hemmings, L., P.A. Kuhlman, D.R. Critchley. 1992. Analysis of the actinbinding domain of alpha-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain. J. Cell Biol. 116:1369-1380. http://dx.doi.org/10.1083/jcb.116.6.1369
    • (1992) J. Cell Biol. , vol.116 , pp. 1369-1380
    • Hemmings, L.1    Kuhlman, P.A.2    Critchley, D.R.3
  • 26
    • 40049088125 scopus 로고    scopus 로고
    • Mice with altered alpha-actinin-4 expression have distinct morphologic patterns of glomerular disease
    • Henderson, J.M., S. Al-Waheeb, A. Weins, S.V. Dandapani, M.R. Pollak. 2008. Mice with altered alpha-actinin-4 expression have distinct morphologic patterns of glomerular disease. Kidney Int. 73:741-750. http://dx.doi.org/10.1038/sj.ki.5002751
    • (2008) Kidney Int , vol.73 , pp. 741-750
    • Henderson, J.M.1    Al-Waheeb, S.2    Weins, A.3    Dandapani, S.V.4    Pollak, M.R.5
  • 27
    • 0033594088 scopus 로고    scopus 로고
    • Functional domains of α-catenin required for the strong state of cadherin-based cell adhesion
    • Imamura, Y., M. Itoh, Y. Maeno, S. Tsukita, A. Nagafuchi. 1999. Functional domains of α-catenin required for the strong state of cadherin-based cell adhesion. J. Cell Biol. 144:1311-1322. http://dx.doi.org/10.1083/jcb.144.6.1311
    • (1999) J. Cell Biol. , vol.144 , pp. 1311-1322
    • Imamura, Y.1    Itoh, M.2    Maeno, Y.3    Tsukita, S.4    Nagafuchi, A.5
  • 28
    • 0030748548 scopus 로고    scopus 로고
    • Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to α catenin and actin filaments
    • Itoh, M., A. Nagafuchi, S. Moroi, S. Tsukita. 1997. Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to α catenin and actin filaments. J. Cell Biol. 138:181-192. http://dx.doi.org/10.1083/jcb.138.1.181
    • (1997) J. Cell Biol. , vol.138 , pp. 181-192
    • Itoh, M.1    Nagafuchi, A.2    Moroi, S.3    Tsukita, S.4
  • 29
    • 0033601258 scopus 로고    scopus 로고
    • Profilin promotes barbed-end actin filament assembly without lowering the critical concentration
    • Kang, F., D.L. Purich, F.S. Southwick. 1999. Profilin promotes barbed-end actin filament assembly without lowering the critical concentration. J. Biol. Chem. 274:36963-36972. http://dx.doi.org/10.1074/jbc.274.52.36963
    • (1999) J. Biol. Chem. , vol.274 , pp. 36963-36972
    • Kang, F.1    Purich, D.L.2    Southwick, F.S.3
  • 31
    • 0028979956 scopus 로고
    • Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alphacatenin
    • Knudsen, K.A., A.P. Soler, K.R. Johnson, M.J. Wheelock. 1995. Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alphacatenin. J. Cell Biol. 130:67-77. http://dx.doi.org/10.1083/jcb.130.1.67
    • (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
  • 32
    • 1342310742 scopus 로고    scopus 로고
    • Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables
    • Kobielak, A., H.A. Pasolli, E. Fuchs. 2004. Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables. Nat. Cell Biol. 6:21-30. http://dx.doi.org/10.1038/ncb1075
    • (2004) Nat. Cell Biol. , vol.6 , pp. 21-30
    • Kobielak, A.1    Pasolli, H.A.2    Fuchs, E.3
  • 33
    • 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., M. Goodwin, R.G. Ali, A.D. Paterson, A.S. Yap. 2002. 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. http://dx.doi.org/10.1016/S0960-9822(02)00661-9
    • (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
  • 34
    • 79960984867 scopus 로고    scopus 로고
    • N- WASP regulates the epithelial junctional actin cytoskeleton through a non-canonical post-nucleation pathway
    • Kovacs, E.M., S. Verma, R.G. Ali, A. Ratheesh, N.A. Hamilton, A. Akhmanova, A.S. Yap. 2011. N-WASP regulates the epithelial junctional actin cytoskeleton through a non-canonical post-nucleation pathway. Nat. Cell Biol. 13:934-943. http://dx.doi.org/10.1038/ncb2290
    • (2011) Nat. Cell Biol. , vol.13 , pp. 934-943
    • 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
  • 37
    • 34547191723 scopus 로고    scopus 로고
    • Cell surface mechanics and the control of cell shape tissue patterns and morphogenesis
    • Lecuit, T., P.F. Lenne. 2007. Cell surface mechanics and the control of cell shape, tissue patterns and morphogenesis. Nat. Rev. Mol. Cell Biol. 8:633-644. http://dx.doi.org/10.1038/nrm2222
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 633-644
    • Lecuit, T.1    Lenne, P.F.2
  • 38
    • 0033040628 scopus 로고    scopus 로고
    • The Arp2/3 complex: A multifunctional actin organizer
    • Machesky, L.M., K.L. Gould. 1999. The Arp2/3 complex: A multifunctional actin organizer. Curr. Opin. Cell Biol. 11:117-121. http://dx.doi.org/10.1016/S0955-0674(99)80014-3
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 117-121
    • Machesky, L.M.1    Gould, K.L.2
  • 39
    • 14444271574 scopus 로고    scopus 로고
    • Afadin: A novel actin filament-binding protein with one PDZ domain localized at cadherin-based cell-to-cell adherens junction
    • Mandai, K., H. Nakanishi, A. Satoh, H. Obaishi, M. Wada, H. Nishioka, M. Itoh, A. Mizoguchi, T. Aoki, T. Fujimoto, et al. 1997. Afadin: A novel actin filament-binding protein with one PDZ domain localized at cadherin-based cell-to-cell adherens junction. J. Cell Biol. 139:517-528. http://dx.doi.org/10.1083/jcb.139.2.517
    • (1997) J. Cell Biol. , vol.139 , pp. 517-528
    • Mandai, K.1    Nakanishi, H.2    Satoh, A.3    Obaishi, H.4    Wada, M.5    Nishioka, H.6    Itoh, M.7    Mizoguchi, A.8    Aoki, T.9    Fujimoto, T.10
  • 40
    • 0029670514 scopus 로고    scopus 로고
    • Purification and properties of a Ca(2+)-independent barbed-end actin filament capping protein, CapZ, from human polymorphonuclear leukocytes
    • Maun, N.A., D.W. Speicher, M.J. DiNubile, F.S. Southwick. 1996. Purification and properties of a Ca(2+)-independent barbed-end actin filament capping protein, CapZ, from human polymorphonuclear leukocytes. Biochemistry. 35:3518-3524. http://dx.doi.org/10.1021/bi952470p
    • (1996) Biochemistry , vol.35 , pp. 3518-3524
    • Maun, N.A.1    Speicher, D.W.2    DiNubile, M.J.3    Southwick, F.S.4
  • 41
    • 0027398589 scopus 로고
    • Spatial and temporal dissection of immediate and early events following cadherin-mediated epithelial cell adhesion
    • McNeill, H., T.A. Ryan, S.J. Smith, W.J. Nelson. 1993. Spatial and temporal dissection of immediate and early events following cadherin-mediated epithelial cell adhesion. J. Cell Biol. 120:1217-1226. http://dx.doi.org/10.1083/jcb.120.5.1217
    • (1993) J. Cell Biol. , vol.120 , pp. 1217-1226
    • McNeill, H.1    Ryan, T.A.2    Smith, S.J.3    Nelson, W.J.4
  • 42
    • 33748443594 scopus 로고    scopus 로고
    • Regulation of cell-cell junctions by the cytoskeleton
    • Mège, R.M., J. Gavard, M. Lambert. 2006. Regulation of cell-cell junctions by the cytoskeleton. Curr. Opin. Cell Biol. 18:541-548. http://dx.doi.org/10.1016/j.ceb.2006.08.004
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 541-548
    • Mège, R.M.1    Gavard, J.2    Lambert, M.3
  • 43
    • 33748417728 scopus 로고    scopus 로고
    • FSGSassociated alpha-actinin-4 (K256E) impairs cytoskeletal dynamics in podocytes
    • Michaud, J.L., K.M. Chaisson, R.J. Parks, C.R. Kennedy. 2006. FSGSassociated alpha-actinin-4 (K256E) impairs cytoskeletal dynamics in podocytes. Kidney Int. 70:1054-1061. http://dx.doi.org/10.1038/sj.ki.5001665
    • (2006) Kidney Int , vol.70 , pp. 1054-1061
    • Michaud, J.L.1    Chaisson, K.M.2    Parks, R.J.3    Kennedy, C.R.4
  • 44
    • 57349197819 scopus 로고    scopus 로고
    • Morphogenetic cell movements: Diversity from modular mechanical properties
    • Montell, D.J. 2008. Morphogenetic cell movements: Diversity from modular mechanical properties. Science. 322:1502-1505. http://dx.doi.org/10.1126/science.1164073
    • (2008) Science , vol.322 , pp. 1502-1505
    • Montell, D.J.1
  • 45
    • 0033775855 scopus 로고    scopus 로고
    • Latrunculin alters the actin-monomer subunit interface to prevent polymerization
    • Morton, W.M., K.R. Ayscough, P.J. McLaughlin. 2000. Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Nat. Cell Biol. 2:376-378. http://dx.doi.org/10.1038/35014075
    • (2000) Nat. Cell Biol. , vol.2 , pp. 376-378
    • Morton, W.M.1    Ayscough, K.R.2    McLaughlin, P.J.3
  • 46
    • 67650760556 scopus 로고    scopus 로고
    • N- and E-cadherins in Xenopus are specifically required in the neural and nonneural ectoderm, respectively, for F-actin assembly and morphogenetic movements
    • Nandadasa, S., Q. Tao, N.R. Menon, J. Heasman, C. Wylie. 2009. N- and E-cadherins in Xenopus are specifically required in the neural and nonneural ectoderm, respectively, for F-actin assembly and morphogenetic movements. Development. 136:1327-1338. http://dx.doi.org/10.1242/dev.031203
    • (2009) Development , vol.136 , pp. 1327-1338
    • Nandadasa, S.1    Tao, Q.2    Menon, N.R.3    Heasman, J.4    Wylie, C.5
  • 48
    • 2442481067 scopus 로고    scopus 로고
    • Alpha-actinin revisited: A fresh look at an old player
    • Otey, C.A., O. Carpen. 2004. Alpha-actinin revisited: A fresh look at an old player. Cell Motil. Cytoskeleton. 58:104-111. http://dx.doi.org/10.1002/cm.20007
    • (2004) Cell Motil. Cytoskeleton. , vol.58 , pp. 104-111
    • Otey, C.A.1    Carpen, O.2
  • 49
    • 44349090393 scopus 로고    scopus 로고
    • Ena/VASP proteins capture actin filament barbed ends
    • Pasic, L., T. Kotova, D.A. Schafer. 2008. Ena/VASP proteins capture actin filament barbed ends. J. Biol. Chem. 283:9814-9819. http://dx.doi.org/10.1074/jbc.M710475200
    • (2008) J. Biol. Chem. , vol.283 , pp. 9814-9819
    • Pasic, L.1    Kotova, T.2    Schafer, D.A.3
  • 50
    • 0026589150 scopus 로고
    • Profilin-actin complexes directly elongate actin filaments at the barbed end
    • Pring, M., A. Weber, M.R. Bubb. 1992. Profilin-actin complexes directly elongate actin filaments at the barbed end. Biochemistry. 31:1827-1836. http://dx.doi.org/10.1021/bi00121a035
    • (1992) Biochemistry , vol.31 , pp. 1827-1836
    • Pring, M.1    Weber, A.2    Bubb, M.R.3
  • 51
    • 57049160895 scopus 로고    scopus 로고
    • Nature and anisotropy of cortical forces orienting Drosophila tissue morphogenesis
    • Rauzi, M., P. Verant, T. Lecuit, P.F. Lenne. 2008. Nature and anisotropy of cortical forces orienting Drosophila tissue morphogenesis. Nat. Cell Biol. 10:1401-1410. http://dx.doi.org/10.1038/ncb1798
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1401-1410
    • Rauzi, M.1    Verant, P.2    Lecuit, T.3    Lenne, P.F.4
  • 52
    • 0028981208 scopus 로고
    • Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex
    • Rimm, D.L., E.R. Koslov, P. Kebriaei, C.D. Cianci, J.S. Morrow. 1995. Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex. Proc. Natl. Acad. Sci. USA. 92:8813-8817. http://dx.doi.org/10.1073/pnas.92.19.8813
    • (1995) Proc. Natl. Acad. Sci. USA. , vol.92 , pp. 8813-8817
    • Rimm, D.L.1    Koslov, E.R.2    Kebriaei, P.3    Cianci, C.D.4    Morrow, J.S.5
  • 53
    • 72049090358 scopus 로고    scopus 로고
    • Identification and characterization of a small molecule inhibitor of formin-mediated actin assembly
    • Rizvi, S.A., E.M. Neidt, J. Cui, Z. Feiger, C.T. Skau, M.L. Gardel, S.A. Kozmin, D.R. Kovar. 2009. Identification and characterization of a small molecule inhibitor of formin-mediated actin assembly. Chem. Biol. 16:1158-1168. http://dx.doi.org/10.1016/j.chembiol.2009.10.006
    • (2009) Chem. Biol. , vol.16 , pp. 1158-1168
    • Rizvi, S.A.1    Neidt, E.M.2    Cui, J.3    Feiger, Z.4    Skau, C.T.5    Gardel, M.L.6    Kozmin, S.A.7    Kovar, D.R.8
  • 54
    • 67650472867 scopus 로고    scopus 로고
    • The Drosophila afadin homologue Canoe regulates linkage of the actin cytoskeleton to adherens junctions during apical constriction
    • Sawyer, J.K., N.J. Harris, K.C. Slep, U. Gaul, M. Peifer. 2009. The Drosophila afadin homologue Canoe regulates linkage of the actin cytoskeleton to adherens junctions during apical constriction. J. Cell Biol. 186:57-73. http://dx.doi.org/10.1083/jcb.200904001
    • (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
  • 55
    • 33745058119 scopus 로고    scopus 로고
    • The podocyte's response to injury: Role in proteinuria and glomerulosclerosis
    • Shankland, S.J. 2006. The podocyte's response to injury: Role in proteinuria and glomerulosclerosis. Kidney Int. 69:2131-2147. http://dx.doi.org/10.1038/sj.ki.5000410
    • (2006) Kidney Int , vol.69 , pp. 2131-2147
    • Shankland, S.J.1
  • 56
    • 0038109935 scopus 로고    scopus 로고
    • The cell junction protein VAB-9 regulates adhesion and epidermal morphology in C. elegans
    • Simske, J.S., M. Köppen, P. Sims, J. Hodgkin, A. Yonkof, J. Hardin. 2003. The cell junction protein VAB-9 regulates adhesion and epidermal morphology in C. elegans. Nat. Cell Biol. 5:619-625. http://dx.doi.org/10.1038/ncb1002
    • (2003) Nat. Cell Biol. , vol.5 , pp. 619-625
    • Simske, J.S.1    Köppen, M.2    Sims, P.3    Hodgkin, J.4    Yonkof, A.5    Hardin, J.6
  • 57
    • 33745611527 scopus 로고    scopus 로고
    • Gastrulation in zebrafish - all just about adhesion?
    • Solnica-Krezel, L. 2006. Gastrulation in zebrafish - all just about adhesion? Curr. Opin. Genet. Dev. 16:433-441. http://dx.doi.org/10.1016/j.gde.2006.06.009
    • (2006) Curr. Opin. Genet. Dev. , vol.16 , pp. 433-441
    • Solnica-Krezel, L.1
  • 58
    • 34248200358 scopus 로고    scopus 로고
    • Proteomic and bioinformatic analysis of epithelial tight junction reveals an unexpected cluster of synaptic molecules
    • Tang, V.W. 2006. Proteomic and bioinformatic analysis of epithelial tight junction reveals an unexpected cluster of synaptic molecules. Biol. Direct. 1:37. http://dx.doi.org/10.1186/1745-6150-1-37
    • (2006) Biol. Direct. , vol.1 , pp. 37
    • Tang, V.W.1
  • 59
    • 34547727349 scopus 로고    scopus 로고
    • G- proteincoupled signals control cortical actin assembly by controlling cadherin expression in the early Xenopus embryo
    • Tao, Q., S. Nandadasa, P.D. McCrea, J. Heasman, C. Wylie. 2007. G-proteincoupled signals control cortical actin assembly by controlling cadherin expression in the early Xenopus embryo. Development. 134:2651-2661. http://dx.doi.org/10.1242/dev.002824
    • (2007) Development , vol.134 , pp. 2651-2661
    • Tao, Q.1    Nandadasa, S.2    McCrea, P.D.3    Heasman, J.4    Wylie, C.5
  • 60
    • 55749101603 scopus 로고    scopus 로고
    • New insights into cadherin function in epidermal sheet formation and maintenance of tissue integrity
    • Tinkle, C.L., H.A. Pasolli, N. Stokes, E. Fuchs. 2008. New insights into cadherin function in epidermal sheet formation and maintenance of tissue integrity. Proc. Natl. Acad. Sci. USA. 105:15405-15410. http://dx.doi.org/10.1073/pnas.0807374105
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 15405-15410
    • Tinkle, C.L.1    Pasolli, H.A.2    Stokes, N.3    Fuchs, E.4
  • 61
    • 0026071148 scopus 로고
    • Binding of actin to liver cell membranes: The state of membrane-bound actin
    • Tranter, M.P., S.P. Sugrue, M.A. Schwartz. 1991. Binding of actin to liver cell membranes: The state of membrane-bound actin. J. Cell Biol. 112:891-901. http://dx.doi.org/10.1083/jcb.112.5.891
    • (1991) J. Cell Biol. , vol.112 , pp. 891-901
    • Tranter, M.P.1    Sugrue, S.P.2    Schwartz, M.A.3
  • 62
    • 0031967863 scopus 로고    scopus 로고
    • Sites of monomeric actin incorporation in living PtK2 and REF-52 cells
    • Turnacioglu, K.K., J.W. Sanger, J.M. Sanger. 1998. Sites of monomeric actin incorporation in living PtK2 and REF-52 cells. Cell Motil. Cytoskeleton. 40:59-70. http://dx.doi.org/10.1002/(SICI)1097-0169(1998)40:1<59::AIDCM6>3.0.CO;2-A
    • (1998) Cell Motil. Cytoskeleton. , vol.40 , pp. 59-70
    • Turnacioglu, K.K.1    Sanger, J.W.2    Sanger, J.M.3
  • 63
    • 67249154039 scopus 로고    scopus 로고
    • Trafficking and cell migration
    • Ulrich, F., C.P. Heisenberg. 2009. Trafficking and cell migration. Traffic. 10:811-818. http://dx.doi.org/10.1111/j.1600-0854.2009.00929.x
    • (2009) Traffic , vol.10 , pp. 811-818
    • Ulrich, F.1    Heisenberg, C.P.2
  • 64
    • 0034695656 scopus 로고    scopus 로고
    • Directed actin polymerization is the driving force for epithelial cell-cell adhesion
    • Vasioukhin, V., C. Bauer, M. Yin, E. Fuchs. 2000. Directed actin polymerization is the driving force for epithelial cell-cell adhesion. Cell. 100: 209-219. http://dx.doi.org/10.1016/S0092-8674(00)81559-7
    • (2000) Cell , vol.100 , pp. 209-219
    • Vasioukhin, V.1    Bauer, C.2    Yin, M.3    Fuchs, E.4
  • 67
    • 0020082249 scopus 로고
    • High-affinity interaction of vinculin with actin filaments in vitro
    • Wilkins, J.A., S. Lin. 1982. High-affinity interaction of vinculin with actin filaments in vitro. Cell. 28:83-90. http://dx.doi.org/10.1016/0092-8674(82)90377-4
    • (1982) Cell , vol.28 , pp. 83-90
    • Wilkins, J.A.1    Lin, S.2
  • 69
    • 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., K. Irie, A. Fukuhara, T. Ooshio, Y. Takai. 2004. 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. 9:843-855. http://dx.doi.org/10.1111/j.1365-2443.2004.00768.x
    • (2004) Genes Cells , vol.9 , pp. 843-855
    • Yamada, A.1    Irie, K.2    Fukuhara, A.3    Ooshio, T.4    Takai, Y.5
  • 70
    • 28344433073 scopus 로고    scopus 로고
    • Deconstructing the cadherin-catenin-actin complex
    • Yamada, S., S. Pokutta, F. Drees, W.I. Weis, W.J. Nelson. 2005. Deconstructing the cadherin-catenin-actin complex. Cell. 123:889-901. http://dx.doi.org/10.1016/j.cell.2005.09.020
    • (2005) Cell , vol.123 , pp. 889-901
    • Yamada, S.1    Pokutta, S.2    Drees, F.3    Weis, W.I.4    Nelson, W.J.5
  • 71
    • 0037387121 scopus 로고    scopus 로고
    • Crystal structure of CapZ: Structural basis for actin filament barbed end capping
    • Yamashita, A., K. Maeda, Y. Maéda. 2003. Crystal structure of CapZ: Structural basis for actin filament barbed end capping. EMBO J. 22:1529-1538. http://dx.doi.org/10.1093/emboj/cdg167
    • (2003) EMBO J , vol.22 , pp. 1529-1538
    • Yamashita, A.1    Maeda, K.2    Maéda, Y.3
  • 72
    • 16644399642 scopus 로고    scopus 로고
    • Alpha-actinin-4-mediated FSGS: An inherited kidney disease caused by an aggregated and rapidly degraded cytoskeletal protein
    • Yao, J., T.C. Le, C.H. Kos, J.M. Henderson, P.G. Allen, B.M. Denker, M.R. Pollak. 2004. Alpha-actinin-4-mediated FSGS: An inherited kidney disease caused by an aggregated and rapidly degraded cytoskeletal protein. PLoS Biol. 2:e167. http://dx.doi.org/10.1371/journal.pbio.0020167
    • (2004) PLoS Biol , vol.2
    • Yao, J.1    Le, T.C.2    Kos, C.H.3    Henderson, J.M.4    Allen, P.G.5    Denker, B.M.6    Pollak, M.R.7
  • 73
    • 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., M. Itoh, A. Nagafuchi, S. Tsukita. 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
  • 74
    • 77953123743 scopus 로고    scopus 로고
    • alpha-Catenin as a tension transducer that induces adherens junction development
    • Yonemura, S., Y. Wada, T. Watanabe, A. Nagafuchi, M. Shibata. 2010. alpha-Catenin as a tension transducer that induces adherens junction development. Nat. Cell Biol. 12:533-542. http://dx.doi.org/10.1038/ncb2055
    • (2010) Nat. Cell Biol. , vol.12 , pp. 533-542
    • Yonemura, S.1    Wada, Y.2    Watanabe, T.3    Nagafuchi, A.4    Shibata, M.5
  • 75
    • 4444254413 scopus 로고    scopus 로고
    • Yeast actin patches are networks of branched actin filaments
    • Young, M.E., J.A. Cooper, P.C. Bridgman. 2004. Yeast actin patches are networks of branched actin filaments. J. Cell Biol. 166:629-635. http://dx.doi.org/10.1083/jcb.200404159
    • (2004) J. Cell Biol. , vol.166 , pp. 629-635
    • Young, M.E.1    Cooper, J.A.2    Bridgman, P.C.3
  • 76
    • 30544433202 scopus 로고    scopus 로고
    • Actin at cell-cell junctions is composed of two dynamic and functional populations
    • Zhang, J., M. Betson, J. Erasmus, K. Zeikos, M. Bailly, L.P. Cramer, V.M. Braga. 2005. Actin at cell-cell junctions is composed of two dynamic and functional populations. J. Cell Sci. 118:5549-5562. http://dx.doi.org/10.1242/jcs.02639
    • (2005) J. Cell Sci. , vol.118 , pp. 5549-5562
    • Zhang, J.1    Betson, M.2    Erasmus, J.3    Zeikos, K.4    Bailly, M.5    Cramer, L.P.6    Braga, V.M.7


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