메뉴 건너뛰기




Volumn 270, Issue 2, 2008, Pages 354-361

Mutation of Y925F in focal adhesion kinase (FAK) suppresses melanoma cell proliferation and metastasis

Author keywords

B16F10 cells; Erk; FAK; Metastasis; Paxillin; Y925F mutation

Indexed keywords

FOCAL ADHESION KINASE; PAXILLIN; PROTEIN TYROSINE KINASE; VASCULOTROPIN;

EID: 52149083736     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2008.05.042     Document Type: Article
Times cited : (45)

References (25)
  • 1
    • 0038481970 scopus 로고    scopus 로고
    • The pathogenesis of cancer metastasis the 'seed and soil' hypothesis revisited
    • Fidler I.J. The pathogenesis of cancer metastasis the 'seed and soil' hypothesis revisited. Nat. Rev. Cancer 3 (2003) 453-458
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 453-458
    • Fidler, I.J.1
  • 2
    • 0036794592 scopus 로고    scopus 로고
    • Cancer spread and micrometastasis development: quantitative approaches for in vivo models
    • MacDonald I.C., Groom A.C., and Chambers A.F. Cancer spread and micrometastasis development: quantitative approaches for in vivo models. Bioessays 24 (2002) 885-893
    • (2002) Bioessays , vol.24 , pp. 885-893
    • MacDonald, I.C.1    Groom, A.C.2    Chambers, A.F.3
  • 5
    • 0142141199 scopus 로고    scopus 로고
    • Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility
    • Hanks S.K., Ryzhova L., Shin N.Y., and Brábek J. Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility. Front. Biosci. 8 (2003) 982-996
    • (2003) Front. Biosci. , vol.8 , pp. 982-996
    • Hanks, S.K.1    Ryzhova, L.2    Shin, N.Y.3    Brábek, J.4
  • 6
    • 33846554255 scopus 로고    scopus 로고
    • Focal adhesion kinase: a potential target in cancer therapy
    • van Nimwegen M.J., and van de Water B. Focal adhesion kinase: a potential target in cancer therapy. Biochem. Pharmacol. 73 (2007) 597-609
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 597-609
    • van Nimwegen, M.J.1    van de Water, B.2
  • 7
    • 0033538078 scopus 로고    scopus 로고
    • FAK is the upstream signal protein of the phosphatidylinositol 3-kinase-Akt survival pathway in hydrogen peroxide-induced apoptosis of a human glioblastoma cell line
    • Sonoda Y., Watanabe S., Matsumoto Y., Aizu-Yokota E., and Kasahara T. FAK is the upstream signal protein of the phosphatidylinositol 3-kinase-Akt survival pathway in hydrogen peroxide-induced apoptosis of a human glioblastoma cell line. J. Biol. Chem. 274 (1999) 10566-10570
    • (1999) J. Biol. Chem. , vol.274 , pp. 10566-10570
    • Sonoda, Y.1    Watanabe, S.2    Matsumoto, Y.3    Aizu-Yokota, E.4    Kasahara, T.5
  • 8
    • 0034717285 scopus 로고    scopus 로고
    • Anti-apoptosis of focal adhesion kinase (FAK). Induction of inhibitor-of-apoptosis proteins and apoptosis suppression by the overexpression of FAK in a human leukemic cell line, HL-60
    • Sonoda Y., Matsumoto Y., Funakoshi M., Yamamoto D., Hanks S.K., and Kasahara T. Anti-apoptosis of focal adhesion kinase (FAK). Induction of inhibitor-of-apoptosis proteins and apoptosis suppression by the overexpression of FAK in a human leukemic cell line, HL-60. J. Biol. Chem. 275 (2000) 16309-16315
    • (2000) J. Biol. Chem. , vol.275 , pp. 16309-16315
    • Sonoda, Y.1    Matsumoto, Y.2    Funakoshi, M.3    Yamamoto, D.4    Hanks, S.K.5    Kasahara, T.6
  • 9
    • 0033578641 scopus 로고    scopus 로고
    • Suppression of ultraviolet irradiation-induced apoptosis by overexpression of focal adhesion kinase in Madin-Darby canine kidney cells
    • Chan P.C., Lai J.F., Cheng C.H., Tang M.J., Chiu C.C., and Chen H.C. Suppression of ultraviolet irradiation-induced apoptosis by overexpression of focal adhesion kinase in Madin-Darby canine kidney cells. J. Biol. Chem. 274 (1999) 26901-26906
    • (1999) J. Biol. Chem. , vol.274 , pp. 26901-26906
    • Chan, P.C.1    Lai, J.F.2    Cheng, C.H.3    Tang, M.J.4    Chiu, C.C.5    Chen, H.C.6
  • 10
    • 0034742531 scopus 로고    scopus 로고
    • Integrin alphavbeta3 mediates K1735 murine melanoma cell motility in vivo and in vitro
    • Li X., Regezi J., Ross F.P., Blystone S., Ili D., Leong S.P., and Ramos D.M. Integrin alphavbeta3 mediates K1735 murine melanoma cell motility in vivo and in vitro. J. Cell Sci. 114 (2001) 2665-2672
    • (2001) J. Cell Sci. , vol.114 , pp. 2665-2672
    • Li, X.1    Regezi, J.2    Ross, F.P.3    Blystone, S.4    Ili, D.5    Leong, S.P.6    Ramos, D.M.7
  • 11
    • 33646822656 scopus 로고    scopus 로고
    • Integrin alpha2-mediated ERK and calpain activation play a critical role in cell adhesion and motility via focal adhesion kinase signaling: identification of a novel signaling pathway
    • Sawhney R.S., Cookson M.M., Omar Y., Hauser J., and Brattain M.G. Integrin alpha2-mediated ERK and calpain activation play a critical role in cell adhesion and motility via focal adhesion kinase signaling: identification of a novel signaling pathway. J. Biol. Chem. 281 (2006) 8497-8510
    • (2006) J. Biol. Chem. , vol.281 , pp. 8497-8510
    • Sawhney, R.S.1    Cookson, M.M.2    Omar, Y.3    Hauser, J.4    Brattain, M.G.5
  • 12
    • 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., Metcaf III C.A., Sawyer T.K., and Frame M.C. 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 (2005) 1335-1342
    • (2005) Cancer Res. , vol.65 , pp. 1335-1342
    • Brunton, V.G.1    Avizienyte, E.2    Fincham, V.J.3    Serrels, B.4    Metcaf III, C.A.5    Sawyer, T.K.6    Frame, M.C.7
  • 13
    • 20444405314 scopus 로고    scopus 로고
    • Foot in mouth: do focal adhesions disassemble by endocytosis?
    • Burridge K. Foot in mouth: do focal adhesions disassemble by endocytosis?. Nat. Cell Biol. 7 (2005) 545-547
    • (2005) Nat. Cell Biol. , vol.7 , pp. 545-547
    • Burridge, K.1
  • 14
    • 20444370219 scopus 로고    scopus 로고
    • Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase
    • Ezratty E.J., Partridge M.A., and Gundersen G.G. Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase. Nat. Cell Biol. 7 (2005) 581-590
    • (2005) Nat. Cell Biol. , vol.7 , pp. 581-590
    • Ezratty, E.J.1    Partridge, M.A.2    Gundersen, G.G.3
  • 15
    • 0018829269 scopus 로고
    • Distribution of membrane anionic sites on B16 melanoma variants with differing lung colonising potential
    • Raz A., Bucana C., McLellan W., and Fidler I.J. Distribution of membrane anionic sites on B16 melanoma variants with differing lung colonising potential. Nature 284 (1980) 363-364
    • (1980) Nature , vol.284 , pp. 363-364
    • Raz, A.1    Bucana, C.2    McLellan, W.3    Fidler, I.J.4
  • 16
    • 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. 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 (1995) 954-963
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 17
    • 3142733866 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase (ERK)-dependent gene expression contributes to L1 cell adhesion molecule-dependent motility and invasion
    • Silletti S., Yebra M., Perez B., Cirulli V., McMahon M., and Montgomery A.M. Extracellular signal-regulated kinase (ERK)-dependent gene expression contributes to L1 cell adhesion molecule-dependent motility and invasion. J. Biol. Chem. 279 (2004) 28880-28888
    • (2004) J. Biol. Chem. , vol.279 , pp. 28880-28888
    • Silletti, S.1    Yebra, M.2    Perez, B.3    Cirulli, V.4    McMahon, M.5    Montgomery, A.M.6
  • 19
    • 0034834329 scopus 로고    scopus 로고
    • Fibronectin, integrins, and growth control
    • Danen E.H.J., and Yamada K.M. Fibronectin, integrins, and growth control. J. Cell Physiol. 189 (2001) 1-13
    • (2001) J. Cell Physiol. , vol.189 , pp. 1-13
    • Danen, E.H.J.1    Yamada, K.M.2
  • 21
    • 33644647192 scopus 로고    scopus 로고
    • Inhibition of SRC expression and activity inhibits tumor progression and metastasis of human pancreatic adenocarcinoma cells in an orthotopic nude mouse model
    • Trevino J.G., Summy J.M., Lesslie D.P., Parikh N.U., Hong D.S., Lee F.Y., Donato N.J., Abbruzzese J.L., Baker C.H., and Gallick G.E. Inhibition of SRC expression and activity inhibits tumor progression and metastasis of human pancreatic adenocarcinoma cells in an orthotopic nude mouse model. Am. J. Pathol. 168 (2006) 962-972
    • (2006) Am. J. Pathol. , vol.168 , pp. 962-972
    • Trevino, J.G.1    Summy, J.M.2    Lesslie, D.P.3    Parikh, N.U.4    Hong, D.S.5    Lee, F.Y.6    Donato, N.J.7    Abbruzzese, J.L.8    Baker, C.H.9    Gallick, G.E.10
  • 22
    • 33744945040 scopus 로고    scopus 로고
    • Multiple signaling pathways mediate compaction of collagen matrices by EGF-stimulated fibroblasts
    • Smith K.D., Wells A., and Lauffenburger D.A. Multiple signaling pathways mediate compaction of collagen matrices by EGF-stimulated fibroblasts. Exp. Cell Res. 312 (2006) 1970-1982
    • (2006) Exp. Cell Res. , vol.312 , pp. 1970-1982
    • Smith, K.D.1    Wells, A.2    Lauffenburger, D.A.3
  • 23
    • 0033229742 scopus 로고    scopus 로고
    • Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlates with cleavage of pp125(FAK), paxillin, and talin
    • Carragher N.O., Levkau B., Ross R., and Raines E.W. Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlates with cleavage of pp125(FAK), paxillin, and talin. J. Cell Biol. 147 (1999) 619-623
    • (1999) J. Cell Biol. , vol.147 , pp. 619-623
    • Carragher, N.O.1    Levkau, B.2    Ross, R.3    Raines, E.W.4
  • 24
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin: adapting to change
    • Brown M.C., and Turner C.E. Paxillin: adapting to change. Physiol. Rev. 84 (2004) 1315-1339
    • (2004) Physiol. Rev. , vol.84 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.