메뉴 건너뛰기




Volumn 19, Issue 7, 1999, Pages 4806-4818

Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; FOCAL ADHESION KINASE; FOCAL ADHESION KINASE 2; TETRACYCLINE; UNCLASSIFIED DRUG;

EID: 0033002997     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.7.4806     Document Type: Article
Times cited : (346)

References (83)
  • 4
    • 0027227263 scopus 로고
    • Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin
    • Bockholt, S. M., and K. Burridge. 1993. Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin. J. Biol. Chem. 268:14565-14567.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14565-14567
    • Bockholt, S.M.1    Burridge, K.2
  • 5
    • 0026445719 scopus 로고
    • FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell Biol. 119:893-903.
    • (1992) J. Cell Biol. , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 7
    • 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., T. R. Polte, and S. K. Hanks. 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
  • 8
    • 0030597218 scopus 로고    scopus 로고
    • Focal adhesion kinase tyrosine-861 is a major site of phosphorylation by Src
    • Calalb, M. B., X. Zhang, T. R. Polte, and S. K. Hanks. 1996. Focal adhesion kinase tyrosine-861 is a major site of phosphorylation by Src. Biochem. Biophys. Res. Commun. 228:662-668.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 662-668
    • Calalb, M.B.1    Zhang, X.2    Polte, T.R.3    Hanks, S.K.4
  • 9
    • 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., J. F. Chang, and J.-L. Guan. 1996. Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn. J. Cell Sci. 109:1787-1794.
    • (1996) J. Cell Sci. , vol.109 , pp. 1787-1794
    • Cary, L.A.1    Chang, J.F.2    Guan, J.-L.3
  • 11
    • 0029979722 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase
    • Chen, H.-C., P. A. Appeddu, H. Isoda, and J.-L. Guan. 1996. Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase. J. Biol. Chem. 271:26329-26334.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26329-26334
    • Chen, H.-C.1    Appeddu, P.A.2    Isoda, H.3    Guan, J.-L.4
  • 12
    • 0028089832 scopus 로고
    • Epidermal growth factor receptor-mediated cell motility: Phospholipase C activity is required, but mitogen-activated protein kinase activity is not sufficient for induced cell movement
    • Chen, P., H. Xie, M. C. Sekar, K. Gupta, and A. Wells. 1994. Epidermal growth factor receptor-mediated cell motility: phospholipase C activity is required, but mitogen-activated protein kinase activity is not sufficient for induced cell movement. J. Cell Biol. 127:847-857.
    • (1994) J. Cell Biol. , vol.127 , pp. 847-857
    • Chen, P.1    Xie, H.2    Sekar, M.C.3    Gupta, K.4    Wells, A.5
  • 13
    • 0032572557 scopus 로고    scopus 로고
    • Integrin-mediated signals regulated by members of the Rho family of GTPases
    • Clark, E. A., W. G. King, J. S. Brugge, M. Symons, and R. O. Hynes. 1998. Integrin-mediated signals regulated by members of the Rho family of GTPases. J. Cell Biol. 142:573-586.
    • (1998) J. Cell Biol. , vol.142 , pp. 573-586
    • Clark, E.A.1    King, W.G.2    Brugge, J.S.3    Symons, M.4    Hynes, R.O.5
  • 14
    • 0029907265 scopus 로고    scopus 로고
    • A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
    • Dikic, I., G. Tokiwa, S. Lev, S. A. Courtneidge, and J. Schlessinger. 1996. A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature 383:547-550.
    • (1996) Nature , vol.383 , pp. 547-550
    • Dikic, I.1    Tokiwa, G.2    Lev, S.3    Courtneidge, S.A.4    Schlessinger, J.5
  • 15
    • 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 M. C. Frame. 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
  • 16
    • 0028018234 scopus 로고
    • Potential role for focal adhesion kinase in migrating and proliferating keratinocytes near epidermal wounds and in culture
    • Gates, R. E., L. E. King, Jr., S. K. Hanks, and L. B. Nanney. 1994. Potential role for focal adhesion kinase in migrating and proliferating keratinocytes near epidermal wounds and in culture. Cell Growth Differ. 5:891-899.
    • (1994) Cell Growth Differ. , vol.5 , pp. 891-899
    • Gates, R.E.1    King L.E., Jr.2    Hanks, S.K.3    Nanney, L.B.4
  • 17
    • 0029741102 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation
    • Gilmore, A. P., and L. H. Romer. 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
  • 18
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen, M., and H. Bujard. 1992. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl. Acad. Sci. USA 89:5547-5551.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 19
    • 0026759309 scopus 로고
    • Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • Guan, J.-L., and D. Shalloway. 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
  • 23
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks, S. K., M. B. Calalb, M. C. Harper, and S. K. Patel. 1992. Focal adhesion protein-tyrosine 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
  • 24
    • 0031081425 scopus 로고    scopus 로고
    • Signaling through focal adhesion kinase
    • Hanks, S. K, and T. R. Polte. 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
  • 27
    • 0029055784 scopus 로고
    • Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase
    • Hildebrand, J. D., M. D. Schaller, and J. T. Parsons. 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
  • 30
    • 0025376378 scopus 로고
    • Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases
    • Kanner, S. B., A. B. Reynolds, R. R. Vines, and J. T. Parsons. 1990. Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc. Natl. Acad. Sci. USA 87:3328-3332.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3328-3332
    • Kanner, S.B.1    Reynolds, A.B.2    Vines, R.R.3    Parsons, J.T.4
  • 31
    • 0029034939 scopus 로고
    • c-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase-independent mechanism
    • Kaplan, K. B., J. R. Swedlow, D. O. Morgan, and H. E. Varmus. 1995. c-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase-independent mechanism. Genes Dev. 9:1505-1517.
    • (1995) Genes Dev. , vol.9 , pp. 1505-1517
    • Kaplan, K.B.1    Swedlow, J.R.2    Morgan, D.O.3    Varmus, H.E.4
  • 33
    • 0032559562 scopus 로고    scopus 로고
    • CAS/Crk coupling serves as a "molecular switch" for induction of cell migration
    • Klemke, R. L., J. Leng, R. Molander, P. C. Brooks, K. Vuori, and D. A. Cheresh. 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
  • 34
    • 0027055575 scopus 로고
    • Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
    • Kornberg, L. J., H. S. Earp, J. T. Parsons, M. Schaller, and R. L. Juliano. 1992. Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J. Biol. Chem. 267:23439-23442.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23439-23442
    • Kornberg, L.J.1    Earp, H.S.2    Parsons, J.T.3    Schaller, M.4    Juliano, R.L.5
  • 36
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D. A., and A. F. Horwitz. 1996. Cell migration: a physically integrated molecular process. Cell 84:359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 38
    • 0029978533 scopus 로고    scopus 로고
    • Characterization of RAFTK, a novel focal adhesion kinase, and its integrin-dependent phosphorylation and activation in megakaryocytes
    • Li, J., H. Avraham, R. A. Rogers, S. Raja, and S. Avraham. 1996. Characterization of RAFTK, a novel focal adhesion kinase, and its integrin-dependent phosphorylation and activation in megakaryocytes. Blood 88:417-428.
    • (1996) Blood , vol.88 , pp. 417-428
    • Li, J.1    Avraham, H.2    Rogers, R.A.3    Raja, S.4    Avraham, S.5
  • 39
    • 0030944686 scopus 로고    scopus 로고
    • Paxillin is tyrosine-phosphorylated by and preferentially associates with the calcium-dependent tyrosine kinase in rat liver epithelial cells
    • Li, X., and H. S. Earp. 1997. Paxillin is tyrosine-phosphorylated by and preferentially associates with the calcium-dependent tyrosine kinase in rat liver epithelial cells. J. Biol. Chem. 272:14341-14348.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14341-14348
    • Li, X.1    Earp, H.S.2
  • 40
    • 0026497659 scopus 로고
    • Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets
    • Lipfert, L., B. Haimovich, M. D. Schaller, B. S. Cobb, J. T. Parsons, and J. S. Brugge. 1992. Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets. J. Cell Biol. 119:905-912.
    • (1992) J. Cell Biol. , vol.119 , pp. 905-912
    • Lipfert, L.1    Haimovich, B.2    Schaller, M.D.3    Cobb, B.S.4    Parsons, J.T.5    Brugge, J.S.6
  • 41
    • 0020501846 scopus 로고
    • Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses
    • Lipsich, L. A., A. J. Lewis, and J. S. Brugge. 1983. Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses. J. Virol. 48:352-360.
    • (1983) J. Virol. , vol.48 , pp. 352-360
    • Lipsich, L.A.1    Lewis, A.J.2    Brugge, J.S.3
  • 42
    • 0032500744 scopus 로고    scopus 로고
    • Vanadate-dependent FAK activation is accomplished by the sustained FAK Tyr-576/577 phosphorylation
    • Maa, M.-C., and T.-H. Leu. 1998. Vanadate-dependent FAK activation is accomplished by the sustained FAK Tyr-576/577 phosphorylation. Biochem. Biophys. Res. Commun. 251:344-349.
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 344-349
    • Maa, M.-C.1    Leu, T.-H.2
  • 43
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and locomotion
    • Mitchison, T. J., and L. P. Cramer. 1996. Actin-based cell motility and locomotion. Cell 84:371-379.
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 44
    • 0025352187 scopus 로고
    • Advanced mammalian gene transfer: High titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line
    • Morgenstern, J. P., and H. Land. 1990. Advanced mammalian gene transfer: high titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line. Nucleic Acids Res. 18:3587-3596.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3587-3596
    • Morgenstern, J.P.1    Land, H.2
  • 46
    • 0032521559 scopus 로고    scopus 로고
    • Cas-related proteins and a GTPase-activating protein, Graf
    • Cas-related proteins and a GTPase-activating protein, Graf. Biochem. J. 330:1249-1254.
    • (1998) Biochem. J. , vol.330 , pp. 1249-1254
    • Ohba, T.1    Ishino, M.2    Aoto, H.3    Sasaki, T.4
  • 47
    • 0028940658 scopus 로고
    • Adhesion-induced tyrosine phosphorylation of the p130 SRC substrate
    • Petch, L. A., S. M. Bockholt, A. Bouton, J. T. Parsons, and K. Burridge. 1995. Adhesion-induced tyrosine phosphorylation of the p130 SRC substrate. J. Cell Sci. 108:1371-1379.
    • (1995) J. Cell Sci. , vol.108 , pp. 1371-1379
    • Petch, L.A.1    Bockholt, S.M.2    Bouton, A.3    Parsons, J.T.4    Burridge, K.5
  • 49
    • 0031047981 scopus 로고    scopus 로고
    • Cas) are elevated in cytoskeletal-associated fractions following adhesion and Src transformation: Requirements for Src kinase activity and FAK proline-rich motifs
    • Cas) are elevated in cytoskeletal-associated fractions following adhesion and Src transformation: requirements for Src kinase activity and FAK proline-rich motifs. J. Biol. Chem. 272:5501-5509.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5501-5509
    • Polte, T.R.1    Hanks, S.K.2
  • 50
    • 0031844821 scopus 로고    scopus 로고
    • Activation of Rac and Cdc42 by integrins mediates cell spreading
    • Price, L. S., J. Leng, M. A. Schwartz, and G. M. Bokoch. 1998. Activation of Rac and Cdc42 by integrins mediates cell spreading. Mol. Biol. Cell 9: 1863-1871.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1863-1871
    • Price, L.S.1    Leng, J.2    Schwartz, M.A.3    Bokoch, G.M.4
  • 51
    • 0030293886 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/Rho-dependent effector pathways
    • Reif, K., C. D. Nobes, G. Thomas, A. Hall, and D. A. Cantrell. 1996. Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/Rho-dependent effector pathways. Curr. Biol. 6:1445-1455.
    • (1996) Curr. Biol. , vol.6 , pp. 1445-1455
    • Reif, K.1    Nobes, C.D.2    Thomas, G.3    Hall, A.4    Cantrell, D.A.5
  • 52
    • 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., R. K. Malik, J. D. Hildebrand, and J. T. Parsons. 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
  • 54
    • 0032563218 scopus 로고    scopus 로고
    • Bombesin, vasopressin, lysophosphatidic acid, and sphingosylphosphorylcholine induce focal adhesion kinase activation in intact Swiss 3T3 cells
    • Rodriquez-Fernandez, J. L., and E. Rozengurt. 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
    • Rodriquez-Fernandez, J.L.1    Rozengurt, E.2
  • 56
    • 0031297086 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in the action of neuropeptides and growth factors
    • Rozengurt, E., and J. L. Rodriguez-Fernandez. 1997. Tyrosine phosphorylation in the action of neuropeptides and growth factors. Essays Biochem. 32: 73-86.
    • (1997) Essays Biochem. , vol.32 , pp. 73-86
    • Rozengurt, E.1    Rodriguez-Fernandez, J.L.2
  • 60
    • 0029096541 scopus 로고
    • Cloning and characterization of cell adhesion kinase β, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily
    • Sasaki, H., K. Nagura, M. Ishino, H. Tobioka, K. Kotani, and T. Sasaki. 1995. Cloning and characterization of cell adhesion kinase β, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily. J. Biol. Chem. 270; 21206-21219.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21206-21219
    • Sasaki, H.1    Nagura, K.2    Ishino, M.3    Tobioka, H.4    Kotani, K.5    Sasaki, T.6
  • 63
    • 0028986116 scopus 로고
    • FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
    • FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol. Cell. Biol. 15:2635-2645.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2635-2645
    • Schaller, M.D.1    Parsons, J.T.2
  • 64
    • 0030771904 scopus 로고    scopus 로고
    • Differential signaling by the focal adhesion kinase and cell adhesion kinase beta
    • Schaller, M. D., and T. Sasaki. 1997. Differential signaling by the focal adhesion kinase and cell adhesion kinase beta. J. Biol. Chem. 272:25319-25325.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25319-25325
    • Schaller, M.D.1    Sasaki, T.2
  • 65
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer, D. D., S. K. Hanks, T. Hunter, and P. van der Geer. 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
  • 66
    • 0029834447 scopus 로고    scopus 로고
    • Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein-tyrosine kinases
    • Schlaepfer, D. D., and T. Hunter. 1996. Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein-tyrosine kinases. Mol. Cell. Biol. 16:5623-5633.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5623-5633
    • Schlaepfer, D.D.1    Hunter, T.2
  • 68
    • 0030926774 scopus 로고    scopus 로고
    • Focal adhesion kinase overexpression enhances Ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src
    • Schlaepfer, D. D., and T. Hunter. 1997. Focal adhesion kinase overexpression enhances Ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src. J. Biol. Chem. 272:13189-13195.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13189-13195
    • Schlaepfer, D.D.1    Hunter, T.2
  • 69
    • 0031921101 scopus 로고    scopus 로고
    • Multiple Grb2-mediated integrin-stimulated signaling pathways to ERK2 mitogen-activated protein kinase: Summation of both c-Src- and focal adhesion kinase-initiated tyrosine phosphorylation events
    • Schlaepfer, D. D., K. C. Jones, and T. Hunter. 1998. Multiple Grb2-mediated integrin-stimulated signaling pathways to ERK2 mitogen-activated protein kinase: summation of both c-Src- and focal adhesion kinase-initiated tyrosine phosphorylation events. Mol. Cell. Biol. 18:2571-2585.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2571-2585
    • Schlaepfer, D.D.1    Jones, K.C.2    Hunter, T.3
  • 70
    • 0031964022 scopus 로고    scopus 로고
    • Cell migration: Regulation of force on extracellular matrix-integrin complexes
    • Sheets, M. P., D. P. Felsenfeld, and C. G. Galbraith. 1998. Cell migration: regulation of force on extracellular matrix-integrin complexes. Trends Cell Biol. 81:51-54.
    • (1998) Trends Cell Biol. , vol.81 , pp. 51-54
    • Sheets, M.P.1    Felsenfeld, D.P.2    Galbraith, C.G.3
  • 71
    • 0032531732 scopus 로고    scopus 로고
    • Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK- cell migration
    • Sieg, D. J., D. Ilic, K. C. Jones, C. H. Damsky, T. Hunter, and D. D. Schlaepfer. 1998. Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK- cell migration. EMBO J. 17:5933-5947.
    • (1998) EMBO J. , vol.17 , pp. 5933-5947
    • Sieg, D.J.1    Ilic, D.2    Jones, K.C.3    Damsky, C.H.4    Hunter, T.5    Schlaepfer, D.D.6
  • 73
    • 0030669961 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase - A putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates
    • Tachibana, K., T. Urano, H. Fujita, Y. Ohashi, K. Kamiguchi, S. Iwata, H. Hirai, and C. Morimoto. 1997. Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase - a putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates. J. Biol. Chem. 272:29083-29090.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29083-29090
    • Tachibana, K.1    Urano, T.2    Fujita, H.3    Ohashi, Y.4    Kamiguchi, K.5    Iwata, S.6    Hirai, H.7    Morimoto, C.8
  • 74
    • 0033593220 scopus 로고    scopus 로고
    • Adenovirus-mediated overexpression of C-terminal Src kinase (Csk) in type I astrocytes interferes with cell spreading and attachment to fibronectin
    • Takayama, T., S. Tanaka, K. Nagai, and M. Okada. 1999. Adenovirus-mediated overexpression of C-terminal Src kinase (Csk) in type I astrocytes interferes with cell spreading and attachment to fibronectin. J. Biol. Chem. 274:2291-2297.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2291-2297
    • Takayama, T.1    Tanaka, S.2    Nagai, K.3    Okada, M.4
  • 75
    • 0025008074 scopus 로고
    • Paxillin: A new vinculin-binding protein present in focal adhesions
    • Turner, C. E., J. R. Glenney, and K. Burridge. 1990. Paxillin: a new vinculin-binding protein present in focal adhesions. J. Cell Biol. 111:1059-1068.
    • (1990) J. Cell Biol. , vol.111 , pp. 1059-1068
    • Turner, C.E.1    Glenney, J.R.2    Burridge, K.3
  • 77
    • 0029664531 scopus 로고    scopus 로고
    • cas signaling complex formation upon integrin-mediated cell adhesion: A role for Src family kinases
    • cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases. Mol. Cell. Biol. 16:2606-2613.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2606-2613
    • Vuori, K.1    Hirai, H.2    Aizawa, S.3    Ruoslahti, E.4
  • 78
    • 0030087588 scopus 로고    scopus 로고
    • Expression, purification, and characterization of focal adhesion kinase using a baculovirus system
    • Withers, B. E., P. R. Keller, and D. W. Fry. 1996. Expression, purification, and characterization of focal adhesion kinase using a baculovirus system. Protein Expr. Purif. 7:12-18.
    • (1996) Protein Expr. Purif. , vol.7 , pp. 12-18
    • Withers, B.E.1    Keller, P.R.2    Fry, D.W.3
  • 80
    • 0028342938 scopus 로고
    • Direct interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain
    • Xing, Z., H.-C. Chen, J. K. Nowlen, S. J. Taylor, D. Shalloway, and J.-L. Guan. 1994. Direct interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain. Mol. Biol. Cell 5:413-421.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 413-421
    • Xing, Z.1    Chen, H.-C.2    Nowlen, J.K.3    Taylor, S.J.4    Shalloway, D.5    Guan, J.-L.6
  • 81
    • 0010233279 scopus 로고    scopus 로고
    • Activation of a novel calcium-dependent protein-tyrosine kinase. Correlation with c-Jun N-terminal kinase but not mitogen-activated protein kinase activation
    • Yu, H., X. Li, G. S. Marchetto, R. Dy, D. Hunter, B. Calvo, T. L. Dawson, M. Wilm, R. J. Anderegg, L. M. Graves, and H. S. Earp. 1996. Activation of a novel calcium-dependent protein-tyrosine kinase. Correlation with c-Jun N-terminal kinase but not mitogen-activated protein kinase activation. J. Biol. Chem. 271:29993-29998.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29993-29998
    • Yu, H.1    Li, X.2    Marchetto, G.S.3    Dy, R.4    Hunter, D.5    Calvo, B.6    Dawson, T.L.7    Wilm, M.8    Anderegg, R.J.9    Graves, L.M.10    Earp, H.S.11
  • 83
    • 0031917388 scopus 로고    scopus 로고
    • Differential regulation of Pyk2 and focal adhesion kinase (FAK). The C-terminal domain of FAK confers response to cell adhesion
    • Zheng, C., Z. King, Z. C. Blan, C. Guo, A. Akbay, L. Warner, and J.-L. Guan. 1998. Differential regulation of Pyk2 and focal adhesion kinase (FAK). The C-terminal domain of FAK confers response to cell adhesion. J. Biol. Chem. 273:2384-2389.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2384-2389
    • Zheng, C.1    King, Z.2    Blan, Z.C.3    Guo, C.4    Akbay, A.5    Warner, L.6    Guan, J.-L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.