메뉴 건너뛰기




Volumn 16, Issue 9, 2005, Pages 4316-4328

Src and FAK kinases cooperate to phosphorylate paxillin kinase linker, stimulate its focal adhesion localization, and regulate cell spreading and protrusiveness

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; FIBRONECTIN; FOCAL ADHESION KINASE; G PROTEIN COUPLED RECEPTOR KINASE; G PROTEIN COUPLED RECEPTOR KINASE INTERACTING PROTEIN 2; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; INTEGRIN; MUTANT PROTEIN; P21 ACTIVATED KINASE; PAXILLIN; PAXILLIN KINASE LINKER; PROTEIN KINASE; PROTEIN NCK; PROTEIN SH2; PROTEIN SH3; PROTEIN TYROSINE KINASE; RAC PROTEIN; TYROSINE; UNCLASSIFIED DRUG;

EID: 24344508125     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-02-0131     Document Type: Article
Times cited : (146)

References (95)
  • 2
    • 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., and Tremblay, M. L. (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    Tremblay, M.L.7
  • 3
    • 0033529562 scopus 로고    scopus 로고
    • A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins
    • Bagrodia, S., Bailey, D., Lenard, Z., Hart, M., Guan, J. L., Premont, R. T., Taylor, S. J., and Cerione, R. A. (1999). A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins. J. Biol. Chem. 274, 22393-22400.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22393-22400
    • Bagrodia, S.1    Bailey, D.2    Lenard, Z.3    Hart, M.4    Guan, J.L.5    Premont, R.T.6    Taylor, S.J.7    Cerione, R.A.8
  • 5
    • 0038383014 scopus 로고    scopus 로고
    • The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network
    • Bladt, F., Aippersbach, E., Gelkop, S., Strasser, G. A., Nash, P., Tafuri, A., Gertler, F. B., and Pawson, T. (2003). The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network. Mol. Cell. Biol. 23, 4586-4597.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4586-4597
    • Bladt, F.1    Aippersbach, E.2    Gelkop, S.3    Strasser, G.A.4    Nash, P.5    Tafuri, A.6    Gertler, F.B.7    Pawson, T.8
  • 6
    • 0038554077 scopus 로고    scopus 로고
    • Biology of the p21-activated kinases
    • Bokoch, G. M. (2003). Biology of the p21-activated kinases. Annu. Rev. Biochem. 72, 743-781.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 743-781
    • Bokoch, G.M.1
  • 7
    • 0029911521 scopus 로고    scopus 로고
    • Interaction of the Nck adapter protein with p21-activated kinase (PAK1)
    • Bokoch, G. M., Wang, Y., Bohl, B. P., Sells, M. A., Quilliam, L. A., and Knaus, U. G. (1996). Interaction of the Nck adapter protein with p21-activated kinase (PAK1). J. Biol. Chem. 271, 25746-25749.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25746-25749
    • Bokoch, G.M.1    Wang, Y.2    Bohl, B.P.3    Sells, M.A.4    Quilliam, L.A.5    Knaus, U.G.6
  • 8
    • 0031847578 scopus 로고    scopus 로고
    • Serine and threonine phosphorylation of the paxillin LIM domains regulates paxillin focal adhesion localization and cell adhesion to fibronectin
    • Brown, M. C., Perrotta, J. A., and Turner, C. E. (1998a). Serine and threonine phosphorylation of the paxillin LIM domains regulates paxillin focal adhesion localization and cell adhesion to fibronectin. Mol. Biol. Cell 9, 1803-1816.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1803-1816
    • Brown, M.C.1    Perrotta, J.A.2    Turner, C.E.3
  • 9
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin: Adapting to change
    • Brown, M. C., and Turner, C. E. (2004). Paxillin: adapting to change. Physiol. Rev. 84, 1315-1339.
    • (2004) Physiol. Rev. , vol.84 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2
  • 10
    • 0035999990 scopus 로고    scopus 로고
    • Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway
    • Brown, M. C., West, K. A., and Turner, C. E. (2002). Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway. Mol. Biol. Cell 13, 1550-1565.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1550-1565
    • Brown, M.C.1    West, K.A.2    Turner, C.E.3
  • 11
    • 0031784899 scopus 로고    scopus 로고
    • ASAP1, a phospholipid-dependent Arf GTPase-activating protein that associates with and is phosphorylated by Src
    • Brown, M. T., Andrade, J., Radhakrishna, H., Donaldson, J. G., Cooper, J. A., and Randazzo, P. A. (1998b). ASAP1, a phospholipid-dependent Arf GTPase-activating protein that associates with and is phosphorylated by Src. Mol. Cell. Biol. 18, 7038-7051.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7038-7051
    • Brown, M.T.1    Andrade, J.2    Radhakrishna, H.3    Donaldson, J.G.4    Cooper, J.A.5    Randazzo, P.A.6
  • 12
    • 0036015163 scopus 로고    scopus 로고
    • The Nck family of adapter proteins: Regulators of actin cytoskeleton
    • Buday, L., Wunderlich, L., and Tamas, P. (2002). The Nck family of adapter proteins: regulators of actin cytoskeleton. Cell Signal 14, 723-731.
    • (2002) Cell Signal , vol.14 , pp. 723-731
    • Buday, L.1    Wunderlich, L.2    Tamas, P.3
  • 13
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge, K., and Wennerberg, K. (2004). Rho and Rac take center stage. Cell 116, 167-179.
    • (2004) Cell , vol.116 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 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
    • 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
  • 16
    • 0036205320 scopus 로고    scopus 로고
    • SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading
    • Cary, L. A., Klinghoffer, R. A., Sachsenmaier, C., and Cooper, J. A. (2002). SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading. Mol. Cell. Biol. 22, 2427-2440.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2427-2440
    • Cary, L.A.1    Klinghoffer, R.A.2    Sachsenmaier, C.3    Cooper, J.A.4
  • 17
    • 12844258883 scopus 로고    scopus 로고
    • Endothelin 1 induces beta 1Pix translocation and Cdc42 activation via protein kinase A-dependent pathway
    • Chahdi, A., Miller, B., and Sorokin, A. (2005). Endothelin 1 induces beta 1Pix translocation and Cdc42 activation via protein kinase A-dependent pathway. J. Biol. Chem. 280, 578-584.
    • (2005) J. Biol. Chem. , vol.280 , pp. 578-584
    • Chahdi, A.1    Miller, B.2    Sorokin, A.3
  • 18
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen, G. B., Ren, R., and Baltimore, D. (1995). Modular binding domains in signal transduction proteins. Cell 80, 237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 19
    • 0039180030 scopus 로고    scopus 로고
    • Intact LIM 3 and LIM 4 domains of paxillin are required for the association to a novel polyproline region (Pro 2) of protein-tyrosine phosphatase-PEST
    • Cote, J. p., Turner, C. E., and Tremblay, M. L. (1999). Intact LIM 3 and LIM 4 domains of paxillin are required for the association to a novel polyproline region (Pro 2) of protein-tyrosine phosphatase-PEST. J. Biol. Chem. 274, 20550-20560.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20550-20560
    • Cote, J.P.1    Turner, C.E.2    Tremblay, M.L.3
  • 20
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • Feng, S., Chen, J. K., Yu, H., Simon, J. A., and Schreiber, S. L. (1994). Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266, 1241-1247.
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 21
    • 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
  • 22
    • 0028783271 scopus 로고
    • Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK
    • 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) Oncogene , vol.11 , pp. 1989-1995
    • Furuta, Y.1    Ilic, D.2    Kanazawa, S.3    Takeda, N.4    Yamamoto, T.5    Aizawa, S.6
  • 23
    • 0036682924 scopus 로고    scopus 로고
    • Characterization of an activated mutant of focal adhesion kinase: 'SuperFAK'
    • Gabarra-Niecko, V., Keely, P. J., and Schaller, M. D. (2002). Characterization of an activated mutant of focal adhesion kinase: 'SuperFAK.' Biochem. J. 365, 591-603.
    • (2002) Biochem. J. , vol.365 , pp. 591-603
    • Gabarra-Niecko, V.1    Keely, P.J.2    Schaller, M.D.3
  • 24
    • 0029830139 scopus 로고    scopus 로고
    • The adaptor protein Nck links receptor tyrosine kinases with the serine-threonine kinase Pak1
    • Galisteo, M. L., Chernoff, J., Su, Y. C., Skolnik, E. Y., and Schlessinger, J. (1996). The adaptor protein Nck links receptor tyrosine kinases with the serine-threonine kinase Pak1. J. Biol. Chem. 271, 20997-21000.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20997-21000
    • Galisteo, M.L.1    Chernoff, J.2    Su, Y.C.3    Skolnik, E.Y.4    Schlessinger, J.5
  • 25
    • 0345687500 scopus 로고    scopus 로고
    • Positional control of cell fate through joint integrin/receptor protein kinase signaling
    • Giancotti, F. G., and Tarone, G. (2003). Positional control of cell fate through joint integrin/receptor protein kinase signaling. Annu. Rev. Cell. Dev. Biol. 19, 173-206.
    • (2003) Annu. Rev. Cell. Dev. Biol. , vol.19 , pp. 173-206
    • Giancotti, F.G.1    Tarone, G.2
  • 27
    • 0036142219 scopus 로고    scopus 로고
    • The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling
    • Hagel, M., George, E. L., Kim, A., Tamimi, R., Opitz, S. L., Turner, C. E., Imamoto, A., and Thomas, S. M. (2002). The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling. Mol. Cell. Biol. 22, 901-915.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 901-915
    • Hagel, M.1    George, E.L.2    Kim, A.3    Tamimi, R.4    Opitz, S.L.5    Turner, C.E.6    Imamoto, A.7    Thomas, S.M.8
  • 30
    • 0035937140 scopus 로고    scopus 로고
    • Interaction of paxillin with p21-activated Kinase (PAK). Association of paxillin alpha with the kinase-inactive and the Cdc42-activated forms of PAK3
    • Hashimoto, S., Tsubouchi, A., Mazaki, Y., and Sabe, H. (2001). Interaction of paxillin with p21-activated Kinase (PAK). Association of paxillin alpha with the kinase-inactive and the Cdc42-activated forms of PAK3. J. Biol. Chem. 276, 6037-6045.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6037-6045
    • Hashimoto, S.1    Tsubouchi, A.2    Mazaki, Y.3    Sabe, H.4
  • 31
    • 0035413610 scopus 로고    scopus 로고
    • Chinese hamster ovary-Src tyrosine phosphorylation of EGF receptor, P190 RhoGAP, and focal adhesion kinase regulates diverse cellular processes
    • Haskell, M. D., Slack, J. K., Parsons, J. T., and Parsons, S. J. (2001). Chinese hamster ovary-Src tyrosine phosphorylation of EGF receptor, P190 RhoGAP, and focal adhesion kinase regulates diverse cellular processes. Chem. Rev. 101, 2425-2440.
    • (2001) Chem. Rev. , vol.101 , pp. 2425-2440
    • Haskell, M.D.1    Slack, J.K.2    Parsons, J.T.3    Parsons, S.J.4
  • 32
    • 0029955660 scopus 로고    scopus 로고
    • An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase
    • Hildebrand, J. D., Taylor, J. M., and Parsons, J. T. (1996). An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase. Mol. Cell. Biol. 16, 3169-3178.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3169-3178
    • Hildebrand, J.D.1    Taylor, J.M.2    Parsons, J.T.3
  • 33
    • 17344362766 scopus 로고    scopus 로고
    • Cardiovascular anomaly, impaired actin bundling and resistance to Src-induced transformation in mice lacking p130Cas
    • Honda, H., et al. (1998). Cardiovascular anomaly, impaired actin bundling and resistance to Src-induced transformation in mice lacking p130Cas. Nat. Genet. 19, 361-365.
    • (1998) Nat. Genet. , vol.19 , pp. 361-365
    • Honda, H.1
  • 34
    • 0035805512 scopus 로고    scopus 로고
    • Cell adhesion regulates the interaction between Nck and p21-activated kinase
    • Howe, A. K. (2001). Cell adhesion regulates the interaction between Nck and p21-activated kinase. J. Biol. Chem. 276, 14541-14544.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14541-14544
    • Howe, A.K.1
  • 35
    • 0033786922 scopus 로고    scopus 로고
    • Protein tyrosine kinase structure and function
    • Hubbard, S. R., and Till, J. H. (2000). Protein tyrosine kinase structure and function. Annu. Rev. Biochem. 69, 373-398.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 373-398
    • Hubbard, S.R.1    Till, J.H.2
  • 37
    • 0027289232 scopus 로고
    • Disruption of the csk gene, encoding a negative regulator of Src family tyrosine kinases, leads to neural tube defects and embryonic lethality in mice
    • Imamoto, A., and Soriano, P. (1993). Disruption of the csk gene, encoding a negative regulator of Src family tyrosine kinases, leads to neural tube defects and embryonic lethality in mice. Cell 73, 1117-1124.
    • (1993) Cell , vol.73 , pp. 1117-1124
    • Imamoto, A.1    Soriano, P.2
  • 38
    • 20244390565 scopus 로고    scopus 로고
    • Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin in MM1 cancer cell migration
    • Iwasaki, T., et al. (2002). Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin in MM1 cancer cell migration. Int. J. Cancer 97, 330-335.
    • (2002) Int. J. Cancer , vol.97 , pp. 330-335
    • Iwasaki, T.1
  • 40
    • 0036178447 scopus 로고    scopus 로고
    • Signal transduction by cell adhesion receptors and the cytoskeleton: Functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members
    • Juliano, R. L. (2002). Signal transduction by cell adhesion receptors and the cytoskeleton: functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members. Annu. Rev. Pharmacol. Toxicol. 42, 283-323.
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 283-323
    • Juliano, R.L.1
  • 41
    • 0028151515 scopus 로고
    • Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527
    • Kaplan, K. B., Bibbins, K. B., Swedlow, J. R., Arnaud, M., Morgan, D. O., and Varmus, H. E. (1994). Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. EMBO J. 13, 4745-4756.
    • (1994) EMBO J. , vol.13 , pp. 4745-4756
    • Kaplan, K.B.1    Bibbins, K.B.2    Swedlow, J.R.3    Arnaud, M.4    Morgan, D.O.5    Varmus, H.E.6
  • 42
    • 0029034939 scopus 로고
    • Chinese hamster ovary-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase-independent mechanism
    • Kaplan, K. B., Swedlow, J. R., Morgan, D. O., and Varmus, H. E. (1995). Chinese hamster ovary-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
  • 43
    • 0037458544 scopus 로고    scopus 로고
    • The GIT family of proteins forms multimers and associates with the presynaptic cytomatrix protein Piccolo
    • Kim, S., et al. (2003). The GIT family of proteins forms multimers and associates with the presynaptic cytomatrix protein Piccolo. J. Biol. Chem. 278, 6291-6300.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6291-6300
    • Kim, S.1
  • 46
    • 0034008403 scopus 로고    scopus 로고
    • Induction of Rac-guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm) following phosphorylation by the nonreceptor tyrosine kinase Src
    • Kiyono, M., Kaziro, Y., and Satoh, T. (2000). Induction of Rac-guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm) following phosphorylation by the nonreceptor tyrosine kinase Src. J. Biol. Chem. 275, 5441-5446.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5441-5446
    • Kiyono, M.1    Kaziro, Y.2    Satoh, T.3
  • 47
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • Klinghoffer, R. A., Sachsenmaier, C., Cooper, J. A., and Soriano, P. (1999). Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J. 18, 2459-2471.
    • (1999) EMBO J. , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 48
    • 0037769892 scopus 로고    scopus 로고
    • Crk associates with a multimolecular Paxillin/GIT2/beta-PIX complex and promotes Rac-dependent relocalization of Paxillin to focal contacts
    • Lamorte, L., Rodrigues, S., Sangwan, V., Turner, C. E., and Park, M. (2003). Crk associates with a multimolecular Paxillin/GIT2/beta-PIX complex and promotes Rac-dependent relocalization of Paxillin to focal contacts. Mol. Biol. Cell 14, 2818-2831.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2818-2831
    • Lamorte, L.1    Rodrigues, S.2    Sangwan, V.3    Turner, C.E.4    Park, M.5
  • 49
    • 0036146543 scopus 로고    scopus 로고
    • Focal adhesions require catalytic activity of Src family kinases to mediate integrin-marrix adhesion
    • Li, L., Okura, M., and Imamoto, A. (2002). Focal adhesions require catalytic activity of Src family kinases to mediate integrin-marrix adhesion. Mol. Cell. Biol. 22, 1203-1217.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1203-1217
    • Li, L.1    Okura, M.2    Imamoto, A.3
  • 50
    • 0033605594 scopus 로고    scopus 로고
    • Interactions between two cytoskeleton-associated tyrosine kinases: Calcium-dependent tyrosine kinase and focal adhesion tyrosine kinase
    • Li, X., Dy, R. C., Cance, W. G., Graves, L. M., and Earp, H. S. (1999). Interactions between two cytoskeleton-associated tyrosine kinases: calcium-dependent tyrosine kinase and focal adhesion tyrosine kinase. J. Biol. Chem. 274, 8917-8924.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8917-8924
    • Li, X.1    Dy, R.C.2    Cance, W.G.3    Graves, L.M.4    Earp, H.S.5
  • 51
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • Lim, W. A., Richards, F. M., and Fox, R. O. (1994). Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature 372, 375-379.
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 52
    • 0031080595 scopus 로고    scopus 로고
    • Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck
    • Lu, W., Katz, S., Gupta, R., and Mayer, B. J. (1997). Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck. Curr. Biol. 7, 85-94.
    • (1997) Curr. Biol. , vol.7 , pp. 85-94
    • Lu, W.1    Katz, S.2    Gupta, R.3    Mayer, B.J.4
  • 53
    • 0036537895 scopus 로고    scopus 로고
    • GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration
    • Manabe Ri, R., Kovalenko, M., Webb, D. J., and Horwitz, A. R. (2002). GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration. J. Cell Sci. 115, 1497-1510.
    • (2002) J. Cell Sci. , vol.115 , pp. 1497-1510
    • Manabe Ri, R.1    Kovalenko, M.2    Webb, D.J.3    Horwitz, A.R.4
  • 54
  • 55
    • 0035694169 scopus 로고    scopus 로고
    • Molecular mechanisms regulating the subcellular localization of p95-APP1 between the endosomal recycling compartment and sites of actin organization at the cell surface
    • Matafora, V., Paris, S., Dariozzi, S., and de Curtis, I. (2001). Molecular mechanisms regulating the subcellular localization of p95-APP1 between the endosomal recycling compartment and sites of actin organization at the cell surface. J. Cell Sci. 114, 4509-4520.
    • (2001) J. Cell Sci. , vol.114 , pp. 4509-4520
    • Matafora, V.1    Paris, S.2    Dariozzi, S.3    De Curtis, I.4
  • 56
    • 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
  • 57
    • 0036242467 scopus 로고    scopus 로고
    • Myosin VI binds to and localises with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton
    • Morris, S. M., Arden, S. D., Roberts, R. C., Kendrick-Jones, J., Cooper, J. A., Luzio, J. P., and Buss, F. (2002). Myosin VI binds to and localises with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton. Traffic 3, 331-341.
    • (2002) Traffic , vol.3 , pp. 331-341
    • Morris, S.M.1    Arden, S.D.2    Roberts, R.C.3    Kendrick-Jones, J.4    Cooper, J.A.5    Luzio, J.P.6    Buss, F.7
  • 58
    • 0025881470 scopus 로고
    • Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src
    • Nada, S., Okada, M., MacAuley, A., Cooper, J. A., and Nakagawa, H. (1991). Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src. Nature 351, 69-72.
    • (1991) Nature , vol.351 , pp. 69-72
    • Nada, S.1    Okada, M.2    MacAuley, A.3    Cooper, J.A.4    Nakagawa, H.5
  • 59
    • 17344366888 scopus 로고    scopus 로고
    • An alpha4 integrin-paxillin-Arf-GAP complex restricts Rac activation to the leading edge of migrating cells
    • Nishiya, N., Kiosses, W. B., Han, J., and Ginsberg, M. H. (2005). An alpha4 integrin-paxillin-Arf-GAP complex restricts Rac activation to the leading edge of migrating cells. Nat. Cell Biol. 7, 343-352.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 343-352
    • Nishiya, N.1    Kiosses, W.B.2    Han, J.3    Ginsberg, M.H.4
  • 60
    • 0036684982 scopus 로고    scopus 로고
    • Hic-5 interacts with GIT1 with a different binding mode from paxillin
    • Nishiya, N., Shirai, T., Suzuki, W., and Nose, K. (2002). Hic-5 interacts with GIT1 with a different binding mode from paxillin. J. Biochem. 132, 279-289.
    • (2002) J. Biochem. , vol.132 , pp. 279-289
    • Nishiya, N.1    Shirai, T.2    Suzuki, W.3    Nose, K.4
  • 61
    • 0038338507 scopus 로고    scopus 로고
    • Leucine-zipper-mediated homo- and hetero-dimerization of GIT family p95-ARF GT-Pase-activating protein, PIX-, paxillin-interacting proteins 1 and 2
    • Paris, S., Longhi, R., Santambrogio, P., and de Curtis, L. (2003). Leucine-zipper-mediated homo- and hetero-dimerization of GIT family p95-ARF GT-Pase-activating protein, PIX-, paxillin-interacting proteins 1 and 2. Biochem. J. 372, 391-398.
    • (2003) Biochem. J. , vol.372 , pp. 391-398
    • Paris, S.1    Longhi, R.2    Santambrogio, P.3    De Curtis, L.4
  • 62
    • 0034610997 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine residues 31 and 118 on paxillin regulates cell migration through an association with CRK in NBT-II cells
    • Petit, V., Boyer, B., Lentz, D., Turner, C. E., Thiery, J. P., and Valles, A. M. (2000). Phosphorylation of tyrosine residues 31 and 118 on paxillin regulates cell migration through an association with CRK in NBT-II cells. J. Cell Biol. 148, 957-970.
    • (2000) J. Cell Biol. , vol.148 , pp. 957-970
    • Petit, V.1    Boyer, B.2    Lentz, D.3    Turner, C.E.4    Thiery, J.P.5    Valles, A.M.6
  • 63
    • 7944233251 scopus 로고    scopus 로고
    • The interplay between Src and integrins in normal and tumor biology
    • Playford, M. P., and Schaller, M. D. (2004). The interplay between Src and integrins in normal and tumor biology. Oncogene 23, 7928-7946.
    • (2004) Oncogene , vol.23 , pp. 7928-7946
    • Playford, M.P.1    Schaller, M.D.2
  • 64
    • 0034698059 scopus 로고    scopus 로고
    • The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing
    • Premont, R. T., Claing, A., Vitale, N., Perry, S. J., and Lefkowitz, R. J. (2000). The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing. J. Biol. Chem. 275, 22373-22380.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22373-22380
    • Premont, R.T.1    Claing, A.2    Vitale, N.3    Perry, S.J.4    Lefkowitz, R.J.5
  • 65
    • 2942703996 scopus 로고    scopus 로고
    • The GIT/PIX complex: An oligomeric assembly of GIT family ARF GTPase-activating proteins and PIX family Rac1/Cdc42 guanine nucleotide exchange factors
    • Premont, R. T., Perry, S. J., Schmalzigaug, R., Roseman, J. T., Xing, Y., and Claing, A. (2004). The GIT/PIX complex: an oligomeric assembly of GIT family ARF GTPase-activating proteins and PIX family Rac1/Cdc42 guanine nucleotide exchange factors. Cell Signal 16, 1001-1011.
    • (2004) Cell Signal , vol.16 , pp. 1001-1011
    • Premont, R.T.1    Perry, S.J.2    Schmalzigaug, R.3    Roseman, J.T.4    Xing, Y.5    Claing, A.6
  • 66
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • Raftopoulou, M., and Hall, A. (2004). Cell migration: Rho GTPases lead the way. Dev. Biol. 265, 23-32.
    • (2004) Dev. Biol. , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 67
    • 0346725004 scopus 로고    scopus 로고
    • Arf GAPs: Multifunctional proteins that regulate membrane traffic and actin remodelling
    • Randazzo, P. A., and Hirsch, D. S. (2004). Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling. Cell Signal 16, 401-413.
    • (2004) Cell Signal , vol.16 , pp. 401-413
    • Randazzo, P.A.1    Hirsch, D.S.2
  • 68
    • 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
  • 69
    • 0034769929 scopus 로고    scopus 로고
    • Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src
    • Ruest, P. J., Shin, N. Y., Polte, T. R., Zhang, X., and Hanks, S. K. (2001). Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src. Mol. Cell. Biol. 21, 7641-7652.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7641-7652
    • Ruest, P.J.1    Shin, N.Y.2    Polte, T.R.3    Zhang, X.4    Hanks, S.K.5
  • 70
    • 0034715923 scopus 로고    scopus 로고
    • Focal adhesions: A nexus for intracellular signaling and cytoskeletal dynamics
    • Sastry, S. K., and Burridge, K. (2000). Focal adhesions: a nexus for intracellular signaling and cytoskeletal dynamics. Exp. Cell Res. 261, 25-36.
    • (2000) Exp. Cell Res. , vol.261 , pp. 25-36
    • Sastry, S.K.1    Burridge, K.2
  • 71
    • 0032859988 scopus 로고    scopus 로고
    • Complex formation with focal adhesion kinase: A mechanism to regulate activity and subcellular localization of Src kinases
    • Schaller, M. D., Hildebrand, J. D., and Parsons, J. T. (1999). Complex formation with focal adhesion kinase: a mechanism to regulate activity and subcellular localization of Src kinases. Mol. Biol. Cell 10, 3489-3505.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3489-3505
    • Schaller, M.D.1    Hildebrand, J.D.2    Parsons, J.T.3
  • 72
    • 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
  • 73
    • 1942501521 scopus 로고    scopus 로고
    • Identification of Nck interacting proteins in vascular smooth muscle cells
    • Schmitz, U., Thommes, K., Beier, I., Dusing, R., and Vetter, H. (2004). Identification of Nck interacting proteins in vascular smooth muscle cells. Clin. Exp. Hypertens. 26, 267-275.
    • (2004) Clin. Exp. Hypertens. , vol.26 , pp. 267-275
    • Schmitz, U.1    Thommes, K.2    Beier, I.3    Dusing, R.4    Vetter, H.5
  • 76
    • 0031105660 scopus 로고    scopus 로고
    • Human p21-acrivated kinase (Pak1) regulates actin organization in mammalian cells
    • Sells, M. A., Knaus, U. G., Bagrodia, S., Ambrose, D. M., Bokoch, G. M., and Chernoff, J. (1997). Human p21-acrivated kinase (Pak1) regulates actin organization in mammalian cells. Curr. Biol. 7, 202-210.
    • (1997) Curr. Biol. , vol.7 , pp. 202-210
    • Sells, M.A.1    Knaus, U.G.2    Bagrodia, S.3    Ambrose, D.M.4    Bokoch, G.M.5    Chernoff, J.6
  • 77
    • 0033954773 scopus 로고    scopus 로고
    • The noncatalyric domain of protein-tyrosine phosphatase-PEST targets paxillin for dephosphorylation in vivo
    • Shen, Y., Lyons, P., Cooley, M., Davidson, D., Veillette, A., Salgia, R., Griffin, J. D., and Schaller, M. D. (2000). The noncatalyric domain of protein-tyrosine phosphatase-PEST targets paxillin for dephosphorylation in vivo. J. Biol. Chem. 275, 1405-1413.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1405-1413
    • Shen, Y.1    Lyons, P.2    Cooley, M.3    Davidson, D.4    Veillette, A.5    Salgia, R.6    Griffin, J.D.7    Schaller, M.D.8
  • 78
    • 0032513047 scopus 로고    scopus 로고
    • Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin
    • Shen, Y., Schneider, G., Cloutier, J. F., Veillette, A., and Schaller, M. D. (1998). Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin. J. Biol. Chem. 273, 6474-6481.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6474-6481
    • Shen, Y.1    Schneider, G.2    Cloutier, J.F.3    Veillette, A.4    Schaller, M.D.5
  • 79
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopepride sequences
    • Songyang, Z., et al. (1993). SH2 domains recognize specific phosphopepride sequences. Cell 72, 767-778.
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1
  • 80
    • 12344338685 scopus 로고    scopus 로고
    • ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP-dependent manner
    • Stacey, T. T., Nie, Z., Stewart, A., Najdovska, M., Hall, N. E., He, H., Randazzo, P. A., and Lock, P. (2004). ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP-dependent manner. J. Cell Sci. 117, 6071-6084.
    • (2004) J. Cell Sci. , vol.117 , pp. 6071-6084
    • Stacey, T.T.1    Nie, Z.2    Stewart, A.3    Najdovska, M.4    Hall, N.E.5    He, H.6    Randazzo, P.A.7    Lock, P.8
  • 81
    • 1542786900 scopus 로고    scopus 로고
    • Regulation of cortical actin networks in cell migration
    • Suetsugu, S., and Takenawa, T. (2003). Regulation of cortical actin networks in cell migration. Int. Rev. Cytol. 229, 245-286.
    • (2003) Int. Rev. Cytol. , vol.229 , pp. 245-286
    • Suetsugu, S.1    Takenawa, T.2
  • 83
    • 1442290184 scopus 로고    scopus 로고
    • EGF-dependent regulation of Cdc42 is mediated by the Src tyrosine kinase
    • Tu, S., Wu, W. J., Wang, J., and Cerione, R. A. (2003). EGF-dependent regulation of Cdc42 is mediated by the Src tyrosine kinase. J. Biol. Chem. 278, 49293-49300.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49293-49300
    • Tu, S.1    Wu, W.J.2    Wang, J.3    Cerione, R.A.4
  • 85
    • 7244250167 scopus 로고    scopus 로고
    • Activation of Rac1 by paxillin-Crk-DOCK180 signaling complex is antagonized by Rap1 in migrating NBT-II cells
    • Valles, A. M., Beuvin, M., and Boyer, B. (2004). Activation of Rac1 by paxillin-Crk-DOCK180 signaling complex is antagonized by Rap1 in migrating NBT-II cells. J. Biol. Chem. 279, 44490-44496.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44490-44496
    • Valles, A.M.1    Beuvin, M.2    Boyer, B.3
  • 87
    • 0034607876 scopus 로고    scopus 로고
    • GIT proteins, a novel family of phosphatidylinositol 3,4, 5-trisphosphate-stimulated GTPase-activating proteins for ARF6
    • Vitale, N., Patton, W. A., Moss, J., Vaughan, M., Lefkowitz, R.J., and Premont, R. T. (2000). GIT proteins, A novel family of phosphatidylinositol 3,4, 5-trisphosphate-stimulated GTPase-activating proteins for ARF6. J. Biol. Chem. 275, 13901-13906.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13901-13906
    • Vitale, N.1    Patton, W.A.2    Moss, J.3    Vaughan, M.4    Lefkowitz, R.J.5    Premont, R.T.6
  • 88
    • 0033166866 scopus 로고    scopus 로고
    • Angiotensin II stimulates serine phosphorylation of the adaptor protein Nck: Physical association with the serine/threonine kinases Pak1 and casein kinase I
    • Voisin, L., Larose, L., and Meloche, S. (1999). Angiotensin II stimulates serine phosphorylation of the adaptor protein Nck: physical association with the serine/threonine kinases Pak1 and casein kinase I. Biochem. J. 341, 217-223.
    • (1999) Biochem. J. , vol.341 , pp. 217-223
    • Voisin, L.1    Larose, L.2    Meloche, S.3
  • 90
    • 0035833251 scopus 로고    scopus 로고
    • The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL)
    • West, K. A., Zhang, H., Brown, M. C., Nikolopoulos, S. N., Riedy, M. C., Horwitz, A. F., and Turner, C. E. (2001). The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL). J. Cell Biol. 154, 161-176.
    • (2001) J. Cell Biol. , vol.154 , pp. 161-176
    • West, K.A.1    Zhang, H.2    Brown, M.C.3    Nikolopoulos, S.N.4    Riedy, M.C.5    Horwitz, A.F.6    Turner, C.E.7
  • 91
    • 0346095319 scopus 로고    scopus 로고
    • GIT1 functions as a scaffold for MEK1-extracellular signal-regulated kinase 1 and 2 activation by angiotensin II and EGF
    • Yin, G., Haendeler, J., Yan, C., and Berk, B. C. (2004). GIT1 functions as a scaffold for MEK1-extracellular signal-regulated kinase 1 and 2 activation by angiotensin II and EGF. Mol. Cell. Biol. 24, 875-885.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 875-885
    • Yin, G.1    Haendeler, J.2    Yan, C.3    Berk, B.C.4
  • 93
    • 0034082699 scopus 로고    scopus 로고
    • Interaction between PAK and Nck: A template for Nck targets and role of PAK autophosphorylation
    • Zhao, Z. S., Manser, E., and Lim, L. (2000a). Interaction between PAK and Nck: a template for Nck targets and role of PAK autophosphorylation. Mol. Cell. Biol. 20, 3906-3917.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3906-3917
    • Zhao, Z.S.1    Manser, E.2    Lim, L.3
  • 94
    • 0033843129 scopus 로고    scopus 로고
    • Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly
    • Zhao, Z. S., Manser, E., Loo, T. H., and Lim, L. (2000b). Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly. Mol. Cell. Biol. 20, 6354-6363.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6354-6363
    • Zhao, Z.S.1    Manser, E.2    Loo, T.H.3    Lim, L.4
  • 95
    • 0242664130 scopus 로고    scopus 로고
    • Akt phosphorylation of serine 21 on Pak1 modulates Nck binding and cell migration
    • Zhou, G. L., Zhuo, Y., King, C. C., Fryer, B. H., Bokoch, G. M., and Field, J. (2003). Akt phosphorylation of serine 21 on Pak1 modulates Nck binding and cell migration. Mol. Cell. Biol. 23, 8058-8069.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8058-8069
    • Zhou, G.L.1    Zhuo, Y.2    King, C.C.3    Fryer, B.H.4    Bokoch, G.M.5    Field, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.