메뉴 건너뛰기




Volumn 140, Issue 20, 2013, Pages 4266-4276

A dominant-negative provides new insights into FAK regulation and function in early embryonic morphogenesis

Author keywords

Dominant negative; Epiboly; FAK; FERM; Xenopus

Indexed keywords

FIBRONECTIN; FOCAL ADHESION KINASE;

EID: 84884951627     PISSN: 09501991     EISSN: 14779129     Source Type: Journal    
DOI: 10.1242/dev.096073     Document Type: Article
Times cited : (23)

References (52)
  • 3
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src family kinases
    • Calalb, M. B., Polte, T. R. and Hanks, S. K. (1995). Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. Mol. Cell. Biol. 15, 954-963.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 4
    • 33644863663 scopus 로고    scopus 로고
    • Crystal structure of the FERM domain of focal adhesion kinase
    • Ceccarelli, D. F., Song, H. K., Poy, F., Schaller, M. D. and Eck, M. J. (2006). Crystal structure of the FERM domain of focal adhesion kinase. J. Biol. Chem. 281, 252-259.
    • (2006) J. Biol. Chem. , vol.281 , pp. 252-259
    • Ceccarelli, D.F.1    Song, H.K.2    Poy, F.3    Schaller, M.D.4    Eck, M.J.5
  • 5
    • 33745468872 scopus 로고    scopus 로고
    • Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factorinduced cell invasion
    • Chen, S. Y. and Chen, H. C. (2006). Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factorinduced cell invasion. Mol. Cell. Biol. 26, 5155-5167.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5155-5167
    • Chen, S.Y.1    Chen, H.C.2
  • 8
    • 0242495710 scopus 로고    scopus 로고
    • Regulation of focal adhesion kinase by its amino-terminal domain through an autoinhibitory interaction
    • Cooper, L. A., Shen, T. L. and Guan, J. L. (2003). Regulation of focal adhesion kinase by its amino-terminal domain through an autoinhibitory interaction. Mol. Cell. Biol. 23, 8030-8041.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8030-8041
    • Cooper, L.A.1    Shen, T.L.2    Guan, J.L.3
  • 9
    • 33646186048 scopus 로고    scopus 로고
    • Integrin alpha5beta1 and fibronectin regulate polarized cell protrusions required for Xenopus convergence and extension
    • Davidson, L. A., Marsden, M., Keller, R. and Desimone, D. W. (2006). Integrin alpha5beta1 and fibronectin regulate polarized cell protrusions required for Xenopus convergence and extension. Curr. Biol. 16, 833-844.
    • (2006) Curr. Biol. , vol.16 , pp. 833-844
    • Davidson, L.A.1    Marsden, M.2    Keller, R.3    Desimone, D.W.4
  • 10
    • 77956302465 scopus 로고    scopus 로고
    • Focal adhesion kinase is essential for cardiac looping and multichamber heart formation
    • Doherty, J. T., Conlon, F. L., Mack, C. P. and Taylor, J. M. (2010). Focal adhesion kinase is essential for cardiac looping and multichamber heart formation. Genesis 48, 492-504.
    • (2010) Genesis , vol.48 , pp. 492-504
    • Doherty, J.T.1    Conlon, F.L.2    Mack, C.P.3    Taylor, J.M.4
  • 11
    • 20444370219 scopus 로고    scopus 로고
    • Microtubuleinduced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase
    • Ezratty, E. J., Partridge, M. A. and Gundersen, G. G. (2005). Microtubuleinduced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase. Nat. Cell Biol. 7, 581-590.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 581-590
    • Ezratty, E.J.1    Partridge, M.A.2    Gundersen, G.G.3
  • 12
    • 79959892925 scopus 로고    scopus 로고
    • Focal adhesion kinase protein regulates Wnt3a gene expression to control cell fate specification in the developing neural plate
    • Fonar, Y., Gutkovich, Y. E., Root, H., Malyarova, A., Aamar, E., Golubovskaya, V. M., Elias, S., Elkouby, Y. M. and Frank, D. (2011). Focal adhesion kinase protein regulates Wnt3a gene expression to control cell fate specification in the developing neural plate. Mol. Biol. Cell 22, 2409-2421.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2409-2421
    • Fonar, Y.1    Gutkovich, Y.E.2    Root, H.3    Malyarova, A.4    Aamar, E.5    Golubovskaya, V.M.6    Elias, S.7    Elkouby, Y.M.8    Frank, D.9
  • 13
    • 0028783271 scopus 로고
    • Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK
    • Furuta, Y., Ilić, D., Kanazawa, S., Takeda, N., Yamamoto, T. and Aizawa, S. (1995). Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK. Oncogene 11, 1989-1995.
    • (1995) Oncogene , vol.11 , pp. 1989-1995
    • Furuta, Y.1    Ilić, D.2    Kanazawa, S.3    Takeda, N.4    Yamamoto, T.5    Aizawa, S.6
  • 14
    • 0027379724 scopus 로고
    • Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin
    • George, E. L., Georges-Labouesse, E. N., Patel-King, R. S., Rayburn, H. and Hynes, R. O. (1993). Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development 119, 1079-1091.
    • (1993) Development , vol.119 , pp. 1079-1091
    • George, E.L.1    Georges-Labouesse, E.N.2    Patel-King, R.S.3    Rayburn, H.4    Hynes, R.O.5
  • 15
    • 21644466387 scopus 로고    scopus 로고
    • Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53
    • Golubovskaya, V. M., Finch, R. and Cance, W. G. (2005). Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53. J. Biol. Chem. 280, 25008-25021.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25008-25021
    • Golubovskaya, V.M.1    Finch, R.2    Cance, W.G.3
  • 16
    • 0036172186 scopus 로고    scopus 로고
    • The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin
    • Hayashi, I., Vuori, K. and Liddington, R. C. (2002). The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin. Nat. Struct. Biol. 9, 101-106.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 101-106
    • Hayashi, I.1    Vuori, K.2    Liddington, R.C.3
  • 17
    • 0029153296 scopus 로고
    • Molecular analysis and developmental expression of the focal adhesion kinase pp125FAK in Xenopus laevis
    • Hens, M. D. and DeSimone, D. W. (1995). Molecular analysis and developmental expression of the focal adhesion kinase pp125FAK in Xenopus laevis. Dev. Biol. 170, 274-288.
    • (1995) Dev. Biol. , vol.170 , pp. 274-288
    • Hens, M.D.1    DeSimone, D.W.2
  • 18
    • 0027428367 scopus 로고
    • Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions
    • Hildebrand, J. D., Schaller, M. D. and Parsons, J. T. (1993). Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions. J. Cell Biol. 123, 993-1005.
    • (1993) J. Cell Biol. , vol.123 , pp. 993-1005
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 19
    • 0029055784 scopus 로고
    • Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase
    • Hildebrand, J. D., Schaller, M. D. and Parsons, J. T. (1995). Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol. Biol. Cell 6, 637-647.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 637-647
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 22
    • 23044467828 scopus 로고    scopus 로고
    • A truncated FAK lacking the FERM domain displays high catalytic activity but retains responsiveness to adhesionmediated signals
    • Jácamo, R. O. and Rozengurt, E. (2005). A truncated FAK lacking the FERM domain displays high catalytic activity but retains responsiveness to adhesionmediated signals. Biochem. Biophys. Res. Commun. 334, 1299-1304.
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 1299-1304
    • Jácamo, R.O.1    Rozengurt, E.2
  • 23
    • 0019225669 scopus 로고
    • The cellular basis of epiboly: An SEM study of deep-cell rearrangement during gastrulation in Xenopus laevis
    • Keller, R. E. (1980). The cellular basis of epiboly: an SEM study of deep-cell rearrangement during gastrulation in Xenopus laevis. J. Embryol. Exp. Morphol. 60, 201-234.
    • (1980) J. Embryol. Exp. Morphol. , vol.60 , pp. 201-234
    • Keller, R.E.1
  • 24
    • 0027481383 scopus 로고
    • Xenopus Gastrulation without a blastocoel roof
    • Keller, R. and Jansa, S. (1992). Xenopus Gastrulation without a blastocoel roof. Dev. Dyn. 195, 162-176.
    • (1992) Dev. Dyn. , vol.195 , pp. 162-176
    • Keller, R.1    Jansa, S.2
  • 26
    • 84867243955 scopus 로고    scopus 로고
    • Integrin adhesions: Who's on first? What's on second? Connections between FAK and talin
    • Lawson, C. and Schlaepfer, D. D. (2012). Integrin adhesions: who's on first? What's on second? Connections between FAK and talin. Cell Adh. Migr. 6, 302-306.
    • (2012) Cell Adh. Migr. , vol.6 , pp. 302-306
    • Lawson, C.1    Schlaepfer, D.D.2
  • 28
    • 38349058006 scopus 로고    scopus 로고
    • PyK2 and FAK connections to p190Rho guanine nucleotide exchange factor regulate RhoA activity, focal adhesion formation, and cell motility
    • Lim, Y., Lim, S. T., Tomar, A., Gardel, M., Bernard-Trifilo, J. A., Chen, X. L., Uryu, S. A., Canete-Soler, R., Zhai, J., Lin, H. et al. (2008b). PyK2 and FAK connections to p190Rho guanine nucleotide exchange factor regulate RhoA activity, focal adhesion formation, and cell motility. J. Cell Biol. 180, 187-203.
    • (2008) J. Cell Biol. , vol.180 , pp. 187-203
    • Lim, Y.1    Lim, S.T.2    Tomar, A.3    Gardel, M.4    Bernard-Trifilo, J.A.5    Chen, X.L.6    Uryu, S.A.7    Canete-Soler, R.8    Zhai, J.9    Lin, H.10
  • 29
    • 0034796439 scopus 로고    scopus 로고
    • Regulation of cell polarity, radial intercalation and epiboly in Xenopus: Novel roles for integrin and fibronectin
    • Marsden, M. and DeSimone, D. W. (2001). Regulation of cell polarity, radial intercalation and epiboly in Xenopus: novel roles for integrin and fibronectin. Development 128, 3635-3647.
    • (2001) Development , vol.128 , pp. 3635-3647
    • Marsden, M.1    DeSimone, D.W.2
  • 30
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: In command and control of cell motility
    • Mitra, S. K., Hanson, D. A. and Schlaepfer, D. D. (2005). Focal adhesion kinase: in command and control of cell motility. Nat. Rev. Mol. Cell Biol. 6, 56-68.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 31
    • 66149099270 scopus 로고    scopus 로고
    • Role of focal adhesion kinase Ser-732 phosphorylation in centrosome function during mitosis
    • Park, A. Y., Shen, T. L., Chien, S. and Guan, J. L. (2009). Role of focal adhesion kinase Ser-732 phosphorylation in centrosome function during mitosis. J. Biol. Chem. 284, 9418-9425.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9418-9425
    • Park, A.Y.1    Shen, T.L.2    Chien, S.3    Guan, J.L.4
  • 33
    • 0033731010 scopus 로고    scopus 로고
    • Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover
    • Ren, X. D., Kiosses, W. B., Sieg, D. J., Otey, C. A., Schlaepfer, D. D. and Schwartz, M. A. (2000). Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover. J. Cell Sci. 113, 3673-3678.
    • (2000) J. Cell Sci. , vol.113 , pp. 3673-3678
    • Ren, X.D.1    Kiosses, W.B.2    Sieg, D.J.3    Otey, C.A.4    Schlaepfer, D.D.5    Schwartz, M.A.6
  • 34
    • 0030694182 scopus 로고    scopus 로고
    • Inhibition of cell spreading by expression of the C-terminal domain of focal adhesion kinase (FAK) is rescued by coexpression of Src or catalytically inactive FAK: A role for paxillin tyrosine phosphorylation
    • Richardson, A., Malik, R. K., Hildebrand, J. D. and Parsons, J. T. (1997). Inhibition of cell spreading by expression of the C-terminal domain of focal adhesion kinase (FAK) is rescued by coexpression of Src or catalytically inactive FAK: a role for paxillin tyrosine phosphorylation. Mol. Cell. Biol. 17, 6906-6914.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6906-6914
    • Richardson, A.1    Malik, R.K.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 35
    • 60549114314 scopus 로고    scopus 로고
    • The physical state of fibronectin matrix differentially regulates morphogenetic movements in vivo
    • Rozario, T., Dzamba, B., Weber, G. F., Davidson, L. A. and DeSimone, D. W. (2009). The physical state of fibronectin matrix differentially regulates morphogenetic movements in vivo. Dev. Biol. 327, 386-398.
    • (2009) Dev. Biol. , vol.327 , pp. 386-398
    • Rozario, T.1    Dzamba, B.2    Weber, G.F.3    Davidson, L.A.4    DeSimone, D.W.5
  • 36
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • Schaller, M. D., Hildebrand, J. D., Shannon, J. D., Fox, J. W., Vines, R. R. and Parsons, J. T. (1994). Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol. Cell. Biol. 14, 1680-1688.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5    Parsons, J.T.6
  • 37
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains
    • Schaller, M. D., Otey, C. A., Hildebrand, J. D. and Parsons, J. T. (1995). Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains. J. Cell Biol. 130, 1181-1187.
    • (1995) J. Cell Biol. , vol.130 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 38
  • 39
    • 0032820782 scopus 로고    scopus 로고
    • Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration
    • Sieg, D. J., Hauck, C. R. and Schlaepfer, D. D. (1999). Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration. J. Cell Sci. 112, 2677-2691.
    • (1999) J. Cell Sci. , vol.112 , pp. 2677-2691
    • Sieg, D.J.1    Hauck, C.R.2    Schlaepfer, D.D.3
  • 41
    • 0025932959 scopus 로고
    • Injected Xwnt-8 RNA acts early in Xenopus embryos to promote formation of a vegetal dorsalizing center
    • Smith, W. C. and Harland, R. M. (1991). Injected Xwnt-8 RNA acts early in Xenopus embryos to promote formation of a vegetal dorsalizing center. Cell 67, 753-765.
    • (1991) Cell , vol.67 , pp. 753-765
    • Smith, W.C.1    Harland, R.M.2
  • 42
    • 70349543966 scopus 로고    scopus 로고
    • Imaging morphogenesis, in Xenopus with Quantum Dot nanocrystals
    • Stylianou, P. and Skourides, P. A. (2009). Imaging morphogenesis, in Xenopus with Quantum Dot nanocrystals. Mech. Dev. 126, 828-841.
    • (2009) Mech. Dev. , vol.126 , pp. 828-841
    • Stylianou, P.1    Skourides, P.A.2
  • 43
    • 0028980418 scopus 로고
    • Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK
    • Tachibana, K., Sato, T., D'Avirro, N. and Morimoto, C. (1995). Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK. J. Exp. Med. 182, 1089-1099.
    • (1995) J. Exp. Med. , vol.182 , pp. 1089-1099
    • Tachibana, K.1    Sato, T.2    D'Avirro, N.3    Morimoto, C.4
  • 44
    • 0035137373 scopus 로고    scopus 로고
    • Selective expression of an endogenous inhibitor of FAK regulates proliferation and migration of vascular smooth muscle cells
    • Taylor, J. M., Mack, C. P., Nolan, K., Regan, C. P., Owens, G. K. and Parsons, J. T. (2001). Selective expression of an endogenous inhibitor of FAK regulates proliferation and migration of vascular smooth muscle cells. Mol. Cell. Biol. 21, 1565-1572.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1565-1572
    • Taylor, J.M.1    Mack, C.P.2    Nolan, K.3    Regan, C.P.4    Owens, G.K.5    Parsons, J.T.6
  • 45
    • 69449103232 scopus 로고    scopus 로고
    • A FAK-p120RasGAPp190RhoGAP complex regulates polarity in migrating cells
    • Tomar, A., Lim, S. T., Lim, Y. and Schlaepfer, D. D. (2009). A FAK-p120RasGAPp190RhoGAP complex regulates polarity in migrating cells. J. Cell Sci. 122, 1852-1862.
    • (2009) J. Cell Sci. , vol.122 , pp. 1852-1862
    • Tomar, A.1    Lim, S.T.2    Lim, Y.3    Schlaepfer, D.D.4
  • 46
    • 0031800794 scopus 로고    scopus 로고
    • Patterns and control of cell motility in the Xenopus gastrula
    • Wacker, S., Brodbeck, A., Lemaire, P., Niehrs, C. and Winklbauer, R. (1998). Patterns and control of cell motility in the Xenopus gastrula. Development 125, 1931-1942.
    • (1998) Development , vol.125 , pp. 1931-1942
    • Wacker, S.1    Brodbeck, A.2    Lemaire, P.3    Niehrs, C.4    Winklbauer, R.5
  • 47
    • 84859869529 scopus 로고    scopus 로고
    • Spindle position in symmetric cell divisions during epiboly is controlled by opposing and dynamic apicobasal forces
    • Woolner, S. and Papalopulu, N. (2012). Spindle position in symmetric cell divisions during epiboly is controlled by opposing and dynamic apicobasal forces. Dev. Cell 22, 775-787.
    • (2012) Dev. Cell , vol.22 , pp. 775-787
    • Woolner, S.1    Papalopulu, N.2
  • 48
    • 3543023861 scopus 로고    scopus 로고
    • Focal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a beta 1 integrin viability signaling pathway
    • Xia, H., Nho, R. S., Kahm, J., Kleidon, J. and Henke, C. A. (2004). Focal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a beta 1 integrin viability signaling pathway. J. Biol. Chem. 279, 33024-33034.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33024-33034
    • Xia, H.1    Nho, R.S.2    Kahm, J.3    Kleidon, J.4    Henke, C.A.5
  • 49
    • 0042329506 scopus 로고    scopus 로고
    • Serine 732 phosphorylation of FAK by Cdk5 is important for microtubule organization, nuclear movement, and neuronal migration
    • Xie, Z., Sanada, K., Samuels, B. A., Shih, H. and Tsai, L. H. (2003). Serine 732 phosphorylation of FAK by Cdk5 is important for microtubule organization, nuclear movement, and neuronal migration. Cell 114, 469-482.
    • (2003) Cell , vol.114 , pp. 469-482
    • Xie, Z.1    Sanada, K.2    Samuels, B.A.3    Shih, H.4    Tsai, L.H.5
  • 50
    • 0033601745 scopus 로고    scopus 로고
    • Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: Role of mitosis-specific serine phosphorylation of FAK
    • Yamakita, Y., Totsukawa, G., Yamashiro, S., Fry, D., Zhang, X., Hanks, S. K. and Matsumura, F. (1999). Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: role of mitosis-specific serine phosphorylation of FAK. J. Cell Biol. 144, 315-324.
    • (1999) J. Cell Biol. , vol.144 , pp. 315-324
    • Yamakita, Y.1    Totsukawa, G.2    Yamashiro, S.3    Fry, D.4    Zhang, X.5    Hanks, S.K.6    Matsumura, F.7
  • 51
    • 0027371908 scopus 로고
    • Embryonic mesodermal defects in alpha 5 integrin-deficient mice
    • Yang, J. T., Rayburn, H. and Hynes, R. O. (1993). Embryonic mesodermal defects in alpha 5 integrin-deficient mice. Development 119, 1093-1105.
    • (1993) Development , vol.119 , pp. 1093-1105
    • Yang, J.T.1    Rayburn, H.2    Hynes, R.O.3
  • 52
    • 0032576547 scopus 로고    scopus 로고
    • Regulation of the cell cycle by focal adhesion kinase
    • Zhao, J. H., Reiske, H. and Guan, J. L. (1998). Regulation of the cell cycle by focal adhesion kinase. J. Cell Biol. 143, 1997-2008.
    • (1998) J. Cell Biol. , vol.143 , pp. 1997-2008
    • Zhao, J.H.1    Reiske, H.2    Guan, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.