메뉴 건너뛰기




Volumn 87, Issue 8-9, 2008, Pages 721-734

The Rsu-1-PINCH1-ILK complex is regulated by Ras activation in tumor cells

Author keywords

Adhesion; Focal adhesion; Integrin linked kinase; Migration; PINCH1; Ras; Rsu 1

Indexed keywords

GUANOSINE TRIPHOSPHATE; INTEGRIN LINKED KINASE; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN PINCH 1; PROTEIN RSU 1; RAC PROTEIN; RAS PROTEIN; RNA; SMALL INTERFERING RNA; TUMOR SUPPRESSOR PROTEIN;

EID: 49249096493     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2008.02.011     Document Type: Article
Times cited : (70)

References (76)
  • 1
    • 0037009371 scopus 로고    scopus 로고
    • Tyrosine 221 in Crk regulates adhesion-dependent membrane localization of Crk and Rac and activation of Rac signaling
    • Abassi Y.A., and Vuori K. Tyrosine 221 in Crk regulates adhesion-dependent membrane localization of Crk and Rac and activation of Rac signaling. EMBO J. 21 (2002) 4571-4582
    • (2002) EMBO J. , vol.21 , pp. 4571-4582
    • Abassi, Y.A.1    Vuori, K.2
  • 2
    • 0141995796 scopus 로고    scopus 로고
    • Integrin-linked kinase expression increases with ovarian tumour grade and is sustained by peritoneal tumour fluid
    • Ahmed N., Riley C., Oliva K., Stutt E., Rice G.E., and Quinn M.A. Integrin-linked kinase expression increases with ovarian tumour grade and is sustained by peritoneal tumour fluid. J. Pathol. 201 (2003) 229-237
    • (2003) J. Pathol. , vol.201 , pp. 229-237
    • Ahmed, N.1    Riley, C.2    Oliva, K.3    Stutt, E.4    Rice, G.E.5    Quinn, M.A.6
  • 5
    • 0033966557 scopus 로고    scopus 로고
    • Nck-interacting Ste20 kinase couples Eph receptors to c-Jun N-terminal kinase and integrin activation
    • Becker E., Huynh-Do U., Holland S., Pawson T., Daniel T.O., and Skolnik E.Y. Nck-interacting Ste20 kinase couples Eph receptors to c-Jun N-terminal kinase and integrin activation. Mol. Cell. Biol. 20 (2000) 1537-1545
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1537-1545
    • Becker, E.1    Huynh-Do, U.2    Holland, S.3    Pawson, T.4    Daniel, T.O.5    Skolnik, E.Y.6
  • 6
    • 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. 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 (2003) 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
  • 7
    • 0033604899 scopus 로고    scopus 로고
    • Identification of Grb4/Nckb, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck
    • Braverman L., and Quilliam L. Identification of Grb4/Nckb, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck. J. Biol. Chem. 274 (1999) 5542-5549
    • (1999) J. Biol. Chem. , vol.274 , pp. 5542-5549
    • Braverman, L.1    Quilliam, L.2
  • 8
    • 0036015163 scopus 로고    scopus 로고
    • The Nck family of adapter proteins: regulators of actin cytoskeleton
    • Buday L., Wunderlich L., and Tamas P. The Nck family of adapter proteins: regulators of actin cytoskeleton. Cell Signal. 14 (2002) 723-731
    • (2002) Cell Signal. , vol.14 , pp. 723-731
    • Buday, L.1    Wunderlich, L.2    Tamas, P.3
  • 9
    • 1642421365 scopus 로고    scopus 로고
    • Actin cytoskeleton remodelling via local inhibition of contractility at discrete microdomains
    • Burgstaller G., and Gimona M. Actin cytoskeleton remodelling via local inhibition of contractility at discrete microdomains. J. Cell Sci. 117 (2004) 223-231
    • (2004) J. Cell Sci. , vol.117 , pp. 223-231
    • Burgstaller, G.1    Gimona, M.2
  • 10
    • 33645220093 scopus 로고    scopus 로고
    • Regulation of CD44 alternative splicing by SRm160 and its potential role in tumor cell invasion
    • Cheng C., and Sharp P.A. Regulation of CD44 alternative splicing by SRm160 and its potential role in tumor cell invasion. Mol. Cell. Biol. 26 (2006) 362-370
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 362-370
    • Cheng, C.1    Sharp, P.A.2
  • 11
    • 33745606029 scopus 로고    scopus 로고
    • A positive feedback loop couples Ras activation and CD44 alternative splicing
    • Cheng C., Yaffe M.B., and Sharp P.A. A positive feedback loop couples Ras activation and CD44 alternative splicing. Genes Dev. 20 (2006) 1715-1720
    • (2006) Genes Dev. , vol.20 , pp. 1715-1720
    • Cheng, C.1    Yaffe, M.B.2    Sharp, P.A.3
  • 12
    • 0036900276 scopus 로고    scopus 로고
    • Identification of an alternatively spliced RNA for the Ras suppressor RSU-1 in human gliomas
    • Chunduru S., Kawami H., Gullick R., Monacci W.J., Dougherty G., and Cutler M.L. Identification of an alternatively spliced RNA for the Ras suppressor RSU-1 in human gliomas. J. Neurooncol. 60 (2002) 201-211
    • (2002) J. Neurooncol. , vol.60 , pp. 201-211
    • Chunduru, S.1    Kawami, H.2    Gullick, R.3    Monacci, W.J.4    Dougherty, G.5    Cutler, M.L.6
  • 13
    • 0038409304 scopus 로고    scopus 로고
    • Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes
    • Clark K.A., McGrail M., and Beckerle M.C. Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes. Development 130 (2003) 2611-2621
    • (2003) Development , vol.130 , pp. 2611-2621
    • Clark, K.A.1    McGrail, M.2    Beckerle, M.C.3
  • 14
    • 0026658729 scopus 로고
    • Isolation of rsp-1, a novel cDNA capable of suppressing v-ras
    • Cutler M., Bassin R., Zanoni L., and Talbot N. Isolation of rsp-1, a novel cDNA capable of suppressing v-ras. Mol. Cell. Biol. 12 (1992) 3750-3756
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3750-3756
    • Cutler, M.1    Bassin, R.2    Zanoni, L.3    Talbot, N.4
  • 15
    • 0141891463 scopus 로고    scopus 로고
    • Increased expression of integrin-linked kinase is correlated with melanoma progression and poor patient survival
    • Dai D.L., Makretsov N., Campos E.I., Huang C., Zhou Y., Huntsman D., Martinka M., and Li G. Increased expression of integrin-linked kinase is correlated with melanoma progression and poor patient survival. Clin. Cancer Res. 9 (2003) 4409-4414
    • (2003) Clin. Cancer Res. , vol.9 , pp. 4409-4414
    • Dai, D.L.1    Makretsov, N.2    Campos, E.I.3    Huang, C.4    Zhou, Y.5    Huntsman, D.6    Martinka, M.7    Li, G.8
  • 17
    • 0034104592 scopus 로고    scopus 로고
    • Cell-substrate interactions and signaling through ILK
    • Dedhar S. Cell-substrate interactions and signaling through ILK. Curr. Opin. Cell Biol. 12 (2000) 250-256
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 250-256
    • Dedhar, S.1
  • 18
    • 18844394310 scopus 로고    scopus 로고
    • The Ras suppressor Rsu-1 binds to the LIM 5 domain of the adaptor protein PINCH1 and participates in adhesion-related functions
    • Dougherty G.W., Chopp T., Qi S.M., and Cutler M.L. The Ras suppressor Rsu-1 binds to the LIM 5 domain of the adaptor protein PINCH1 and participates in adhesion-related functions. Exp. Cell Res. 306 (2005) 168-179
    • (2005) Exp. Cell Res. , vol.306 , pp. 168-179
    • Dougherty, G.W.1    Chopp, T.2    Qi, S.M.3    Cutler, M.L.4
  • 19
    • 0037085375 scopus 로고    scopus 로고
    • Regulation of the Cool/Pix proteins: key binding partners of the Cdc42/Rac targets, the p21-activated kinases
    • Feng Q., Albeck J.G., Cerione R.A., and Yang W. Regulation of the Cool/Pix proteins: key binding partners of the Cdc42/Rac targets, the p21-activated kinases. J. Biol. Chem. 277 (2002) 5644-5650
    • (2002) J. Biol. Chem. , vol.277 , pp. 5644-5650
    • Feng, Q.1    Albeck, J.G.2    Cerione, R.A.3    Yang, W.4
  • 20
    • 26944439126 scopus 로고    scopus 로고
    • Integrin-linked kinase activity regulates Rac- and Cdc42-mediated actin cytoskeleton reorganization via alpha-PIX
    • Filipenko N.R., Attwell S., Roskelley C., and Dedhar S. Integrin-linked kinase activity regulates Rac- and Cdc42-mediated actin cytoskeleton reorganization via alpha-PIX. Oncogene 24 (2005) 5837-5849
    • (2005) Oncogene , vol.24 , pp. 5837-5849
    • Filipenko, N.R.1    Attwell, S.2    Roskelley, C.3    Dedhar, S.4
  • 21
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch S.M., and Francis H. Disruption of epithelial cell-matrix interactions induces apoptosis. J. Cell Biol. 124 (1994) 619-626
    • (1994) J. Cell Biol. , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 22
    • 0141613755 scopus 로고    scopus 로고
    • The C-terminal end of R-Ras contains a focal adhesion targeting signal
    • Furuhjelm J., and Peranen J. The C-terminal end of R-Ras contains a focal adhesion targeting signal. J. Cell Sci. 116 (2003) 3729-3738
    • (2003) J. Cell Sci. , vol.116 , pp. 3729-3738
    • Furuhjelm, J.1    Peranen, J.2
  • 23
    • 33749411636 scopus 로고    scopus 로고
    • EGF-induced activation of Akt results in mTOR-dependent p70S6 kinase phosphorylation and inhibition of HC11 cell lactogenic differentiation
    • Galbaugh T., Cerrito M.G., Jose C.C., and Cutler M.L. EGF-induced activation of Akt results in mTOR-dependent p70S6 kinase phosphorylation and inhibition of HC11 cell lactogenic differentiation. BMC Cell Biol. 7 (2006) 34
    • (2006) BMC Cell Biol. , vol.7 , pp. 34
    • Galbaugh, T.1    Cerrito, M.G.2    Jose, C.C.3    Cutler, M.L.4
  • 24
    • 11144284670 scopus 로고    scopus 로고
    • Stromal staining for PINCH is an independent prognostic indicator in colorectal cancer
    • Gao J., Arbman G., Rearden A., and Sun X.F. Stromal staining for PINCH is an independent prognostic indicator in colorectal cancer. Neoplasia 6 (2004) 796-801
    • (2004) Neoplasia , vol.6 , pp. 796-801
    • Gao, J.1    Arbman, G.2    Rearden, A.3    Sun, X.F.4
  • 27
    • 0029963547 scopus 로고    scopus 로고
    • A Drosophila homolog of Rac- and cdc42-activated serine/threonine kinase Pak is a potential focal adhesion and focal complex protein that co-localizes with dynamic actin structures
    • Harden N., Lee J., Loh H., Ong Y., Tan I., Leung T., Manser E., and Lim L. A Drosophila homolog of Rac- and cdc42-activated serine/threonine kinase Pak is a potential focal adhesion and focal complex protein that co-localizes with dynamic actin structures. Mol. Cell. Biol. 16 (1996) 1896-1908
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1896-1908
    • Harden, N.1    Lee, J.2    Loh, H.3    Ong, Y.4    Tan, I.5    Leung, T.6    Manser, E.7    Lim, L.8
  • 28
    • 0035476836 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells
    • Hauck C.R., Sieg D.J., Hsia D.A., Loftus J.C., Gaarde W.A., Monia B.P., and Schlaepfer D.D. Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells. Cancer Res. 61 (2001) 7079-7090
    • (2001) Cancer Res. , vol.61 , pp. 7079-7090
    • Hauck, C.R.1    Sieg, D.J.2    Hsia, D.A.3    Loftus, J.C.4    Gaarde, W.A.5    Monia, B.P.6    Schlaepfer, D.D.7
  • 30
  • 31
  • 33
    • 0037295608 scopus 로고    scopus 로고
    • Expression of integrin-linked kinase is closely correlated with invasion and metastasis of gastric carcinoma
    • Ito R., Oue N., Zhu X., Yoshida K., Nakayama H., Yokozaki H., and Yasui W. Expression of integrin-linked kinase is closely correlated with invasion and metastasis of gastric carcinoma. Virchows Arch. 442 (2003) 118-123
    • (2003) Virchows Arch. , vol.442 , pp. 118-123
    • Ito, R.1    Oue, N.2    Zhu, X.3    Yoshida, K.4    Nakayama, H.5    Yokozaki, H.6    Yasui, W.7
  • 34
    • 0032480321 scopus 로고    scopus 로고
    • The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R
    • Jones N., and Dumont D.J. The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R. Oncogene 17 (1998) 1097-1108
    • (1998) Oncogene , vol.17 , pp. 1097-1108
    • Jones, N.1    Dumont, D.J.2
  • 35
    • 8444240109 scopus 로고    scopus 로고
    • The LIM domain: from the cytoskeleton to the nucleus
    • Kadrmas J.L., and Beckerle M.C. The LIM domain: from the cytoskeleton to the nucleus. Nat. Rev. Mol. Cell Biol. 5 (2004) 920-931
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 920-931
    • Kadrmas, J.L.1    Beckerle, M.C.2
  • 37
    • 0030913673 scopus 로고    scopus 로고
    • Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway
    • Khwaja A., Rodriguez-Viciana P., Wennstrom S., Warne P.H., and Downward J. Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway. EMBO J. 16 (1997) 2783-2793
    • (1997) EMBO J. , vol.16 , pp. 2783-2793
    • Khwaja, A.1    Rodriguez-Viciana, P.2    Wennstrom, S.3    Warne, P.H.4    Downward, J.5
  • 40
    • 0033913657 scopus 로고    scopus 로고
    • The SH2 and SH3 adapter Nck: a two-gene family and a linker between tyrosine kinases and multiple signaling networks
    • Li W., and She H. The SH2 and SH3 adapter Nck: a two-gene family and a linker between tyrosine kinases and multiple signaling networks. Histol. Histopathol. 15 (2000) 947-955
    • (2000) Histol. Histopathol. , vol.15 , pp. 947-955
    • Li, W.1    She, H.2
  • 41
    • 0033378656 scopus 로고    scopus 로고
    • Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats
    • Li F., Zhang Y., and Wu C. Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats. J. Cell Sci. 112 (1999) 4589-4599
    • (1999) J. Cell Sci. , vol.112 , pp. 4589-4599
    • Li, F.1    Zhang, Y.2    Wu, C.3
  • 42
    • 0035473460 scopus 로고    scopus 로고
    • Nck/Dock: an adapter between cell surface receptors and the actin cytoskeleton
    • Li W., Fan J., and Woodley D.T. Nck/Dock: an adapter between cell surface receptors and the actin cytoskeleton. Oncogene 20 (2001) 6403-6417
    • (2001) Oncogene , vol.20 , pp. 6403-6417
    • Li, W.1    Fan, J.2    Woodley, D.T.3
  • 45
    • 0036537895 scopus 로고    scopus 로고
    • GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration
    • Manabe R., Kovalenko M., Webb D.J., and Horwitz A.R. GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration. J. Cell Sci. 115 (2002) 1497-1510
    • (2002) J. Cell Sci. , vol.115 , pp. 1497-1510
    • Manabe, R.1    Kovalenko, M.2    Webb, D.J.3    Horwitz, A.R.4
  • 47
    • 0038604840 scopus 로고    scopus 로고
    • Characterisation of integrin-linked kinase signalling in sporadic human colon cancer
    • Marotta A., Parhar K., Owen D., Dedhar S., and Salh B. Characterisation of integrin-linked kinase signalling in sporadic human colon cancer. Br. J. Cancer 88 (2003) 1755-1762
    • (2003) Br. J. Cancer , vol.88 , pp. 1755-1762
    • Marotta, A.1    Parhar, K.2    Owen, D.3    Dedhar, S.4    Salh, B.5
  • 48
    • 0029813250 scopus 로고    scopus 로고
    • Increased expression of the Ras suppressor, Rsu-1, enhances Erk-2 activation and inhibits Jun kinase activation
    • Masuelli L., and Cutler M. Increased expression of the Ras suppressor, Rsu-1, enhances Erk-2 activation and inhibits Jun kinase activation. Mol. Cell. Biol. 16 (1996) 5466-5476
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5466-5476
    • Masuelli, L.1    Cutler, M.2
  • 49
    • 12144291549 scopus 로고    scopus 로고
    • The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging factor
    • Mishima W., Suzuki A., Yamaji S., Yoshimi R., Ueda A., Kaneko T., Tanaka J., Miwa Y., Ohno S., and Ishigatsubo Y. The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging factor. Genes Cells 9 (2004) 193-204
    • (2004) Genes Cells , vol.9 , pp. 193-204
    • Mishima, W.1    Suzuki, A.2    Yamaji, S.3    Yoshimi, R.4    Ueda, A.5    Kaneko, T.6    Tanaka, J.7    Miwa, Y.8    Ohno, S.9    Ishigatsubo, Y.10
  • 50
    • 0034739856 scopus 로고    scopus 로고
    • Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion
    • Nikolopoulos S.N., and Turner C.E. Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion. J. Cell Biol. 151 (2000) 1435-1448
    • (2000) J. Cell Biol. , vol.151 , pp. 1435-1448
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 51
    • 0035968234 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions
    • Nikolopoulos S.N., and Turner C.E. Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions. J. Biol. Chem. 276 (2001) 23499-23505
    • (2001) J. Biol. Chem. , vol.276 , pp. 23499-23505
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 52
    • 0037059789 scopus 로고    scopus 로고
    • Molecular dissection of actopaxin-integrin-linked kinase-paxillin interactions and their role in sub-cellular localization
    • Nikolopoulos S., and Turner C. Molecular dissection of actopaxin-integrin-linked kinase-paxillin interactions and their role in sub-cellular localization. J. Biol. Chem. 277 (2002) 1568-1575
    • (2002) J. Biol. Chem. , vol.277 , pp. 1568-1575
    • Nikolopoulos, S.1    Turner, C.2
  • 53
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes C.D., and Hall A. Rho GTPases control polarity, protrusion, and adhesion during cell movement. J. Cell Biol. 144 (1999) 1235-1244
    • (1999) J. Cell Biol. , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 54
    • 0032479975 scopus 로고    scopus 로고
    • PAK promotes morphological changes by acting upstream of Rac
    • Obermeier A., Ahmed S., Manser E., Yen S.C., Hall C., and Lim L. PAK promotes morphological changes by acting upstream of Rac. EMBO J. 17 (1998) 4328-4339
    • (1998) EMBO J. , vol.17 , pp. 4328-4339
    • Obermeier, A.1    Ahmed, S.2    Manser, E.3    Yen, S.C.4    Hall, C.5    Lim, L.6
  • 57
    • 18844363699 scopus 로고    scopus 로고
    • ILK mediates actin filament rearrangements and cell migration and invasion through PI3K/Akt/Rac1 signaling
    • Qian Y., Zhong X., Flynn D.C., Zheng J.Z., Qiao M., Wu C., Dedhar S., Shi X., and Jiang B.H. ILK mediates actin filament rearrangements and cell migration and invasion through PI3K/Akt/Rac1 signaling. Oncogene 24 (2005) 3154-3165
    • (2005) Oncogene , vol.24 , pp. 3154-3165
    • Qian, Y.1    Zhong, X.2    Flynn, D.C.3    Zheng, J.Z.4    Qiao, M.5    Wu, C.6    Dedhar, S.7    Shi, X.8    Jiang, B.H.9
  • 58
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • Raftopoulou M., and Hall A. Cell migration: Rho GTPases lead the way. Dev. Biol. 265 (2004) 23-32
    • (2004) Dev. Biol. , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 59
    • 33745447261 scopus 로고    scopus 로고
    • Requirement of Nck adaptors for actin dynamics and cell migration stimulated by platelet-derived growth factor B
    • Rivera G.M., Antoku S., Gelkop S., Shin N.Y., Hanks S.K., Pawson T., and Mayer B.J. Requirement of Nck adaptors for actin dynamics and cell migration stimulated by platelet-derived growth factor B. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 9536-9541
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 9536-9541
    • Rivera, G.M.1    Antoku, S.2    Gelkop, S.3    Shin, N.Y.4    Hanks, S.K.5    Pawson, T.6    Mayer, B.J.7
  • 60
    • 0034678411 scopus 로고    scopus 로고
    • Activated Ras prevents down regulation of Bcl-X(L) triggered by detachment from the extracellular matrix
    • Rosen K., Rak J., Leung T., Dean N., Kerbel R., and Filmus J. Activated Ras prevents down regulation of Bcl-X(L) triggered by detachment from the extracellular matrix. J. Cell Biol. 149 (2000) 447-456
    • (2000) J. Cell Biol. , vol.149 , pp. 447-456
    • Rosen, K.1    Rak, J.2    Leung, T.3    Dean, N.4    Kerbel, R.5    Filmus, J.6
  • 61
    • 0035884505 scopus 로고    scopus 로고
    • Akt pathway activation converts anaplastic astrocytoma to glioblastoma multiforme in a human astrocyte model of glioma
    • Sonoda Y., Ozawa T., Aldape K.D., Deen D.F., Berger M.S., and Pieper R.O. Akt pathway activation converts anaplastic astrocytoma to glioblastoma multiforme in a human astrocyte model of glioma. Cancer Res. 61 (2001) 6674-6678
    • (2001) Cancer Res. , vol.61 , pp. 6674-6678
    • Sonoda, Y.1    Ozawa, T.2    Aldape, K.D.3    Deen, D.F.4    Berger, M.S.5    Pieper, R.O.6
  • 62
    • 0035392982 scopus 로고    scopus 로고
    • Formation of intracranial tumors by genetically modified human astrocytes defines four pathways critical in the development of human anaplastic astrocytoma
    • Sonoda Y., Ozawa T., Hirose Y., Aldape K.D., McMahon M., Berger M.S., and Pieper R.O. Formation of intracranial tumors by genetically modified human astrocytes defines four pathways critical in the development of human anaplastic astrocytoma. Cancer Res. 61 (2001) 4956-4960
    • (2001) Cancer Res. , vol.61 , pp. 4956-4960
    • Sonoda, Y.1    Ozawa, T.2    Hirose, Y.3    Aldape, K.D.4    McMahon, M.5    Berger, M.S.6    Pieper, R.O.7
  • 63
    • 0036479113 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates inducible nitric oxide synthase and cyclooxygenase-2 expression in an NF-kappa B-dependent manner
    • Tan C., Mui A., and Dedhar S. Integrin-linked kinase regulates inducible nitric oxide synthase and cyclooxygenase-2 expression in an NF-kappa B-dependent manner. J. Biol. Chem. 277 (2002) 3109-3116
    • (2002) J. Biol. Chem. , vol.277 , pp. 3109-3116
    • Tan, C.1    Mui, A.2    Dedhar, S.3
  • 64
    • 0030461098 scopus 로고    scopus 로고
    • Cell cycle-dependent activation of Ras
    • Taylor S., and Shalloway D. Cell cycle-dependent activation of Ras. Curr. Biol. 6 (1996) 1621-1627
    • (1996) Curr. Biol. , vol.6 , pp. 1621-1627
    • Taylor, S.1    Shalloway, D.2
  • 65
    • 0027332009 scopus 로고
    • Human RSU-1 is highly homologous to mouse Rsu-1 and localizes to human chromosome 10
    • Tsuda T., and Cutler M. Human RSU-1 is highly homologous to mouse Rsu-1 and localizes to human chromosome 10. Genomics 18 (1993) 461-462
    • (1993) Genomics , vol.18 , pp. 461-462
    • Tsuda, T.1    Cutler, M.2
  • 66
    • 0029092309 scopus 로고
    • The Ras suppressor RSU-1 localizes to 10p13 and its expression in the U251 glioblastoma cell line correlates with a decrease in growth rate and tumorigenic potential
    • Tsuda T., Marinetti M., Masuelli L., and Cutler M. The Ras suppressor RSU-1 localizes to 10p13 and its expression in the U251 glioblastoma cell line correlates with a decrease in growth rate and tumorigenic potential. Oncogene 11 (1995) 397-403
    • (1995) Oncogene , vol.11 , pp. 397-403
    • Tsuda, T.1    Marinetti, M.2    Masuelli, L.3    Cutler, M.4
  • 67
    • 0031772910 scopus 로고    scopus 로고
    • Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways
    • Tu Y., Li F., and Wu C. Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways. Mol. Biol. Cell 9 (1998) 3367-3382
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3367-3382
    • Tu, Y.1    Li, F.2    Wu, C.3
  • 68
    • 0033020670 scopus 로고    scopus 로고
    • The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells
    • Tu Y., Li F., Goicoechea S., and Wu C. The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells. Mol. Cell. Biol. 19 (1999) 2425-2434
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2425-2434
    • Tu, Y.1    Li, F.2    Goicoechea, S.3    Wu, C.4
  • 69
    • 0035972170 scopus 로고    scopus 로고
    • A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading
    • Tu Y., Huang Y., Zhang Y., Hua Y., and Wu C. A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading. J. Cell Biol. 153 (2001) 585-598
    • (2001) J. Cell Biol. , vol.153 , pp. 585-598
    • Tu, Y.1    Huang, Y.2    Zhang, Y.3    Hua, Y.4    Wu, C.5
  • 70
    • 0038190982 scopus 로고    scopus 로고
    • Cdc42 is a Rho GTPase family member that can mediate insulin signaling to glucose transport in 3T3-L1 adipocytes
    • Usui I., Imamura T., Huang J., Satoh H., and Olefsky J.M. Cdc42 is a Rho GTPase family member that can mediate insulin signaling to glucose transport in 3T3-L1 adipocytes. J. Biol. Chem. 278 (2003) 13765-13774
    • (2003) J. Biol. Chem. , vol.278 , pp. 13765-13774
    • Usui, I.1    Imamura, T.2    Huang, J.3    Satoh, H.4    Olefsky, J.M.5
  • 71
    • 0033919866 scopus 로고    scopus 로고
    • Ectopic expression of Rsu-1 results in elevation of p21CIP and inhibits anchorage-independent growth of MCF7 breast cancer cells
    • Vasaturo F., Dougherty G.W., and Cutler M.L. Ectopic expression of Rsu-1 results in elevation of p21CIP and inhibits anchorage-independent growth of MCF7 breast cancer cells. Breast Cancer Res. Treat. 61 (2000) 69-78
    • (2000) Breast Cancer Res. Treat. , vol.61 , pp. 69-78
    • Vasaturo, F.1    Dougherty, G.W.2    Cutler, M.L.3
  • 72
    • 0037105384 scopus 로고    scopus 로고
    • The signaling adaptor protein PINCH is up-regulated in the stroma of common cancers, at the invasive edges
    • Wang-Rodriguez J., Dreilinger A., Alsharabi G., and Rearden A. The signaling adaptor protein PINCH is up-regulated in the stroma of common cancers, at the invasive edges. Cancer 95 (2002) 1387-1395
    • (2002) Cancer , vol.95 , pp. 1387-1395
    • Wang-Rodriguez, J.1    Dreilinger, A.2    Alsharabi, G.3    Rearden, A.4
  • 74
    • 0037115611 scopus 로고    scopus 로고
    • Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites
    • Zhang Y., Chen K., Tu Y., Vaelyvis A., Yang Y., Qin J., and Wu C. Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites. J. Cell Sci. 115 (2002) 4777-4786
    • (2002) J. Cell Sci. , vol.115 , pp. 4777-4786
    • Zhang, Y.1    Chen, K.2    Tu, Y.3    Vaelyvis, A.4    Yang, Y.5    Qin, J.6    Wu, C.7
  • 75
    • 0037016703 scopus 로고    scopus 로고
    • A critical role of the PINCH-integrin-linked kinase interaction in the regulation of cell shape change and migration
    • Zhang Y., Guo L., Chen K., and Wu C. A critical role of the PINCH-integrin-linked kinase interaction in the regulation of cell shape change and migration. J. Biol. Chem. 277 (2002) 318-326
    • (2002) J. Biol. Chem. , vol.277 , pp. 318-326
    • Zhang, Y.1    Guo, L.2    Chen, K.3    Wu, C.4
  • 76
    • 4744340477 scopus 로고    scopus 로고
    • Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival
    • Zhang Y., Chen K., Tu Y., and Wu C. Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival. J. Biol. Chem. 279 (2004) 41695-41705
    • (2004) J. Biol. Chem. , vol.279 , pp. 41695-41705
    • Zhang, Y.1    Chen, K.2    Tu, Y.3    Wu, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.