메뉴 건너뛰기




Volumn 126, Issue 8, 2013, Pages 1820-1831

PTP1B promotes focal complex maturation, lamellar persistence and directional migration

Author keywords

Adhesion; FAK; Migration; PTP1B; Src

Indexed keywords

ALPHA ACTININ; GUANOSINE TRIPHOSPHATASE; INTEGRIN; PAXILLIN; PROTEIN KINASE P60; PROTEIN TYROSINE PHOSPHATASE 1B; RAC1 PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 84878001153     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.118828     Document Type: Article
Times cited : (22)

References (83)
  • 1
    • 33846259264 scopus 로고    scopus 로고
    • Direct interaction between ER membrane-bound PTP1B and its plasma membrane-anchored targets
    • Anderie, I., Schulz, I. and Schmid, A. (2007). Direct interaction between ER membrane-bound PTP1B and its plasma membrane-anchored targets. Cell. Signal. 19, 582-592.
    • (2007) Cell. Signal. , vol.19 , pp. 582-592
    • Anderie, I.1    Schulz, I.2    Schmid, A.3
  • 2
    • 0029130199 scopus 로고
    • Osmotic loading of neutralizing antibodies demonstrates a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway
    • Ahmad, F., Li, P. M., Meyerovitch, J. and Goldstein, B. J. (1995). Osmotic loading of neutralizing antibodies demonstrates a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway. J. Biol. Chem. 270, 20503-20508.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20503-20508
    • Ahmad, F.1    Li, P.M.2    Meyerovitch, J.3    Goldstein, B.J.4
  • 4
    • 0032476646 scopus 로고    scopus 로고
    • Impaired integrin-mediated adhesion and signaling in fibroblasts expressing a dominant-negative mutant PTP1B
    • Arregui, C. O., Balsamo, J. and Lilien, J. (1998). Impaired integrin-mediated adhesion and signaling in fibroblasts expressing a dominant-negative mutant PTP1B. J. Cell Biol. 143, 861-873.
    • (1998) J. Cell Biol. , vol.143 , pp. 861-873
    • Arregui, C.O.1    Balsamo, J.2    Lilien, J.3
  • 5
    • 0034659526 scopus 로고    scopus 로고
    • Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism
    • Arthur, W. T., Petch, L. A. and Burridge, K. (2000). Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism. Curr. Biol. 10, 719-722.
    • (2000) Curr. Biol. , vol.10 , pp. 719-722
    • Arthur, W.T.1    Petch, L.A.2    Burridge, K.3
  • 6
    • 0032547736 scopus 로고    scopus 로고
    • The nonreceptor protein tyrosine phosphatase PTP1B binds to the cytoplasmic domain of N-cadherin and regulates the cadherin-actin linkage
    • Balsamo, J., Arregui, C., Leung, T. and Lilien, J. (1998). The nonreceptor protein tyrosine phosphatase PTP1B binds to the cytoplasmic domain of N-cadherin and regulates the cadherin-actin linkage. J. Cell Biol. 143, 523-532.
    • (1998) J. Cell Biol. , vol.143 , pp. 523-532
    • Balsamo, J.1    Arregui, C.2    Leung, T.3    Lilien, J.4
  • 7
    • 0034644537 scopus 로고    scopus 로고
    • Ras and Rho GTPases: a family reunion
    • Bar-Sagi, D. and Hall, A. (2000). Ras and Rho GTPases: a family reunion. Cell 103, 227-238.
    • (2000) Cell , vol.103 , pp. 227-238
    • Bar-Sagi, D.1    Hall, A.2
  • 8
    • 0029166094 scopus 로고
    • Characterization of tyrosine phosphorylation of paxillin in vitro by focal adhesion kinase
    • Bellis, S. L., Miller, J. T. and Turner, C. E. (1995). Characterization of tyrosine phosphorylation of paxillin in vitro by focal adhesion kinase. J. Biol. Chem. 270, 17437-17441.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17437-17441
    • Bellis, S.L.1    Miller, J.T.2    Turner, C.E.3
  • 9
    • 0034731372 scopus 로고    scopus 로고
    • Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines
    • Bjorge, J. D., Pang, A. and Fujita, D. J. (2000). Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines. J. Biol. Chem. 275, 41439-41446.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41439-41446
    • Bjorge, J.D.1    Pang, A.2    Fujita, D.J.3
  • 10
    • 0037367940 scopus 로고    scopus 로고
    • Dynamics of the interaction between the insulin receptor and protein tyrosine-phosphatase 1B in living cells
    • Boute, N., Boubekeur, S., Lacasa, D. and Issad, T. (2003). Dynamics of the interaction between the insulin receptor and protein tyrosine-phosphatase 1B in living cells. EMBO Rep. 4, 313-319.
    • (2003) EMBO Rep , vol.4 , pp. 313-319
    • Boute, N.1    Boubekeur, S.2    Lacasa, D.3    Issad, T.4
  • 11
    • 13944282937 scopus 로고    scopus 로고
    • Identification of Src-specific phosphorylation site on focal adhesion kinase: dissection of the role of Src SH2 and catalytic functions and their consequences for tumor cell behavior
    • Brunton, V. G., Avizienyte, E., Fincham, V. J., Serrels, B., Metcalf, C. A., 3rd, Sawyer, T. K. and Frame, M. C. (2005). Identification of Src-specific phosphorylation site on focal adhesion kinase: dissection of the role of Src SH2 and catalytic functions and their consequences for tumor cell behavior. Cancer Res. 65, 1335-1342.
    • (2005) Cancer Res. , vol.65 , pp. 1335-1342
    • Brunton, V.G.1    Avizienyte, E.2    Fincham, V.J.3    Serrels, B.4    Metcalf, C.A.5    Sawyer, T.K.6    Frame, M.C.7
  • 12
    • 0036121371 scopus 로고    scopus 로고
    • Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts
    • Buckley, D. A., Cheng, A., Kiely, P. A., Tremblay, M. L. and O'Connor, R. (2002). Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts. Mol. Cell. Biol. 22, 1998-2010.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1998-2010
    • Buckley, D.A.1    Cheng, A.2    Kiely, P.A.3    Tremblay, M.L.4    O'Connor, R.5
  • 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
    • 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
  • 15
    • 34147098381 scopus 로고    scopus 로고
    • Cell spreading and focal adhesion dynamics are regulated by spacing of integrin ligands
    • Cavalcanti-Adam, E. A., Volberg, T., Micoulet, A., Kessler, H., Geiger, B. and Spatz, J. P. (2007). Cell spreading and focal adhesion dynamics are regulated by spacing of integrin ligands. Biophys. J. 92, 2964-2974.
    • (2007) Biophys. J. , vol.92 , pp. 2964-2974
    • Cavalcanti-Adam, E.A.1    Volberg, T.2    Micoulet, A.3    Kessler, H.4    Geiger, B.5    Spatz, J.P.6
  • 16
    • 0035854692 scopus 로고    scopus 로고
    • Attenuation of adhesion-dependent signaling and cell spreading in transformed fibroblasts lacking protein tyrosine phosphatase-1B
    • Cheng, A., Bal, G. S., Kennedy, B. P. and Tremblay, M. L. (2001). Attenuation of adhesion-dependent signaling and cell spreading in transformed fibroblasts lacking protein tyrosine phosphatase-1B. J. Biol. Chem. 276, 25848-25855.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25848-25855
    • Cheng, A.1    Bal, G.S.2    Kennedy, B.P.3    Tremblay, M.L.4
  • 17
    • 51049104617 scopus 로고    scopus 로고
    • Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • Choi, C. K., Vicente-Manzanares, M., Zareno, J., Whitmore, L. A., Mogilner, A. and Horwitz, A. R. (2008). Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner. Nat. Cell Biol. 10, 1039-1050.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1039-1050
    • Choi, C.K.1    Vicente-Manzanares, M.2    Zareno, J.3    Whitmore, L.A.4    Mogilner, A.5    Horwitz, A.R.6
  • 18
    • 0037164867 scopus 로고    scopus 로고
    • The fibronectin-binding integrins alpha5beta1 and alphavbeta3 differentially modulate RhoA-GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis
    • Danen, E. H., Sonneveld, P., Brakebusch, C., Fassler, R. and Sonnenberg, A. (2002). The fibronectin-binding integrins alpha5beta1 and alphavbeta3 differentially modulate RhoA-GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis. J. Cell Biol. 159, 1071-1086.
    • (2002) J. Cell Biol. , vol.159 , pp. 1071-1086
    • Danen, E.H.1    Sonneveld, P.2    Brakebusch, C.3    Fassler, R.4    Sonnenberg, A.5
  • 19
    • 0034595381 scopus 로고    scopus 로고
    • Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK
    • del Pozo, M. A., Price, L. S., Alderson, N. B., Ren, X. D. and Schwartz, M. A. (2000). Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK. EMBO J. 19, 2008-2014.
    • (2000) EMBO J. , vol.19 , pp. 2008-2014
    • del Pozo, M.A.1    Price, L.S.2    Alderson, N.B.3    Ren, X.D.4    Schwartz, M.A.5
  • 20
    • 1242296879 scopus 로고    scopus 로고
    • The role of protein tyrosine phosphatase 1B in Ras signaling
    • Dube, N., Cheng, A. and Tremblay, M. L. (2004). The role of protein tyrosine phosphatase 1B in Ras signaling. Proc. Natl. Acad. Sci. USA 101, 1834-1839.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1834-1839
    • Dube, N.1    Cheng, A.2    Tremblay, M.L.3
  • 21
    • 0020685571 scopus 로고
    • Characterising a kinesis response: time averaged measures of cell speed and directional persistence
    • Dunn, G. A. (1983). Characterising a kinesis response: time averaged measures of cell speed and directional persistence. Agents Actions Suppl. 12, 14-33.
    • (1983) Agents Actions Suppl. , vol.12 , pp. 14-33
    • Dunn, G.A.1
  • 22
    • 77649274212 scopus 로고    scopus 로고
    • Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor interaction
    • Eden, E. R., White, I. J., Tsapara, A. and Futter, C. E. (2010). Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor interaction. Nat. Cell Biol. 12, 267-272.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 267-272
    • Eden, E.R.1    White, I.J.2    Tsapara, A.3    Futter, C.E.4
  • 24
    • 0031055324 scopus 로고    scopus 로고
    • Development of ''substrate-trapping'' mutants to identify physiological substrates of protein tyrosine phosphatases
    • Flint, A. J., Tiganis, T., Barford, D. and Tonks, N. K. (1997). Development of ''substrate-trapping'' mutants to identify physiological substrates of protein tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 94, 1680-1685.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1680-1685
    • Flint, A.J.1    Tiganis, T.2    Barford, D.3    Tonks, N.K.4
  • 25
    • 1642575210 scopus 로고    scopus 로고
    • Regulation and localization of CAS substrate domain tyrosine phosphorylation
    • Fonseca, P. M., Shin, N. Y., Brabek, J., Ryzhova, L., Wu, J. and Hanks, S. K. (2004). Regulation and localization of CAS substrate domain tyrosine phosphorylation. Cell. Signal. 16, 621-629.
    • (2004) Cell. Signal. , vol.16 , pp. 621-629
    • Fonseca, P.M.1    Shin, N.Y.2    Brabek, J.3    Ryzhova, L.4    Wu, J.5    Hanks, S.K.6
  • 27
    • 0026584285 scopus 로고
    • The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
    • Frangioni, J. V., Beahm, P. H., Shifrin, V., Jost, C. A. and Neel, B. G. (1992). The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence. Cell 68, 545-560.
    • (1992) Cell , vol.68 , pp. 545-560
    • Frangioni, J.V.1    Beahm, P.H.2    Shifrin, V.3    Jost, C.A.4    Neel, B.G.5
  • 28
    • 65249117751 scopus 로고    scopus 로고
    • Microtubule and cell contact dependency of ERbound PTP1B localization in growth cones
    • Fuentes, F. and Arregui, C. O. (2009). Microtubule and cell contact dependency of ERbound PTP1B localization in growth cones. Mol. Biol. Cell 20, 1878-1889.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1878-1889
    • Fuentes, F.1    Arregui, C.O.2
  • 29
    • 0014862141 scopus 로고
    • The locomotion of mouse fibroblasts in tissue culture
    • Gail, M. H. and Boone, C. W. (1970). The locomotion of mouse fibroblasts in tissue culture. Biophys. J. 10, 980-993.
    • (1970) Biophys. J. , vol.10 , pp. 980-993
    • Gail, M.H.1    Boone, C.W.2
  • 30
    • 0029826289 scopus 로고    scopus 로고
    • Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST
    • Garton, A. J., Flint, A. J. and Tonks, N. K. (1996). Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST. Mol. Cell. Biol. 16, 6408-6418.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6408-6418
    • Garton, A.J.1    Flint, A.J.2    Tonks, N.K.3
  • 32
    • 0033606767 scopus 로고    scopus 로고
    • Shc and FAK differentially regulate cell motility and directionality modulated by PTEN
    • Gu, J., Tamura, M., Pankov, R., Danen, E. H., Takino, T., Matsumoto, K. and Yamada, K. M. (1999). Shc and FAK differentially regulate cell motility and directionality modulated by PTEN. J. Cell Biol. 146, 389-403.
    • (1999) J. Cell Biol. , vol.146 , pp. 389-403
    • Gu, J.1    Tamura, M.2    Pankov, R.3    Danen, E.H.4    Takino, T.5    Matsumoto, K.6    Yamada, K.M.7
  • 33
    • 0025945823 scopus 로고
    • Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate
    • Guan, K. L. and Dixon, J. E. (1991). Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate. J. Biol. Chem. 266, 17026-17030.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17026-17030
    • Guan, K.L.1    Dixon, J.E.2
  • 34
    • 33745245989 scopus 로고    scopus 로고
    • Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration
    • Gupton, S. L. and Waterman-Storer, C. M. (2006). Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration. Cell 125, 1361-1374.
    • (2006) Cell , vol.125 , pp. 1361-1374
    • Gupton, S.L.1    Waterman-Storer, C.M.2
  • 35
    • 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
  • 36
    • 0036500994 scopus 로고    scopus 로고
    • Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum
    • Haj, F. G., Verveer, P. J., Squire, A., Neel, B. G. and Bastiaens, P. I. (2002). Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum. Science 295, 1708-1711.
    • (2002) Science , vol.295 , pp. 1708-1711
    • Haj, F.G.1    Verveer, P.J.2    Squire, A.3    Neel, B.G.4    Bastiaens, P.I.5
  • 38
    • 21244491489 scopus 로고    scopus 로고
    • Directional persistence of EGF-induced cell migration is associated with stabilization of lamellipodial protrusions
    • Harms, B. D., Bassi, G. M., Horwitz, A. R. and Lauffenburger, D. A. (2005). Directional persistence of EGF-induced cell migration is associated with stabilization of lamellipodial protrusions. Biophys. J. 88, 1479-1488.
    • (2005) Biophys. J. , vol.88 , pp. 1479-1488
    • Harms, B.D.1    Bassi, G.M.2    Horwitz, A.R.3    Lauffenburger, D.A.4
  • 39
    • 0029666251 scopus 로고    scopus 로고
    • p130Cas, a substrate associated with v-Src and v-Crk, localizes to focal adhesions and binds to focal adhesion kinase
    • Harte, M. T., Hildebrand, J. D., Burnham, M. R., Bouton, A. H. and Parsons, J. T. (1996). p130Cas, a substrate associated with v-Src and v-Crk, localizes to focal adhesions and binds to focal adhesion kinase. J. Biol. Chem. 271, 13649-13655.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13649-13655
    • Harte, M.T.1    Hildebrand, J.D.2    Burnham, M.R.3    Bouton, A.H.4    Parsons, J.T.5
  • 40
    • 33646800165 scopus 로고    scopus 로고
    • ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
    • Hernandez, M. V., Sala, M. G., Balsamo, J., Lilien, J. and Arregui, C. O. (2006). ER-bound PTP1B is targeted to newly forming cell-matrix adhesions. J. Cell Sci. 119, 1233-1243.
    • (2006) J. Cell Sci. , vol.119 , pp. 1233-1243
    • Hernandez, M.V.1    Sala, M.G.2    Balsamo, J.3    Lilien, J.4    Arregui, C.O.5
  • 41
    • 77950890187 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase PTP1B is required for efficient delivery of N-cadherin to the cell surface
    • Hernandez, M. V., Wehrendt, D. P. and Arregui, C. O. (2010). The protein tyrosine phosphatase PTP1B is required for efficient delivery of N-cadherin to the cell surface. Mol. Biol. Cell 21, 1387-1397.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1387-1397
    • Hernandez, M.V.1    Wehrendt, D.P.2    Arregui, C.O.3
  • 42
    • 53349090308 scopus 로고    scopus 로고
    • Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner
    • Hirata, H., Tatsumi, H. and Sokabe, M. (2008). Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner. J. Cell Sci. 121, 2795-2804.
    • (2008) J. Cell Sci. , vol.121 , pp. 2795-2804
    • Hirata, H.1    Tatsumi, H.2    Sokabe, M.3
  • 43
    • 17344362766 scopus 로고    scopus 로고
    • Cardiovascular anomaly, impaired actin bundling and resistance to Src-induced transformation in mice lacking p130Cas
    • Honda, H., Oda, H., Nakamoto, T., Honda, Z., Sakai, R., Suzuki, T., Saito, T., Nakamura, K., Nakao, K., Ishikawa, T. 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    Oda, H.2    Nakamoto, T.3    Honda, Z.4    Sakai, R.5    Suzuki, T.6    Saito, T.7    Nakamura, K.8    Nakao, K.9    Ishikawa, T.10
  • 44
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C. D., Chinenov, Y. and Kerppola, T. K. (2002). Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9, 789-798.
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 45
    • 0036724188 scopus 로고    scopus 로고
    • Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells
    • Itoh, R. E., Kurokawa, K., Ohba, Y., Yoshizaki, H., Mochizuki, N. and Matsuda, M. (2002). Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells. Mol. Cell. Biol. 22, 6582-6591.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6582-6591
    • Itoh, R.E.1    Kurokawa, K.2    Ohba, Y.3    Yoshizaki, H.4    Mochizuki, N.5    Matsuda, M.6
  • 46
    • 0035800777 scopus 로고    scopus 로고
    • The cytoskeletal/non-muscle isoform of alphaactinin is phosphorylated on its actin-binding domain by the focal adhesion kinase
    • Izaguirre, G., Aguirre, L., Hu, Y. P., Lee, H. Y., Schlaepfer, D. D., Aneskievich, B. J. and Haimovich, B. (2001). The cytoskeletal/non-muscle isoform of alphaactinin is phosphorylated on its actin-binding domain by the focal adhesion kinase. J. Biol. Chem. 276, 28676-28685.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28676-28685
    • Izaguirre, G.1    Aguirre, L.2    Hu, Y.P.3    Lee, H.Y.4    Schlaepfer, D.D.5    Aneskievich, B.J.6    Haimovich, B.7
  • 47
    • 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
  • 48
    • 0029034939 scopus 로고
    • c-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). 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
  • 49
    • 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
  • 50
    • 0035954424 scopus 로고    scopus 로고
    • Differential dynamics of a 5 integrin, paxillin, and a-actinin during formation and disassembly of adhesions in migrating cells
    • Laukaitis, C. M., Webb, D. J., Donais, K. and Horwitz, A. F. (2001). Differential dynamics of a 5 integrin, paxillin, and a-actinin during formation and disassembly of adhesions in migrating cells. J. Cell Biol. 153, 1427-1440.
    • (2001) J. Cell Biol. , vol.153 , pp. 1427-1440
    • Laukaitis, C.M.1    Webb, D.J.2    Donais, K.3    Horwitz, A.F.4
  • 51
    • 21644440357 scopus 로고    scopus 로고
    • The role of protein-tyrosine phosphatase 1B in integrin signaling
    • Liang, F., Lee, S. Y., Liang, J., Lawrence, D. S. and Zhang, Z. Y. (2005). The role of protein-tyrosine phosphatase 1B in integrin signaling. J. Biol. Chem. 280, 24857-24863.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24857-24863
    • Liang, F.1    Lee, S.Y.2    Liang, J.3    Lawrence, D.S.4    Zhang, Z.Y.5
  • 52
    • 38349058006 scopus 로고    scopus 로고
    • PyK2 and FAK connections to p190Rho guanine nucleotide exchange factor regulate RhoA activity, focal adhesion formation, and cell motility
    • Lim, Y., Lim, S. T., Tomar, A., Gardel, M., Bernard-Trifilo, J. A., Chen, X. L., Uryu, S. A., Canete-Soler, R., Zhai, J., Lin, H. et al. (2008). PyK2 and FAK connections to p190Rho guanine nucleotide exchange factor regulate RhoA activity, focal adhesion formation, and cell motility. J. Cell Biol. 180, 187-203.
    • (2008) J. Cell Biol. , vol.180 , pp. 187-203
    • Lim, Y.1    Lim, S.T.2    Tomar, A.3    Gardel, M.4    Bernard-Trifilo, J.A.5    Chen, X.L.6    Uryu, S.A.7    Canete-Soler, R.8    Zhai, J.9    Lin, H.10
  • 54
    • 0029856493 scopus 로고    scopus 로고
    • Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas)
    • Liu, F., Hill, D. E. and Chernoff, J. (1996). Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas). J. Biol. Chem. 271, 31290-31295.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31290-31295
    • Liu, F.1    Hill, D.E.2    Chernoff, J.3
  • 55
    • 33746630192 scopus 로고    scopus 로고
    • Cell_motility: a cross-platform, open source application for the study of cell motion paths
    • Martens, L., Monsieur, G., Ampe, C., Gevaert, K. and Vandekerckhove, J. (2006). Cell_motility: a cross-platform, open source application for the study of cell motion paths. BMC Bioinformatics 7, 289-294.
    • (2006) BMC Bioinformatics , vol.7 , pp. 289-294
    • Martens, L.1    Monsieur, G.2    Ampe, C.3    Gevaert, K.4    Vandekerckhove, J.5
  • 56
    • 84862176440 scopus 로고    scopus 로고
    • ER-bound protein tyrosine phosphatase PTP1B interacts with Src at the plasma membrane/substrate interface
    • Monteleone, M. C., Gonzalez Wusener, A. E., Burdisso, J. E., Conde, C., Caceres, A. and Arregui, C. O. (2012). ER-bound protein tyrosine phosphatase PTP1B interacts with Src at the plasma membrane/substrate interface. PLoS One 7, e38948.
    • (2012) PLoS One , vol.7
    • Monteleone, M.C.1    Gonzalez Wusener, A.E.2    Burdisso, J.E.3    Conde, C.4    Caceres, A.5    Arregui, C.O.6
  • 57
    • 27744494934 scopus 로고    scopus 로고
    • Monitoring spatio-temporal regulation of Ras and Rho GTPase with GFP-based FRET probes
    • Nakamura, T., Aoki, K. and Matsuda, M. (2005). Monitoring spatio-temporal regulation of Ras and Rho GTPase with GFP-based FRET probes. Methods 37, 146- 153.
    • (2005) Methods , vol.37 , pp. 146-153
    • Nakamura, T.1    Aoki, K.2    Matsuda, M.3
  • 59
    • 0023746235 scopus 로고
    • Models of dispersal in biological systems
    • Othmer, H. G., Dunbar, S. R. and Alt, W. (1988). Models of dispersal in biological systems. J. Math. Biol. 26, 263-298.
    • (1988) J. Math. Biol. , vol.26 , pp. 263-298
    • Othmer, H.G.1    Dunbar, S.R.2    Alt, W.3
  • 60
    • 0035863369 scopus 로고    scopus 로고
    • PTP1B regulates neurite extension mediated by cell-cell and cell-matrix adhesion molecules
    • Pathre, P., Arregui, C., Wampler, T., Kue, I., Leung, T. C., Lilien, J. and Balsamo, J. (2001). PTP1B regulates neurite extension mediated by cell-cell and cell-matrix adhesion molecules. J. Neurosci. Res. 63, 143-150.
    • (2001) J. Neurosci. Res. , vol.63 , pp. 143-150
    • Pathre, P.1    Arregui, C.2    Wampler, T.3    Kue, I.4    Leung, T.C.5    Lilien, J.6    Balsamo, J.7
  • 61
    • 77953145912 scopus 로고    scopus 로고
    • Spatio-temporal Rho GTPase signaling - where are we now? J
    • Pertz, O. (2010). Spatio-temporal Rho GTPase signaling - where are we now? J. Cell Sci. 123, 1841-1850.
    • (2010) Cell Sci. , vol.123 , pp. 1841-1850
    • Pertz, O.1
  • 62
    • 0036228954 scopus 로고    scopus 로고
    • Dissecting the link between stress fibers and focal adhesions by CALI with EGFP fusion proteins
    • Rajfur, Z., Roy, P., Otey, C., Romer, L. and Jacobson, K. (2002). Dissecting the link between stress fibers and focal adhesions by CALI with EGFP fusion proteins. Nature Cell Biol. 4, 286-293.
    • (2002) Nature Cell Biol , vol.4 , pp. 286-293
    • Rajfur, Z.1    Roy, P.2    Otey, C.3    Romer, L.4    Jacobson, K.5
  • 63
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTPbinding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X. D., Kiosses, W. B. and Schwartz, M. A. (1999). Regulation of the small GTPbinding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18, 578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 64
    • 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
  • 65
    • 27744551009 scopus 로고    scopus 로고
    • Structure and regulation of Kit protein-tyrosine kinase-the stem cell factor receptor
    • Roskoski, R., Jr (2005). Structure and regulation of Kit protein-tyrosine kinase-the stem cell factor receptor. Biochem. Biophys. Res. Commun. 338, 1307-1315.
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 1307-1315
    • Roskoski, R.1
  • 66
    • 0030889320 scopus 로고    scopus 로고
    • Characterization of the kinase activity essential for tyrosine phosphorylation of p130Cas in fibroblasts
    • Sakai, R., Nakamoto, T., Ozawa, K., Aizawa, S. and Hirai, H. (1997). Characterization of the kinase activity essential for tyrosine phosphorylation of p130Cas in fibroblasts. Oncogene 14, 1419-1426.
    • (1997) Oncogene , vol.14 , pp. 1419-1426
    • Sakai, R.1    Nakamoto, T.2    Ozawa, K.3    Aizawa, S.4    Hirai, H.5
  • 67
    • 80053301137 scopus 로고    scopus 로고
    • Spatial and temporal regulation of integrin signalling during cell migration
    • Scales, T. M. and Parsons, M. (2011). Spatial and temporal regulation of integrin signalling during cell migration. Curr. Opin. Cell Biol. 23, 562-568.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 562-568
    • Scales, T.M.1    Parsons, M.2
  • 68
    • 0028986116 scopus 로고
    • pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
    • Schaller, M. D. and Parsons, J. T. (1995). pp125FAK-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
  • 69
    • 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
  • 70
    • 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
  • 71
    • 0034256024 scopus 로고    scopus 로고
    • Signaling networks linking integrins and rho family GTPases
    • Schwartz, M. A. and Shattil, S. J. (2000). Signaling networks linking integrins and rho family GTPases. Trends Biochem. Sci. 25, 388-391.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 388-391
    • Schwartz, M.A.1    Shattil, S.J.2
  • 72
    • 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., Urano, T., Fujita, H., Ohashi, Y., Kamiguchi, K., Iwata, S., Hirai, H. and Morimoto, C. (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
  • 75
    • 0025249807 scopus 로고
    • Practical design criteria for a dynamic ratio imaging system
    • Tsien, R. Y. and Harootunian, A. T. (1990). Practical design criteria for a dynamic ratio imaging system. Cell Calcium 11, 93-109.
    • (1990) Cell Calcium , vol.11 , pp. 93-109
    • Tsien, R.Y.1    Harootunian, A.T.2
  • 76
    • 65649089183 scopus 로고    scopus 로고
    • Integrins in cell migration-the actin connection
    • Vicente-Manzanares, M., Choi, C. K. and Horwitz, A. R. (2009). Integrins in cell migration-the actin connection. J. Cell Sci. 122, 199-206.
    • (2009) J. Cell Sci. , vol.122 , pp. 199-206
    • Vicente-Manzanares, M.1    Choi, C.K.2    Horwitz, A.R.3
  • 77
    • 0141865507 scopus 로고    scopus 로고
    • Forcedependent integrin-cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2
    • Von Wichert, G., Haimovich, B., Feng, G. S. and Sheetz, M. P. (2003). Forcedependent integrin-cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2. EMBO J. 22, 5023-5035.
    • (2003) EMBO J. , vol.22 , pp. 5023-5035
    • Von Wichert, G.1    Haimovich, B.2    Feng, G.S.3    Sheetz, M.P.4
  • 79
    • 27544435992 scopus 로고    scopus 로고
    • Mechanical force mobilizes zyxin from focal adhesions to actin filaments and regulates cytoskeletal reinforcement
    • Yoshigi, M., Hoffman, L. M., Jensen, C. C., Yost, H. J. and Beckerle, M. C. (2005). Mechanical force mobilizes zyxin from focal adhesions to actin filaments and regulates cytoskeletal reinforcement. J. Cell Biol. 171, 209-215.
    • (2005) J. Cell Biol. , vol.171 , pp. 209-215
    • Yoshigi, M.1    Hoffman, L.M.2    Jensen, C.C.3    Yost, H.J.4    Beckerle, M.C.5
  • 81
    • 0344465841 scopus 로고    scopus 로고
    • Early molecular events in the assembly of matrix adhesions at the leading edge ofmigrating cells
    • Zaidel-Bar, R., Ballestrem, C., Kam, Z. and Geiger, B. (2003). Early molecular events in the assembly of matrix adhesions at the leading edge ofmigrating cells. J. Cell Sci. 116, 4605-4613.
    • (2003) J. Cell Sci. , vol.116 , pp. 4605-4613
    • Zaidel-Bar, R.1    Ballestrem, C.2    Kam, Z.3    Geiger, B.4
  • 82
    • 33644977113 scopus 로고    scopus 로고
    • Phosphorylated alpha-actinin and protein-tyrosine phosphatase 1B coregulate the disassembly of the focal adhesion kinase x Src complex and promote cell migration
    • Zhang, Z., Lin, S. Y., Neel, B. G. and Haimovich, B. (2006). Phosphorylated alpha-actinin and protein-tyrosine phosphatase 1B coregulate the disassembly of the focal adhesion kinase x Src complex and promote cell migration. J. Biol. Chem. 281, 1746-1754.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1746-1754
    • Zhang, Z.1    Lin, S.Y.2    Neel, B.G.3    Haimovich, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.