메뉴 건너뛰기




Volumn , Issue , 2007, Pages 155-179

Focal adhesion kinase in neuritogenesis

Author keywords

[No Author keywords available]

Indexed keywords


EID: 49149090502     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-0-387-68561-8_7     Document Type: Chapter
Times cited : (2)

References (134)
  • 1
    • 0033625536 scopus 로고    scopus 로고
    • Motor proteins regulate force interactions between microtubules and microfilaments in the axon
    • Ahmad, F. J., Hughey, J., Wittmann, T., Hyman, A., Greaser, M., and Baas, P. W., 2000, Motor proteins regulate force interactions between microtubules and microfilaments in the axon, Nat. Cell Biol. 2:276-280.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 276-280
    • Ahmad, F.J.1    Hughey, J.2    Wittmann, T.3    Hyman, A.4    Greaser, M.5    Baas, P.W.6
  • 2
    • 0034194714 scopus 로고    scopus 로고
    • Matrix survival signaling: From fibronectin via focal adhesion kinase to c-Jun. NH (2)-terminal kinase
    • Almeida, E. A., Ilic, D., Han, Q., Hauck, C. R., Jin, F., Kawakatsu, H., et al., 2000, Matrix survival signaling: From fibronectin via focal adhesion kinase to c-Jun. NH (2)-terminal kinase, J. Cell Biol. 149:741-754.
    • (2000) J. Cell Biol. , vol.149 , pp. 741-754
    • Almeida, E.A.1    Ilic, D.2    Han, Q.3    Hauck, C.R.4    Jin, F.5    Kawakatsu, H.6
  • 3
    • 0027260615 scopus 로고
    • Expression of an N-terminally truncated form of human focal adhesion kinase in brain
    • Andre, E., and Becker-Andre, M., 1993, Expression of an N-terminally truncated form of human focal adhesion kinase in brain, Biochem. Biophys. Res. Commun. 190:140-147.
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 140-147
    • Andre, E.1    Becker-Andre, M.2
  • 4
    • 0345593816 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts
    • Angers-Loustau, A., Cote, J. F., Charest, A., Dowbenko, D., Spencer, S., Lasky, L. A., et al., 1999, Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts, J. Cell Biol. 144:1019-1031.
    • (1999) J. Cell Biol. , vol.144 , pp. 1019-1031
    • Angers-Loustau, A.1    Cote, J.F.2    Charest, A.3    Dowbenko, D.4    Spencer, S.5    Lasky, L.A.6
  • 5
    • 0027970388 scopus 로고
    • Characterization of neural cell adhesion sites: Point contacts are the sites of interaction between integrins and the cytoskeleton in PC12 cells
    • Arregui, C. O., Carbonetto, S., and McKerracher, L., 1994, Characterization of neural cell adhesion sites: Point contacts are the sites of interaction between integrins and the cytoskeleton in PC12 cells, J. Neurosci. 14:6967-6977.
    • (1994) J. Neurosci. , vol.14 , pp. 6967-6977
    • Arregui, C.O.1    Carbonetto, S.2    McKerracher, L.3
  • 6
    • 0037509860 scopus 로고    scopus 로고
    • Stereotyped pruning of long hippocampal axon branches triggered by retraction inducers of the semaphorin family
    • Bagri, A., Cheng, H. J., Yaron, A., Pleasure, S. J., and Tessier-Lavigne, M., 2003, Stereotyped pruning of long hippocampal axon branches triggered by retraction inducers of the semaphorin family, Cell 11:285-299.
    • (2003) Cell , vol.11 , pp. 285-299
    • Bagri, A.1    Cheng, H.J.2    Yaron, A.3    Pleasure, S.J.4    Tessier-Lavigne, M.5
  • 7
    • 0027971705 scopus 로고
    • NCAM-dependent neurite outgrowth is inhibited in neurons from Fyn-minus mice
    • Beggs, H. E., Soriano, P., and Maness, P. F., 1994, NCAM-dependent neurite outgrowth is inhibited in neurons from Fyn-minus mice, J. Cell Biol. 127:825-833.
    • (1994) J. Cell Biol. , vol.127 , pp. 825-833
    • Beggs, H.E.1    Soriano, P.2    Maness, P.F.3
  • 8
    • 0030887348 scopus 로고    scopus 로고
    • NCAM140 interacts with the focal adhesion kinase p125 (fak) and the SRC-related tyrosine kinase p59 (fyn)
    • Beggs, H. E., Baragona, S. C., Hemperly, J. J., and Maness, P. F., 1997, NCAM140 interacts with the focal adhesion kinase p125 (fak) and the SRC-related tyrosine kinase p59 (fyn), J. Biol. Chem. 272:8310-8319.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8310-8319
    • Beggs, H.E.1    Baragona, S.C.2    Hemperly, J.J.3    Maness, P.F.4
  • 9
    • 0345550397 scopus 로고    scopus 로고
    • FAK deficiency in cells contributing to the basal lamina results in cortical abnormalities resembling congenital muscular dystrophies
    • Beggs, H. E., Schahin-Reed, D., Zang, K., Goebbels, S., Nave, K. A., Gorski, J., et al., 2003, FAK deficiency in cells contributing to the basal lamina results in cortical abnormalities resembling congenital muscular dystrophies, Neuron 40:501-514.
    • (2003) Neuron , vol.40 , pp. 501-514
    • Beggs, H.E.1    Schahin-Reed, D.2    Zang, K.3    Goebbels, S.4    Nave, K.A.5    Gorski, J.6
  • 10
    • 0342748583 scopus 로고    scopus 로고
    • Sequential steps in clathrin-mediated synaptic vesicle endocytosis
    • Brodin, L., Low, P., and Shupliakov, O., 2000, Sequential steps in clathrin-mediated synaptic vesicle endocytosis, Curr. Opin. Neurobiol. 10:312-320.
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 312-320
    • Brodin, L.1    Low, P.2    Shupliakov, O.3
  • 11
    • 0030009393 scopus 로고    scopus 로고
    • Cloning of focal adhesion kinase, pp125FAK, from rat brain reveals multiple transcripts with different patterns of expression
    • Burgaya, F., and Girault, J. A., 1996, Cloning of focal adhesion kinase, pp125FAK, from rat brain reveals multiple transcripts with different patterns of expression, Brain Res. Mol. Brain Res. 37:63-73.
    • (1996) Brain Res. Mol. Brain Res. , vol.37 , pp. 63-73
    • Burgaya, F.1    Girault, J.A.2
  • 13
    • 0030725406 scopus 로고    scopus 로고
    • Alternatively spliced focal adhesion kinase in rat brain with increased autophosphorylation activity
    • Burgaya, F., Toutant, M., Studler, J. M., Costa, A., Le Bert, M., Gelman, M., et al., 1997, Alternatively spliced focal adhesion kinase in rat brain with increased autophosphorylation activity, J. Biol. Chem. 272:28720-28725.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28720-28725
    • Burgaya, F.1    Toutant, M.2    Studler, J.M.3    Costa, A.4    Le Bert, M.5    Gelman, M.6
  • 14
    • 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
  • 15
    • 0034044795 scopus 로고    scopus 로고
    • Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: Correlation with preinvasive and invasive phenotypes
    • Cance, W. G., Harris, J. E., Iacocca, M. V., Roche, E., Yang, X., Chang, J., et al., 2000, Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: Correlation with preinvasive and invasive phenotypes, Clin. Cancer Res. 6:2417-2423.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 2417-2423
    • Cance, W.G.1    Harris, J.E.2    Iacocca, M.V.3    Roche, E.4    Yang, X.5    Chang, J.6
  • 16
    • 0041924982 scopus 로고    scopus 로고
    • A novel role for FAK as a protease-targeting adaptor protein: Regulation by p42 ERK and Src
    • Carragher, N. O., Westhoff, M. A., Fincham, V. J., Schaller, M. D., and Frame, M. C., 2003, A novel role for FAK as a protease-targeting adaptor protein: Regulation by p42 ERK and Src, Curr. Biol. 13:1442-1450.
    • (2003) Curr. Biol. , vol.13 , pp. 1442-1450
    • Carragher, N.O.1    Westhoff, M.A.2    Fincham, V.J.3    Schaller, M.D.4    Frame, M.C.5
  • 17
    • 0036045804 scopus 로고    scopus 로고
    • EphrinA1-induced cytoskeletal re-organization requires FAK and p130 (cas)
    • Carter, N., Nakamoto, T., Hirai, H., and Hunter, T., 2002, EphrinA1-induced cytoskeletal re-organization requires FAK and p130 (cas), Nat. Cell Biol. 4:565-573.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 565-573
    • Carter, N.1    Nakamoto, T.2    Hirai, H.3    Hunter, T.4
  • 18
    • 0029948080 scopus 로고    scopus 로고
    • Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn
    • Cary, L. A., Chang, J. F., and Guan, J. L., 1996, Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn, J. Cell. Sci. 109(Pt. 7):1787-1794.
    • (1996) J. Cell. Sci. , vol.109 , Issue.PART 7 , pp. 1787-1794
    • Cary, L.A.1    Chang, J.F.2    Guan, J.L.3
  • 19
    • 0032509565 scopus 로고    scopus 로고
    • Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration
    • Cary, L. A., Han, D. C., Polte, T. R., Hanks, S. K., and Guan, J. L., 1998, Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration, J. Cell Biol. 140:211-221.
    • (1998) J. Cell Biol. , vol.140 , pp. 211-221
    • Cary, L.A.1    Han, D.C.2    Polte, T.R.3    Hanks, S.K.4    Guan, J.L.5
  • 20
    • 0035003136 scopus 로고    scopus 로고
    • Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain
    • Chen, R., Kim, O., Li, M., Xiong, X., Guan, J. L., Kung, H. J., et al., 2001, Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain, Nat. Cell Biol. 3:439-444.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 439-444
    • Chen, R.1    Kim, O.2    Li, M.3    Xiong, X.4    Guan, J.L.5    Kung, H.J.6
  • 21
    • 0037072731 scopus 로고    scopus 로고
    • Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells
    • Chen, B. H., Tzen, J. T., Bresnick, A. R., and Chen, H. C., 2002, Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells, J. Biol. Chem. 277:33857-33863.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33857-33863
    • Chen, B.H.1    Tzen, J.T.2    Bresnick, A.R.3    Chen, H.C.4
  • 22
    • 0037128213 scopus 로고    scopus 로고
    • Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold
    • Cho, S. Y., and Klemke, R. L., 2002, Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold, J. Cell Biol. 156:725-736.
    • (2002) J. Cell Biol. , vol.156 , pp. 725-736
    • Cho, S.Y.1    Klemke, R.L.2
  • 23
    • 0028173980 scopus 로고
    • Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK
    • Cobb, B. S., Schaller, M. D., Leu, T. H., and Parsons, J. T., 1994, Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK, Mol. Cell. Biol. 14:147-155.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 147-155
    • Cobb, B.S.1    Schaller, M.D.2    Leu, T.H.3    Parsons, J.T.4
  • 25
    • 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
  • 26
    • 0028841220 scopus 로고
    • Tyrosine phosphorylation and cytoskeletal tension regulate the release of fibroblast adhesions
    • Crowley, E., and Horwitz, A. F., 1995, Tyrosine phosphorylation and cytoskeletal tension regulate the release of fibroblast adhesions, J. Cell Biol. 131:525-537.
    • (1995) J. Cell Biol. , vol.131 , pp. 525-537
    • Crowley, E.1    Horwitz, A.F.2
  • 28
    • 0031079657 scopus 로고    scopus 로고
    • Integrin-mediated tyrosine phosphorylation and redistribution of paxillin during neuronal adhesion
    • De Curtis, I., and Malanchini, B., 1997, Integrin-mediated tyrosine phosphorylation and redistribution of paxillin during neuronal adhesion, Exp. Cell Res. 230:233-243.
    • (1997) Exp. Cell Res. , vol.230 , pp. 233-243
    • De Curtis, I.1    Malanchini, B.2
  • 30
    • 0031814171 scopus 로고    scopus 로고
    • Differential regulation of FAK+ and PYK2/Cakbeta, two related tyrosine kinases, in rat hippocampal slices: Effects of LPA, carbachol, depolarization and hyperosmolarity
    • Derkinderen, P., Siciliano, J., Toutant, M., and Girault, J. A., 1998, Differential regulation of FAK+ and PYK2/Cakbeta, two related tyrosine kinases, in rat hippocampal slices: Effects of LPA, carbachol, depolarization and hyperosmolarity, Eur. J. Neurosci. 10:1667-1675.
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 1667-1675
    • Derkinderen, P.1    Siciliano, J.2    Toutant, M.3    Girault, J.A.4
  • 31
    • 0025004998 scopus 로고
    • A threshold effect of the major isoforms of NCAM on neurite outgrowth
    • Doherty, P., Fruns, M., Seaton, P., Dickson, G., Barton, C. H., Sears, T. A., et al., 1990, A threshold effect of the major isoforms of NCAM on neurite outgrowth, Nature 343:464-466.
    • (1990) Nature , vol.343 , pp. 464-466
    • Doherty, P.1    Fruns, M.2    Seaton, P.3    Dickson, G.4    Barton, C.H.5    Sears, T.A.6
  • 32
    • 0036544562 scopus 로고    scopus 로고
    • Src-mediated coupling of focal adhesion kinase to integrin alpha (v) beta5 in vascular endothelial growth factor signaling
    • Eliceiri, B. P., Puente, X. S., Hood, J. D., Stupack, D. G., Schlaepfer, D. D., Huang, X. Z., et al., 2002, Src-mediated coupling of focal adhesion kinase to integrin alpha (v) beta5 in vascular endothelial growth factor signaling, J. Cell Biol. 157:149-160.
    • (2002) J. Cell Biol. , vol.157 , pp. 149-160
    • Eliceiri, B.P.1    Puente, X.S.2    Hood, J.D.3    Stupack, D.G.4    Schlaepfer, D.D.5    Huang, X.Z.6
  • 33
    • 0033175564 scopus 로고    scopus 로고
    • Selective regulation of integrin-cytoskeleton interactions by the tyrosine kinase Src
    • Felsenfeld, D. P., Schwartzberg, P. L., Venegas, A., Tse, R., and Sheetz, M. P., 1999, Selective regulation of integrin-cytoskeleton interactions by the tyrosine kinase Src, Nat. Cell Biol. 1:200-206.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 200-206
    • Felsenfeld, D.P.1    Schwartzberg, P.L.2    Venegas, A.3    Tse, R.4    Sheetz, M.P.5
  • 34
    • 0032472411 scopus 로고    scopus 로고
    • The catalytic activity of Src is dispensable for translocation to focal adhesions but controls the turnover of these structures during cell motility
    • Fincham, V. J., and Frame, M. C., 1998, The catalytic activity of Src is dispensable for translocation to focal adhesions but controls the turnover of these structures during cell motility, EMBO J. 17:81-92.
    • (1998) EMBO J. , vol.17 , pp. 81-92
    • Fincham, V.J.1    Frame, M.C.2
  • 35
    • 0028783271 scopus 로고
    • Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase
    • Furuta, Y., Ilic, 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) FAK, Oncogene , vol.11 , pp. 1989-1995
    • Furuta, Y.1    Ilic, D.2    Kanazawa, S.3    Takeda, N.4    Yamamoto, T.5    Aizawa, S.6
  • 37
    • 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
  • 38
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F. G., and Ruoslahti, E., 1999, Integrin signaling, Science 285:1028-1032.
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 39
    • 0029741102 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation
    • Gilmore, A. P., and Romer, L. H., 1996, Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation, Mol. Biol. Cell 7:1209-1224.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1209-1224
    • Gilmore, A.P.1    Romer, L.H.2
  • 40
    • 0032586727 scopus 로고    scopus 로고
    • FAK and PYK2/CAKbeta in the nervous system: A link between neuronal activity, plasticity and survival?
    • Girault, J. A., Costa, A., Derkinderen, P., Studler, J. M., and Toutant, M., 1999a, FAK and PYK2/CAKbeta in the nervous system: A link between neuronal activity, plasticity and survival? Trends Neurosci. 22:257-263.
    • (1999) Trends Neurosci. , vol.22 , pp. 257-263
    • Girault, J.A.1    Costa, A.2    Derkinderen, P.3    Studler, J.M.4    Toutant, M.5
  • 42
    • 0026759309 scopus 로고
    • Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • Guan, J. L., and Shalloway, D., 1992, Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation, Nature 358:690-692.
    • (1992) Nature , vol.358 , pp. 690-692
    • Guan, J.L.1    Shalloway, D.2
  • 43
  • 44
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A., 1998, Rho GTPases and the actin cytoskeleton, Science 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 45
    • 0000226650 scopus 로고    scopus 로고
    • Association of focal adhesion kinase with Grb7 and its role in cell migration
    • Han, D. C., and Guan, J. L., 1999, Association of focal adhesion kinase with Grb7 and its role in cell migration, J. Biol. Chem. 274:24425-24430.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24425-24430
    • Han, D.C.1    Guan, J.L.2
  • 46
    • 0031081425 scopus 로고    scopus 로고
    • Signaling through focal adhesion kinase
    • Hanks, S. K., and Polte, T. R., 1997, Signaling through focal adhesion kinase, Bioessays 19:137-145.
    • (1997) Bioessays , vol.19 , pp. 137-145
    • Hanks, S.K.1    Polte, T.R.2
  • 47
    • 0026674919 scopus 로고
    • Focal adhesion proteintyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks, S. K., Calalb, M. B., Harper, M. C., and Patel, S. K., 1992, Focal adhesion proteintyrosine kinase phosphorylated in response to cell attachment to fibronectin, Proc. Natl. Acad. Sci. USA 89:8487-8491.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 48
    • 0035476836 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells
    • Hauck, C. R., Sieg, D. J., Hsia, D. A., Loftus, J. C., Gaarde, W. A., Monia, B. P., et al., 2001, Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells, Cancer Res. 61:7079-7090.
    • (2001) Cancer Res. , vol.61 , pp. 7079-7090
    • Hauck, C.R.1    Sieg, D.J.2    Hsia, D.A.3    Loftus, J.C.4    Gaarde, W.A.5    Monia, B.P.6
  • 49
    • 0037066778 scopus 로고    scopus 로고
    • V-Src SH3-enhanced interaction with focal adhesion kinase at beta 1 integrin-containing invadopodia promotes cell invasion
    • Hauck, C. R., Hsia, D. A., Ilic, D., and Schlaepfer, D. D., 2002, v-Src SH3-enhanced interaction with focal adhesion kinase at beta 1 integrin-containing invadopodia promotes cell invasion, J. Biol. Chem. 277:12487-12490.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12487-12490
    • Hauck, C.R.1    Hsia, D.A.2    Ilic, D.3    Schlaepfer, D.D.4
  • 50
    • 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
  • 51
    • 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
  • 52
    • 0033603256 scopus 로고    scopus 로고
    • A ligand-gated association between cytoplasmic domains of UNC5 and DCC family receptors converts netrin-induced growth cone attraction to repulsion
    • Hong, K., Hinck, L., Nishiyama, M., Poo, M. M., Tessier-Lavigne, M., and Stein, E., 1999, A ligand-gated association between cytoplasmic domains of UNC5 and DCC family receptors converts netrin-induced growth cone attraction to repulsion, Cell 97:927-941.
    • (1999) Cell , vol.97 , pp. 927-941
    • Hong, K.1    Hinck, L.2    Nishiyama, M.3    Poo, M.M.4    Tessier-Lavigne, M.5    Stein, E.6
  • 53
    • 0033517355 scopus 로고    scopus 로고
    • Growth-cone attraction to netrin-1 is converted to repulsion by laminin-1
    • Hopker, V. H., Shewan, D., Tessier-Lavigne, M., Poo, M., and Holt, C., 1999, Growth-cone attraction to netrin-1 is converted to repulsion by laminin-1, Nature 401:69-73.
    • (1999) Nature , vol.401 , pp. 69-73
    • Hopker, V.H.1    Shewan, D.2    Tessier-Lavigne, M.3    Poo, M.4    Holt, C.5
  • 55
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O., 1992, Integrins: Versatility, modulation, and signaling in cell adhesion, Cell 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 56
    • 0033430117 scopus 로고    scopus 로고
    • Cell adhesion: Old and new questions
    • Hynes, R. O., 1999, Cell adhesion: Old and new questions, Trends Cell Biol. 9:M33-7.
    • (1999) Trends Cell Biol. , vol.9
    • Hynes, R.O.1
  • 57
    • 0028347820 scopus 로고
    • Impaired neurite outgrowth of src-minus cerebellar neurons on the cell adhesion molecule L1
    • Ignelzi, M. A., Jr., Miller, D. R., Soriano, P., and Maness, P. F., 1994, Impaired neurite outgrowth of src-minus cerebellar neurons on the cell adhesion molecule L1, Neuron 12:873-884.
    • (1994) Neuron , vol.12 , pp. 873-884
    • Ignelzi Jr., M.A.1    Miller, D.R.2    Soriano, P.3    Maness, P.F.4
  • 58
    • 0029120440 scopus 로고
    • Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
    • Ilic, D., Furuta, Y., Kanazawa, S., Takeda, N., Sobue, K., Nakatsuji, N., et al., 1995, Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice, Nature 377:539-544.
    • (1995) Nature , vol.377 , pp. 539-544
    • Ilic, D.1    Furuta, Y.2    Kanazawa, S.3    Takeda, N.4    Sobue, K.5    Nakatsuji, N.6
  • 59
    • 0034282247 scopus 로고    scopus 로고
    • Pyk2 and FAK regulate neurite outgrowth induced by growth factors and integrins
    • Ivankovic-Dikic, I., Gronroos, E., Blaukat, A., Barth, B. U., and Dikic, I., 2000, Pyk2 and FAK regulate neurite outgrowth induced by growth factors and integrins, Nat. Cell Biol. 2:574-581.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 574-581
    • Ivankovic-Dikic, I.1    Gronroos, E.2    Blaukat, A.3    Barth, B.U.4    Dikic, I.5
  • 60
    • 0028021308 scopus 로고
    • Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho
    • Jalink, K., Van Corven, E. J., Hengeveld, T., Morii, N., Narumiya, S., and Moolenaar, W. H., 1994, Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho, J. Cell Biol. 126:801-810.
    • (1994) J. Cell Biol. , vol.126 , pp. 801-810
    • Jalink, K.1    Van Corven, E.J.2    Hengeveld, T.3    Morii, N.4    Narumiya, S.5    Moolenaar, W.H.6
  • 61
    • 0346220294 scopus 로고    scopus 로고
    • PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation
    • Kadare, G., Toutant, M., Formstecher, E., Corvol, J. C., Carnaud, M., Boutterin, M. C., et al., 2003, PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation, J. Biol. Chem. 278:47434-47440.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47434-47440
    • Kadare, G.1    Toutant, M.2    Formstecher, E.3    Corvol, J.C.4    Carnaud, M.5    Boutterin, M.C.6
  • 62
    • 0031846706 scopus 로고    scopus 로고
    • Differential regulation of focal adhesion kinase and mitogen-activated protein kinase tyrosine phosphorylation during insulin-like growth factor-I-mediated cytoskeletal reorganization
    • Kim, B., and Feldman, E. L., 1998, Differential regulation of focal adhesion kinase and mitogen-activated protein kinase tyrosine phosphorylation during insulin-like growth factor-I-mediated cytoskeletal reorganization, J. Neurochem. 71:1333-1336.
    • (1998) J. Neurochem. , vol.71 , pp. 1333-1336
    • Kim, B.1    Feldman, E.L.2
  • 63
    • 0032559562 scopus 로고    scopus 로고
    • CAS/Crk coupling serves as a "molecular switch" for induction of cell migration
    • Klemke, R. L., Leng, J., Molander, R., Brooks, P. C., Vuori, K., and Cheresh, D. A., 1998, CAS/Crk coupling serves as a "molecular switch" for induction of cell migration, J. Cell Biol. 140:961-972.
    • (1998) J. Cell Biol. , vol.140 , pp. 961-972
    • Klemke, R.L.1    Leng, J.2    Molander, R.3    Brooks, P.C.4    Vuori, K.5    Cheresh, D.A.6
  • 64
    • 0028872784 scopus 로고
    • Laminin and fibronectin guideposts signal sustained but opposite effects to passing growth cones
    • Kuhn, T. B., Schmidt, M. F., and Kater, S. B., 1995, Laminin and fibronectin guideposts signal sustained but opposite effects to passing growth cones, Neuron 14:275-285.
    • (1995) Neuron , vol.14 , pp. 275-285
    • Kuhn, T.B.1    Schmidt, M.F.2    Kater, S.B.3
  • 65
    • 0029154733 scopus 로고
    • Protein tyrosine kinase PYK2 involved in Ca (2+)-induced regulation of ion channel and MAP kinase functions
    • Lev, S., Moreno, H., Martinez, R., Canoll, P., Peles, E., Musacchio, J. M., et al., 1995, Protein tyrosine kinase PYK2 involved in Ca (2+)-induced regulation of ion channel and MAP kinase functions, Nature 376:737-745.
    • (1995) Nature , vol.376 , pp. 737-745
    • Lev, S.1    Moreno, H.2    Martinez, R.3    Canoll, P.4    Peles, E.5    Musacchio, J.M.6
  • 66
    • 7044260519 scopus 로고    scopus 로고
    • Activation of FAK and Src are receptor-proximal events required for netrin signaling
    • Li, W., Lee, J., Vikis, H. G., Lee, S. H., Liu, G., Aurandt, J., et al., 2004, Activation of FAK and Src are receptor-proximal events required for netrin signaling, Nat. Neurosci. 7:1213-1221.
    • (2004) Nat. Neurosci. , vol.7 , pp. 1213-1221
    • Li, W.1    Lee, J.2    Vikis, H.G.3    Lee, S.H.4    Liu, G.5    Aurandt, J.6
  • 67
    • 0028953495 scopus 로고
    • Growth cone advance is inversely proportional to retrograde F-actin flow
    • Lin, C. H., and Forscher, P., 1995, Growth cone advance is inversely proportional to retrograde F-actin flow, Neuron 14:763-771.
    • (1995) Neuron , vol.14 , pp. 763-771
    • Lin, C.H.1    Forscher, P.2
  • 68
    • 0028104673 scopus 로고
    • Cytoskeletal reorganization underlying growth cone motility
    • Lin, C. H., Thompson, C. A., and Forscher, P., 1994, Cytoskeletal reorganization underlying growth cone motility, Curr. Opin. Neurobiol. 4:640-647.
    • (1994) Curr. Opin. Neurobiol. , vol.4 , pp. 640-647
    • Lin, C.H.1    Thompson, C.A.2    Forscher, P.3
  • 69
    • 7044254701 scopus 로고    scopus 로고
    • Netrin requires focal adhesion kinase and Src family kinases for axon outgrowth and attraction
    • Liu, G., Beggs, H., Jurgensen, C., Park, H. T., Tang, H., Gorski, J., et al., 2004, Netrin requires focal adhesion kinase and Src family kinases for axon outgrowth and attraction, Nat. Neurosci. 7:1222-1232.
    • (2004) Nat. Neurosci. , vol.7 , pp. 1222-1232
    • Liu, G.1    Beggs, H.2    Jurgensen, C.3    Park, H.T.4    Tang, H.5    Gorski, J.6
  • 71
    • 0028870428 scopus 로고
    • K-252a induces tyrosine phosphorylation of the focal adhesion kinase and neurite outgrowth in human neuroblastoma SH-SY5Y cells
    • Maroney, A. C., Lipfert, L., Forbes, M. E., Glicksman, M. A., Neff, N. T., Siman, R., et al., 1995, K-252a induces tyrosine phosphorylation of the focal adhesion kinase and neurite outgrowth in human neuroblastoma SH-SY5Y cells, J. Neurochem. 64:540-549.
    • (1995) J. Neurochem. , vol.64 , pp. 540-549
    • Maroney, A.C.1    Lipfert, L.2    Forbes, M.E.3    Glicksman, M.A.4    Neff, N.T.5    Siman, R.6
  • 73
    • 0033168047 scopus 로고    scopus 로고
    • Eph receptors and ephrins restrict cell intermingling and communication
    • Mellitzer, G., Xu, Q., and Wilkinson, D. G., 1999, Eph receptors and ephrins restrict cell intermingling and communication, Nature 400:77-81.
    • (1999) Nature , vol.400 , pp. 77-81
    • Mellitzer, G.1    Xu, Q.2    Wilkinson, D.G.3
  • 74
    • 0032590021 scopus 로고    scopus 로고
    • FA K + and PYK2/CAKbeta, two related tyrosine kinases highly expressed in the central nervous system: Similarities and differences in the expression pattern
    • Menegon, A., Burgaya, F., Baudot, P., Dunlap, D. D., Girault, J. A., and Valtorta, F., 1999, FA K + and PYK2/CAKbeta, two related tyrosine kinases highly expressed in the central nervous system: Similarities and differences in the expression pattern, Eur. J. Neurosci. 11:3777-3788.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 3777-3788
    • Menegon, A.1    Burgaya, F.2    Baudot, P.3    Dunlap, D.D.4    Girault, J.A.5    Valtorta, F.6
  • 75
    • 0033785409 scopus 로고    scopus 로고
    • Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation
    • Miao, H., Burnett, E., Kinch, M., Simon, E., and Wang, B., 2000, Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation, Nat. Cell Biol. 2:62-69.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 62-69
    • Miao, H.1    Burnett, E.2    Kinch, M.3    Simon, E.4    Wang, B.5
  • 76
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison, T. J., and Cramer, L. P., 1996, Actin-based cell motility and cell locomotion, Cell 84:371-379.
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 77
    • 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
  • 79
    • 0032942775 scopus 로고    scopus 로고
    • Growth cone guidance: First steps towards a deeper understanding
    • Mueller, B. K., 1999, Growth cone guidance: First steps towards a deeper understanding, Annu. Rev. Neurosci. 22:351-388.
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 351-388
    • Mueller, B.K.1
  • 80
    • 0037314984 scopus 로고    scopus 로고
    • Control of hippocampal dendritic spine morphology through ephrin-A3/EphA4 signaling
    • Murai, K. K., Nguyen, L. N., Irie, F., Yamaguchi, Y., and Pasquale, E. B., 2003, Control of hippocampal dendritic spine morphology through ephrin-A3/EphA4 signaling, Nat. Neurosci. 6:153-160.
    • (2003) Nat. Neurosci. , vol.6 , pp. 153-160
    • Murai, K.K.1    Nguyen, L.N.2    Irie, F.3    Yamaguchi, Y.4    Pasquale, E.B.5
  • 81
    • 0025858874 scopus 로고
    • Cell/substratum adhesions in RSV-transformed rat fibroblasts
    • Nermut, M. V., Eason, P., Hirst, E. M., and Kellie, S., 1991, Cell/substratum adhesions in RSV-transformed rat fibroblasts, Exp. Cell Res. 193:382-397.
    • (1991) Exp. Cell Res. , vol.193 , pp. 382-397
    • Nermut, M.V.1    Eason, P.2    Hirst, E.M.3    Kellie, S.4
  • 82
    • 0347285297 scopus 로고    scopus 로고
    • The molecular mystery of neuronal migration: FAK and Cdk5
    • Nikolic, M., 2004, The molecular mystery of neuronal migration: FAK and Cdk5, Trends Cell Biol. 14:1-5.
    • (2004) Trends Cell Biol. , vol.14 , pp. 1-5
    • Nikolic, M.1
  • 83
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes, C. D., and Hall, A., 1999, Rho GTPases control polarity, protrusion, and adhesion during cell movement, J. Cell Biol. 144:1235-1244.
    • (1999) J. Cell Biol. , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 84
    • 0034907213 scopus 로고    scopus 로고
    • MDia mediates Rhoregulated formation and orientation of stable microtubules
    • Palazzo, A. F., Cook, T. A., Alberts, A. S., and Gundersen, G. G., 2001, mDia mediates Rhoregulated formation and orientation of stable microtubules, Nat. Cell Biol. 3:723-729.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 723-729
    • Palazzo, A.F.1    Cook, T.A.2    Alberts, A.S.3    Gundersen, G.G.4
  • 85
    • 0842331443 scopus 로고    scopus 로고
    • Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling
    • Palazzo, A. F., Eng, C. H., Schlaepfer, D. D., Marcantonio, E. E., and Gundersen, G. G., 2004, Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling, Science 303:836-839.
    • (2004) Science , vol.303 , pp. 836-839
    • Palazzo, A.F.1    Eng, C.H.2    Schlaepfer, D.D.3    Marcantonio, E.E.4    Gundersen, G.G.5
  • 86
    • 0034733540 scopus 로고    scopus 로고
    • Characterization of the tyrosine kinases RAFTK/Pyk2 and FAK in nerve growth factor-induced neuronal differentiation
    • Park, S. Y., Avraham, H., and Avraham, S., 2000, Characterization of the tyrosine kinases RAFTK/Pyk2 and FAK in nerve growth factor-induced neuronal differentiation, J. Biol. Chem. 275:19768-19777.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19768-19777
    • Park, S.Y.1    Avraham, H.2    Avraham, S.3
  • 87
    • 0037320703 scopus 로고    scopus 로고
    • Semaphorin junction: Making tracks toward neural connectivity
    • Pasterkamp, R. J., and Kolodkin, A. L., 2003, Semaphorin junction: Making tracks toward neural connectivity, Curr. Opin. Neurobiol. 13:79-89.
    • (2003) Curr. Opin. Neurobiol. , vol.13 , pp. 79-89
    • Pasterkamp, R.J.1    Kolodkin, A.L.2
  • 88
    • 0043033220 scopus 로고    scopus 로고
    • Semaphorin 7A promotes axon outgrowth through integrins and MAPKs
    • Pasterkamp, R. J., Peschon, J. J., Spriggs, M. K., and Kolodkin, A. L., 2003, Semaphorin 7A promotes axon outgrowth through integrins and MAPKs, Nature 424:398-405.
    • (2003) Nature , vol.424 , pp. 398-405
    • Pasterkamp, R.J.1    Peschon, J.J.2    Spriggs, M.K.3    Kolodkin, A.L.4
  • 89
    • 0035813119 scopus 로고    scopus 로고
    • Ezrin interacts with focal adhesion kinase and induces its activation independently of cell-matrix adhesion
    • Poullet, P., Gautreau, A., Kadare, G., Girault, J. A., Louvard, D., and Arpin, M., 2001, Ezrin interacts with focal adhesion kinase and induces its activation independently of cell-matrix adhesion, J. Biol. Chem. 276:37686-37691.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37686-37691
    • Poullet, P.1    Gautreau, A.2    Kadare, G.3    Girault, J.A.4    Louvard, D.5    Arpin, M.6
  • 90
    • 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
  • 93
    • 0033229747 scopus 로고    scopus 로고
    • Focal adhesion kinase mediates the integrin signaling requirement for growth factor activation of MAP kinase
    • Renshaw, M. W., Price, L. S., and Schwartz, M. A., 1999, Focal adhesion kinase mediates the integrin signaling requirement for growth factor activation of MAP kinase, J. Cell Biol. 147:611-618.
    • (1999) J. Cell Biol. , vol.147 , pp. 611-618
    • Renshaw, M.W.1    Price, L.S.2    Schwartz, M.A.3
  • 94
    • 0029971297 scopus 로고    scopus 로고
    • A mechanism for regulation of the adhesionassociated proteintyrosine kinase pp125FAK
    • Richardson, A., and Parsons, T., 1996, A mechanism for regulation of the adhesionassociated proteintyrosine kinase pp125FAK, Nature 380:538-540.
    • (1996) Nature , vol.380 , pp. 538-540
    • Richardson, A.1    Parsons, T.2
  • 96
    • 0032563218 scopus 로고    scopus 로고
    • Bombesin, vasopressin, lysophosphatidic acid, and sphingosylphosphorylcholine induce focal adhesion kinase activation in intact Swiss 3T3 cells
    • Rodriguez-Fernandez, J. L., and Rozengurt, E., 1998, Bombesin, vasopressin, lysophosphatidic acid, and sphingosylphosphorylcholine induce focal adhesion kinase activation in intact Swiss 3T3 cells, J. Biol. Chem. 273:19321-19328.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19321-19328
    • Rodriguez-Fernandez, J.L.1    Rozengurt, E.2
  • 98
    • 0027439594 scopus 로고
    • Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK
    • Schaller, M. D., Borgman, C. A., and Parsons, J. T., 1993, Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK, Mol. Cell. Biol. 13:785-791.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 785-791
    • Schaller, M.D.1    Borgman, C.A.2    Parsons, J.T.3
  • 99
    • 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
  • 100
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer, D. D., Hanks, S. K., Hunter, T., and Van Der Geer, P., 1994, Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase, Nature 372:786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 101
    • 0032911020 scopus 로고    scopus 로고
    • Bidirectional signaling between the cytoskeleton and integrins
    • Schoenwaelder, S. M., and Burridge, K., 1999, Bidirectional signaling between the cytoskeleton and integrins, Curr. Opin. Cell Biol. 11:274-286.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 274-286
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 102
    • 0031148599 scopus 로고    scopus 로고
    • Cell migration: May the force be with you
    • Schwarzbauer, J. E., 1997, Cell migration: May the force be with you, Curr. Biol. 7:R292-R294.
    • (1997) Curr. Biol. , vol.7
    • Schwarzbauer, J.E.1
  • 103
    • 0037047324 scopus 로고    scopus 로고
    • Association of Grb7 with phosphoinositides and its role in the regulation of cell migration
    • Shen, T. L., Han, D. C., and Guan, J. L., 2002, Association of Grb7 with phosphoinositides and its role in the regulation of cell migration, J. Biol. Chem. 277:29069-29077.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29069-29077
    • Shen, T.L.1    Han, D.C.2    Guan, J.L.3
  • 104
    • 0032803067 scopus 로고    scopus 로고
    • Focal adhesion targeting: The critical determinant of FAK regulation and substrate phosphorylation
    • Shen, Y., and Schaller, M. D., 1999, Focal adhesion targeting: The critical determinant of FAK regulation and substrate phosphorylation, Mol. Biol. Cell 10:2507-2518.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2507-2518
    • Shen, Y.1    Schaller, M.D.2
  • 105
    • 0029840588 scopus 로고    scopus 로고
    • Differential regulation of proline-rich tyrosine kinase 2/cell adhesion kinase beta (PYK2/CAKbeta) and pp125 (FAK) by glutamate and depolarization in rat hippocampus
    • Siciliano, J. C., Toutant, M., Derkinderen, P., Sasaki, T., and Girault, J. A., 1996, Differential regulation of proline-rich tyrosine kinase 2/cell adhesion kinase beta (PYK2/CAKbeta) and pp125 (FAK) by glutamate and depolarization in rat hippocampus, J. Biol. Chem. 271:28942-28946.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28942-28946
    • Siciliano, J.C.1    Toutant, M.2    Derkinderen, P.3    Sasaki, T.4    Girault, J.A.5
  • 106
    • 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
  • 109
    • 0031967521 scopus 로고    scopus 로고
    • An emerging link between cytoskeletal dynamics and cell adhesion molecules in growth cone guidance
    • Suter, D. M., and Forscher, P., 1998, An emerging link between cytoskeletal dynamics and cell adhesion molecules in growth cone guidance, Curr. Opin. Neurobiol. 8:106-116.
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 106-116
    • Suter, D.M.1    Forscher, P.2
  • 110
    • 0035851919 scopus 로고    scopus 로고
    • Transmission of growth cone traction force through apCAM-cytoskeletal linkages is regulated by Src family tyrosine kinase activity
    • Suter, D. M., and Forscher, P., 2001, Transmission of growth cone traction force through apCAM-cytoskeletal linkages is regulated by Src family tyrosine kinase activity, J. Cell Biol. 155:427-438.
    • (2001) J. Cell Biol. , vol.155 , pp. 427-438
    • Suter, D.M.1    Forscher, P.2
  • 111
    • 0032489869 scopus 로고    scopus 로고
    • The Ig superfamily cell adhesion molecule, apCAM, mediates growth cone steering by substrate-cytoskeletal coupling
    • Suter, D. M., Errante, L. D., Belotserkovsky, V., and Forscher, P., 1998, The Ig superfamily cell adhesion molecule, apCAM, mediates growth cone steering by substrate-cytoskeletal coupling, J. Cell Biol. 141:227-240.
    • (1998) J. Cell Biol. , vol.141 , pp. 227-240
    • Suter, D.M.1    Errante, L.D.2    Belotserkovsky, V.3    Forscher, P.4
  • 112
    • 0032486198 scopus 로고    scopus 로고
    • Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN
    • Tamura, M., Gu, J., Matsumoto, K., Aota, S., Parsons, R., and Yamada, K. M., 1998, Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN, Science 280:1614-1617.
    • (1998) Science , vol.280 , pp. 1614-1617
    • Tamura, M.1    Gu, J.2    Matsumoto, K.3    Aota, S.4    Parsons, R.5    Yamada, K.M.6
  • 113
    • 0028863477 scopus 로고
    • Making the connection: Cytoskeletal rearrangements during growth cone guidance
    • Tanaka, E., and Sabry, J., 1995, Making the connection: Cytoskeletal rearrangements during growth cone guidance, Cell 83:171-176.
    • (1995) Cell , vol.83 , pp. 171-176
    • Tanaka, E.1    Sabry, J.2
  • 114
    • 0027444230 scopus 로고
    • Integrins in point contacts mediate cell spreading: Factors that regulate integrin accumulation in point contacts vs. focal contacts
    • Tawil, N., Wilson, P., and Carbonetto, S., 1993, Integrins in point contacts mediate cell spreading: Factors that regulate integrin accumulation in point contacts vs. focal contacts, J. Cell Biol. 120:261-271.
    • (1993) J. Cell Biol. , vol.120 , pp. 261-271
    • Tawil, N.1    Wilson, P.2    Carbonetto, S.3
  • 115
    • 0029959555 scopus 로고    scopus 로고
    • The molecular biology of axon guidance
    • Tessier-Lavigne, M., and Goodman, C. S., 1996, The molecular biology of axon guidance, Science 274:1123-1133.
    • (1996) Science , vol.274 , pp. 1123-1133
    • Tessier-Lavigne, M.1    Goodman, C.S.2
  • 116
    • 0034658330 scopus 로고    scopus 로고
    • Autophosphorylation of Tyr397 and its phosphorylation by Src-family kinases are altered in focal-adhesion-kinase neuronal isoforms
    • Toutant, M., Studler, J. M., Burgaya, F., Costa, A., Ezan, P., Gelman, M., et al., 2000, Autophosphorylation of Tyr397 and its phosphorylation by Src-family kinases are altered in focal-adhesion-kinase neuronal isoforms, Biochem. J. 348:119-128.
    • (2000) Biochem. J. , vol.348 , pp. 119-128
    • Toutant, M.1    Studler, J.M.2    Burgaya, F.3    Costa, A.4    Ezan, P.5    Gelman, M.6
  • 118
    • 0142188658 scopus 로고    scopus 로고
    • MMP-9 deficiency affects axonal outgrowth, migration, and apoptosis in the developing cerebellum
    • Vaillant, C., Meissirel, C., Mutin, M., Belin, M. F., Lund, L. R., and Thomasset, N., 2003, MMP-9 deficiency affects axonal outgrowth, migration, and apoptosis in the developing cerebellum, Mol. Cell. Neurosci. 24:395-408.
    • (2003) Mol. Cell. Neurosci. , vol.24 , pp. 395-408
    • Vaillant, C.1    Meissirel, C.2    Mutin, M.3    Belin, M.F.4    Lund, L.R.5    Thomasset, N.6
  • 120
    • 0027987934 scopus 로고
    • Vinculin-deficient PC12 cell lines extend unstable lamellipodia and filopodia and have a reduced rate of neurite outgrowth
    • Varnum-Finney, B., and Reichardt, L. F., 1994, Vinculin-deficient PC12 cell lines extend unstable lamellipodia and filopodia and have a reduced rate of neurite outgrowth, J. Cell Biol. 127:1071-1084.
    • (1994) J. Cell Biol. , vol.127 , pp. 1071-1084
    • Varnum-Finney, B.1    Reichardt, L.F.2
  • 121
    • 0033582915 scopus 로고    scopus 로고
    • Biochemical purification of a mammalian slit protein as a positive regulator of sensory axon elongation and branching
    • Wang, K. H., Brose, K., Arnott, D., Kidd, T., Goodman, C. S., Henzel, W., et al., 1999, Biochemical purification of a mammalian slit protein as a positive regulator of sensory axon elongation and branching, Cell 96:771-784.
    • (1999) Cell , vol.96 , pp. 771-784
    • Wang, K.H.1    Brose, K.2    Arnott, D.3    Kidd, T.4    Goodman, C.S.5    Henzel, W.6
  • 123
    • 0037107138 scopus 로고    scopus 로고
    • Metalloproteases and guidance of retinal axons in the developing visual system
    • Webber, C. A., Hocking, J. C., Yong, V. W., Stange, C. L., and McFarlane, S., 2002, Metalloproteases and guidance of retinal axons in the developing visual system, J. Neurosci. 22:8091-8100.
    • (2002) J. Neurosci. , vol.22 , pp. 8091-8100
    • Webber, C.A.1    Hocking, J.C.2    Yong, V.W.3    Stange, C.L.4    McFarlane, S.5
  • 124
    • 0027362796 scopus 로고
    • Regulated tyrosine phosphorylation at the tips of growth cone filopodia
    • Wu, D. Y., and Goldberg, D. J., 1993, Regulated tyrosine phosphorylation at the tips of growth cone filopodia, J. Cell Biol. 123:653-664.
    • (1993) J. Cell Biol. , vol.123 , pp. 653-664
    • Wu, D.Y.1    Goldberg, D.J.2
  • 125
    • 1542304700 scopus 로고    scopus 로고
    • Focal adhesion kinase regulation of N-WASP subcellular localization and function
    • Wu, X., Suetsugu, S., Cooper, L. A., Takenawa, T., and Guan, J. L., 2004, Focal adhesion kinase regulation of N-WASP subcellular localization and function, J. Biol. Chem. 279:9565-9576.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9565-9576
    • Wu, X.1    Suetsugu, S.2    Cooper, L.A.3    Takenawa, T.4    Guan, J.L.5
  • 126
    • 22944438407 scopus 로고    scopus 로고
    • FAK-Mediated src phosphorylation of endophilin A2 inhibits endocytosis of MT1-MMP and promotes ECM degradation
    • Wu, X., Gan, B., Yoo, Y., and Guan, J. L., 2005, FAK-Mediated src phosphorylation of endophilin A2 inhibits endocytosis of MT1-MMP and promotes ECM degradation, Dev. Cell. 9:185-196.
    • (2005) Dev. Cell. , vol.9 , pp. 185-196
    • Wu, X.1    Gan, B.2    Yoo, Y.3    Guan, J.L.4
  • 127
    • 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
  • 128
    • 0031846188 scopus 로고    scopus 로고
    • Expression and characterization of splice variants of PYK2, a focal adhesion kinase-related protein
    • Xiong, W. C., Macklem, M., and Parsons, J. T., 1998, Expression and characterization of splice variants of PYK2, a focal adhesion kinase-related protein, J. Cell. Sci. 111:1981-1991.
    • (1998) J. Cell. Sci. , vol.111 , pp. 1981-1991
    • Xiong, W.C.1    Macklem, M.2    Parsons, J.T.3
  • 129
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • Yamada, K. M., and Geiger, B., 1997, Molecular interactions in cell adhesion complexes, Curr. Opin. Cell Biol. 9:76-85.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 76-85
    • Yamada, K.M.1    Geiger, B.2
  • 130
    • 23744452775 scopus 로고    scopus 로고
    • A disintegrin and metalloprotease 21 (ADAM21) is associated with neurogenesis and axonal growth in developing and adult rodent CNS
    • Yang, P., Baker, K. A., and Hagg, T., 2005, A disintegrin and metalloprotease 21 (ADAM21) is associated with neurogenesis and axonal growth in developing and adult rodent CNS, J. Comp. Neurol. 490:163-179.
    • (2005) J. Comp. Neurol. , vol.490 , pp. 163-179
    • Yang, P.1    Baker, K.A.2    Hagg, T.3
  • 131
    • 3543036342 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion
    • Yu, D. H., Qu, C. K., Henegariu, O., Lu, X., and Feng, G. S., 1998, Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion, J. Biol. Chem. 273:21125-21131.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21125-21131
    • Yu, D.H.1    Qu, C.K.2    Henegariu, O.3    Lu, X.4    Feng, G.S.5
  • 132
    • 0026476697 scopus 로고
    • Focal adhesion kinase (p125FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes
    • Zachary, I., and Rozengurt, E., 1992, Focal adhesion kinase (p125FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes, Cell 71:891-894.
    • (1992) Cell , vol.71 , pp. 891-894
    • Zachary, I.1    Rozengurt, E.2
  • 133
    • 0037421205 scopus 로고    scopus 로고
    • PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration
    • Zeng, L., Si, X., Yu, W. P., Le, H. T., Ng, K. P., Teng, R. M., et al., 2003, PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration, J. Cell Biol. 160:137-146.
    • (2003) J. Cell Biol. , vol.160 , pp. 137-146
    • Zeng, L.1    Si, X.2    Yu, W.P.3    Le, H.T.4    Ng, K.P.5    Teng, R.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.