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Volumn 72, Issue 9, 2012, Pages 2405-2415

p120RasGAP-mediated activation of c-Src is critical for oncogenic ras to induce tumor invasion

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE;

EID: 84860535263     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-11-3078     Document Type: Article
Times cited : (22)

References (33)
  • 1
    • 33947594129 scopus 로고    scopus 로고
    • Hyperactive Ras in developmental disorders and cancer
    • DOI 10.1038/nrc2109, PII NRC2109
    • Schubbert S, Shannon K, Bollag G. Hyperactive Ras in developmental disorders and cancer. Nat Rev Cancer 2007;7:295-308. (Pubitemid 46480970)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.4 , pp. 295-308
    • Schubbert, S.1    Shannon, K.2    Bollag, G.3
  • 2
    • 13444252631 scopus 로고    scopus 로고
    • GEF means go: Turning on Rho GTPases with guanine nucleotide-exchange factors
    • DOI 10.1038/nrm1587
    • Rossman KL, Der CJ, Sondek J. GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors. Nat Rev Mol Cell Biol 2005;6:167-80. (Pubitemid 40215811)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.2 , pp. 167-180
    • Rossman, K.L.1    Der, C.J.2    Sondek, J.3
  • 3
    • 0037805547 scopus 로고    scopus 로고
    • RAS oncogenes: The first 30 years
    • DOI 10.1038/nrc1097
    • Malumbres M, Barbacid M. RAS oncogenes: the first 30 years. Nat Rev Cancer 2003;3:459-65. (Pubitemid 37328850)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.6 , pp. 459-465
    • Malumbres, M.1    Barbacid, M.2
  • 4
    • 33644864788 scopus 로고    scopus 로고
    • Compartmentalized Ras/MAPK signaling
    • Mor A, Philips MR. Compartmentalized Ras/MAPK signaling. Annu Rev Immunol 2006;24:771-800.
    • (2006) Annu Rev Immunol , vol.24 , pp. 771-800
    • Mor, A.1    Philips, M.R.2
  • 7
  • 9
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • DOI 10.1038/385595a0
    • Xu W, Harrison SC, Eck MJ. Three-dimensional structure of the tyrosine kinase c-Src. Nature 1997;385:595-602. (Pubitemid 27087566)
    • (1997) Nature , vol.385 , Issue.6617 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 10
    • 70349758510 scopus 로고    scopus 로고
    • Src kinases as therapeutic targets for cancer
    • Kim LC, Song L, Haura EB. Src kinases as therapeutic targets for cancer. Nat Rev Clin Oncol 2009;6:587-95.
    • (2009) Nat Rev Clin Oncol , vol.6 , pp. 587-595
    • Kim, L.C.1    Song, L.2    Haura, E.B.3
  • 11
    • 0030293986 scopus 로고    scopus 로고
    • The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions
    • van der Geer P, Wiley S, Gish GD, Pawson T. The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions. Curr Biol 1996;6:1435-44. (Pubitemid 27012242)
    • (1996) Current Biology , vol.6 , Issue.11 , pp. 1435-1444
    • Van Der, G.P.1    Wiley, S.2    Gish, G.D.3    Pawson, T.4
  • 12
    • 0034034785 scopus 로고    scopus 로고
    • Suppression of malignant growth potentials of v-Src-transformed human gallbladder epithelial cells by adenovirus-mediated dominant negative H-Ras
    • DOI 10.1002/(SICI)1097-4652(200005)183:2<221::AID-JCP8>3.0.CO;2-L
    • Tokumitsu Y, Nakano S, Ueno H, Niho Y. Suppression of malignant growth potentials of v-Src-transformed human gallbladder epithelial cells by adenovirus-mediated dominant negative H-Ras. J Cell Physiol 2000;183:221-7. (Pubitemid 30185940)
    • (2000) Journal of Cellular Physiology , vol.183 , Issue.2 , pp. 221-227
    • Tokumitsu, Y.1    Nakano, S.2    Ueno, H.3    Niho, Y.4
  • 15
    • 0037849951 scopus 로고    scopus 로고
    • Differences on the inhibitory specificities of H-Ras, K-Ras, and N-Ras (N17) dominant negative mutants are related to their membrane microlocalization
    • DOI 10.1074/jbc.M209807200
    • Matallanas D, Arozarena I, Berciano MT, Aaronson DS, Pellicer A, Lafarga M, et al. Differences on the inhibitory specificities of H-Ras, KRas, and N-Ras (N17) dominant negative mutants are related to their membrane microlocalization. J Biol Chem 2003;278:4572-81. (Pubitemid 36800954)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.7 , pp. 4572-4581
    • Matallanas, D.1    Arozarena, I.2    Berciano, M.T.3    Aaronson, D.S.4    Pellicer, A.5    Lafarga, M.6    Crespo, P.7
  • 18
    • 0021285532 scopus 로고
    • A short sequence in the p60(src) N terminus is required for p60(src) myristylation and membrane association and for cell transformation
    • Cross FR, Garber EA, Pellman D, Hanafusa H. A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation. Mol Cell Biol 1984;4:1834-42. (Pubitemid 14008294)
    • (1984) Molecular and Cellular Biology , vol.4 , Issue.9 , pp. 1834-1842
    • Cross, F.R.1    Garber, E.A.2    Pellman, D.3    Hanafusa, H.4
  • 20
    • 0030936987 scopus 로고    scopus 로고
    • Redox regulation of cellular activation
    • DOI 10.1146/annurev.immunol.15.1.351
    • Nakamura H, Nakamura K, Yodoi J. Redox regulation of cellular activation. Annu Rev Immunol 1997;15:351-69. (Pubitemid 27169285)
    • (1997) Annual Review of Immunology , vol.15 , pp. 351-369
    • Nakamura, H.1    Nakamura, K.2    Yodoi, J.3
  • 21
    • 0037264633 scopus 로고    scopus 로고
    • Targeting RAS signalling pathways in cancer therapy
    • DOI 10.1038/nrc969
    • Downward J. Targeting RAS signalling pathways in cancer therapy. Nat Rev Cancer 2003;3:11-22. (Pubitemid 37328883)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.1 , pp. 11-22
    • Downward, J.1
  • 23
    • 0033762434 scopus 로고    scopus 로고
    • Ras-dependent regulation of c-Jun phosphorylation is mediated by the Ral guanine nucleotide exchange factor-Ral pathway
    • de Ruiter ND, Wolthuis RM, van Dam H, Burgering BM, Bos JL. Ras-dependent regulation of c-Jun phosphorylation is mediated by the Ral guanine nucleotide exchange factor-Ral pathway. Mol Cell Biol 2000;20:8480-8.
    • (2000) Mol Cell Biol , vol.20 , pp. 8480-8488
    • De Ruiter, N.D.1    Wolthuis, R.M.2    Van Dam, H.3    Burgering, B.M.4    Bos, J.L.5
  • 24
    • 0030001017 scopus 로고    scopus 로고
    • p120 Ras GTPase-activating protein interacts with Ras-GTP through specific conserved residues
    • DOI 10.1074/jbc.271.26.15322
    • Miao W, Eichelberger L, Baker L, Marshall MS. p120 Ras GTPase-activating protein interacts with Ras-GTP through specific conserved residues. J Biol Chem 1996;271:15322-9. (Pubitemid 26225297)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.26 , pp. 15322-15329
    • Miao, W.1    Eichelberger, L.2    Baker, L.3    Marshall, M.S.4
  • 25
    • 0031036224 scopus 로고    scopus 로고
    • p120 GAP modulates Ras activation of jun kinases and transformation
    • DOI 10.1074/jbc.272.3.1677
    • Clark GJ, Westwick JK, Der CJ. p120 GAP modulates Ras activation of Jun kinases and transformation. J Biol Chem 1997;272:1677-81. (Pubitemid 27043252)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.3 , pp. 1677-1681
    • Clark, G.J.1    Westwick, J.K.2    Der, C.J.3
  • 26
    • 0034634476 scopus 로고    scopus 로고
    • The Ras/p120 GTPase-activating protein (GAP) interaction is regulated by the p120 GAP pleckstrin homology domain
    • Drugan JK, Rogers-Graham K, Gilmer T, Campbell S, Clark GJ. The Ras/p120 GTPase-activating protein (GAP) interaction is regulated by the p120 GAP pleckstrin homology domain. J Biol Chem 2000;275:35021-7.
    • (2000) J Biol Chem , vol.275 , pp. 35021-35027
    • Drugan, J.K.1    Rogers-Graham, K.2    Gilmer, T.3    Campbell, S.4    Clark, G.J.5
  • 27
    • 9344248103 scopus 로고    scopus 로고
    • The Ras-GTPase-activating protein SH3 domain is required for Cdc2 activation and Mos induction by oncogenic Ras in Xenopus oocytes independently of mitogen-activated protein kinase activation
    • Pomerance M, Thang MN, Tocque B, Pierre M. The Ras-GTPase-activating protein SH3 domain is required for Cdc2 activation and mos induction by oncogenic Ras in Xenopus oocytes independently of mitogen-activated protein kinase activation. Mol Cell Biol 1996;16:3179-86. (Pubitemid 26161315)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.6 , pp. 3179-3186
    • Pomerance, M.1    Thang, M.N.2    Tocque, B.3    Pierre, M.4
  • 28
    • 0029029889 scopus 로고
    • Two SH2domains of p120 Ras GTPase-activating protein bind synergistically to tyrosine phosphorylated p190 Rho GTPase-activating protein
    • Bryant SS, Briggs S, Smithgall TE, Martin GA, McCormick F, Chang JH, Parsons SJ, Jove R. Two SH2domains of p120 Ras GTPase-activating protein bind synergistically to tyrosine phosphorylated p190 Rho GTPase-activating protein. J Biol Chem 1995;270:17947-52.
    • (1995) J Biol Chem , vol.270 , pp. 17947-17952
    • Bryant, S.S.1    Briggs, S.2    Smithgall, T.E.3    Martin, G.A.4    McCormick, F.5    Chang, J.H.6    Parsons, S.J.7    Jove, R.8
  • 29
    • 77950531323 scopus 로고    scopus 로고
    • Src kinase regulates the integrity and function of the Golgi apparatus via activation of dynamin 2
    • Weller SG, Capitani M, Cao H, Micaroni M, Luini A, Sallese M, et al. Src kinase regulates the integrity and function of the Golgi apparatus via activation of dynamin 2. Proc Natl Acad Sci U S A 2010;107:5863-8.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5863-5868
    • Weller, S.G.1    Capitani, M.2    Cao, H.3    Micaroni, M.4    Luini, A.5    Sallese, M.6
  • 30
    • 77953161781 scopus 로고    scopus 로고
    • Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes
    • Gill DJ, Chia J, Senewiratne J, Bard F. Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes. J Cell Biol 2010;189:843-58.
    • (2010) J Cell Biol , vol.189 , pp. 843-858
    • Gill, D.J.1    Chia, J.2    Senewiratne, J.3    Bard, F.4
  • 32
    • 0037481949 scopus 로고    scopus 로고
    • Aberrant O-glycosylation inhibits stable expression of dysadherin, a carcinoma-associated antigen, and facilities cell-cell adhesion
    • DOI 10.1093/glycob/cwg065
    • Tsuiji H, Takasaki S, Sakamoto M, Irimura T, Hirohashi S. Aberrant O-glycosylation inhibits stable expression of dysadherin, a carcinomaassociated antigen, and facilitates cell-cell adhesion. Glycobiology 2003;13:521-7. (Pubitemid 36850125)
    • (2003) Glycobiology , vol.13 , Issue.7 , pp. 521-527
    • Tsuji, H.1    Takasaki, S.2    Sakamoto, M.3    Irimura, T.4    Hirohashi, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.