메뉴 건너뛰기




Volumn 279, Issue 1, 2009, Pages 22-29

v-Src-mediated transformation suppresses the expression of focal adhesion protein vinexin

Author keywords

Focal adhesion; Transformation; v Src; Vinexin

Indexed keywords

FOCAL ADHESION KINASE; MAMMALIAN TARGET OF RAPAMYCIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN TYROSINE KINASE; PROTEIN V SRC; PROTEIN VINEXIN; UNCLASSIFIED DRUG;

EID: 67349189176     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2009.01.017     Document Type: Article
Times cited : (7)

References (47)
  • 1
    • 0034283814 scopus 로고    scopus 로고
    • Integrin and ECM functions: roles in vertebrate development
    • De Arcangelis A., and Georges-Labouesse E. Integrin and ECM functions: roles in vertebrate development. Trends Genet. 16 (2000) 389-395
    • (2000) Trends Genet. , vol.16 , pp. 389-395
    • De Arcangelis, A.1    Georges-Labouesse, E.2
  • 2
    • 1842632667 scopus 로고    scopus 로고
    • Endothelial cell-cell junctions: happy together
    • Dejana E. Endothelial cell-cell junctions: happy together. Nat. Rev. Mol. Cell Biol. 5 (2004) 261-270
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 261-270
    • Dejana, E.1
  • 3
    • 0036595629 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in tumour progression
    • Thiery J.P. Epithelial-mesenchymal transitions in tumour progression. Nat. Rev. Cancer 2 (2002) 442-454
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 442-454
    • Thiery, J.P.1
  • 5
    • 5044238876 scopus 로고    scopus 로고
    • Integrin signalling during tumour progression
    • Guo W., and Giancotti F.G. Integrin signalling during tumour progression. Nat. Rev. Mol. Cell Biol. 5 (2004) 816-826
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 816-826
    • Guo, W.1    Giancotti, F.G.2
  • 6
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood J.D., and Cheresh D.A. Role of integrins in cell invasion and migration. Nat. Rev. Cancer 2 (2002) 91-100
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 7
    • 6844259884 scopus 로고    scopus 로고
    • Activation of c-Src by receptor tyrosine kinases in human colon cancer cells with high metastatic potential
    • Mao W., Irby R., Coppola D., Fu L., Wloch M., Turner J., Yu H., Garcia R., Jove R., and Yeatman T.J. Activation of c-Src by receptor tyrosine kinases in human colon cancer cells with high metastatic potential. Oncogene 15 (1997) 3083-3090
    • (1997) Oncogene , vol.15 , pp. 3083-3090
    • Mao, W.1    Irby, R.2    Coppola, D.3    Fu, L.4    Wloch, M.5    Turner, J.6    Yu, H.7    Garcia, R.8    Jove, R.9    Yeatman, T.J.10
  • 8
    • 0034469080 scopus 로고    scopus 로고
    • Tyrosine kinase signalling in breast cancer
    • Hynes N.E. Tyrosine kinase signalling in breast cancer. Breast Cancer Res. 2 (2000) 154-157
    • (2000) Breast Cancer Res. , vol.2 , pp. 154-157
    • Hynes, N.E.1
  • 10
    • 2942618768 scopus 로고    scopus 로고
    • A renaissance for SRC
    • Yeatman T.J. A renaissance for SRC. Nat. Rev. Cancer 4 (2004) 470-480
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 470-480
    • Yeatman, T.J.1
  • 11
    • 0035921792 scopus 로고    scopus 로고
    • The mechanism of cell cycle regulation by v-Src
    • Riley D., Carragher N.O., Frame M.C., and Wyke J.A. The mechanism of cell cycle regulation by v-Src. Oncogene 20 (2001) 5941-5950
    • (2001) Oncogene , vol.20 , pp. 5941-5950
    • Riley, D.1    Carragher, N.O.2    Frame, M.C.3    Wyke, J.A.4
  • 13
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch S.M., Vuori K., Ruoslahti E., and Chan-Hui P.Y. Control of adhesion-dependent cell survival by focal adhesion kinase. J. Cell Biol. 134 (1996) 793-799
    • (1996) J. Cell Biol. , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan-Hui, P.Y.4
  • 14
    • 4444338326 scopus 로고    scopus 로고
    • SRC-mediated phosphorylation of focal adhesion kinase couples actin and adhesion dynamics to survival signaling
    • Westhoff M.A., Serrels B., Fincham V.J., Frame M.C., and Carragher N.O. SRC-mediated phosphorylation of focal adhesion kinase couples actin and adhesion dynamics to survival signaling. Mol. Cell Biol. 24 (2004) 8113-8133
    • (2004) Mol. Cell Biol. , vol.24 , pp. 8113-8133
    • Westhoff, M.A.1    Serrels, B.2    Fincham, V.J.3    Frame, M.C.4    Carragher, N.O.5
  • 15
    • 0035830903 scopus 로고    scopus 로고
    • Cleavage of focal adhesion kinase by different proteases during SRC-regulated transformation and apoptosis. Distinct roles for calpain and caspases
    • Carragher N.O., Fincham V.J., Riley D., and Frame M.C. Cleavage of focal adhesion kinase by different proteases during SRC-regulated transformation and apoptosis. Distinct roles for calpain and caspases. J. Biol. Chem. 276 (2001) 4270-4275
    • (2001) J. Biol. Chem. , vol.276 , pp. 4270-4275
    • Carragher, N.O.1    Fincham, V.J.2    Riley, D.3    Frame, M.C.4
  • 18
    • 18844369343 scopus 로고    scopus 로고
    • Spatial distribution and functional significance of activated vinculin in living cells
    • Chen H., Cohen D.M., Choudhury D.M., Kioka N., and Craig S.W. Spatial distribution and functional significance of activated vinculin in living cells. J. Cell Biol. 169 (2005) 459-470
    • (2005) J. Cell Biol. , vol.169 , pp. 459-470
    • Chen, H.1    Cohen, D.M.2    Choudhury, D.M.3    Kioka, N.4    Craig, S.W.5
  • 20
    • 17844392598 scopus 로고    scopus 로고
    • A novel isoform of vinexin, vinexin gamma, regulates Sox9 gene expression through activation of MAPK cascade in mouse fetal gonad
    • Matsuyama M., Mizusaki H., Shimono A., Mukai T., Okumura K., Abe K., Shimada K., and Morohashi K. A novel isoform of vinexin, vinexin gamma, regulates Sox9 gene expression through activation of MAPK cascade in mouse fetal gonad. Genes Cells 10 (2005) 421-434
    • (2005) Genes Cells , vol.10 , pp. 421-434
    • Matsuyama, M.1    Mizusaki, H.2    Shimono, A.3    Mukai, T.4    Okumura, K.5    Abe, K.6    Shimada, K.7    Morohashi, K.8
  • 21
    • 34848888944 scopus 로고    scopus 로고
    • Changes in vinexin expression patterns in the mouse testis induced by developmental exposure to 17beta-estradiol
    • Paz M., Lopez-Casas P.P., and Del Mazo J. Changes in vinexin expression patterns in the mouse testis induced by developmental exposure to 17beta-estradiol. Biol. Reprod. (2007)
    • (2007) Biol. Reprod.
    • Paz, M.1    Lopez-Casas, P.P.2    Del Mazo, J.3
  • 22
    • 0033544921 scopus 로고    scopus 로고
    • Vinexin forms a signaling complex with Sos and modulates epidermal growth factor-induced c-Jun N-terminal kinase/stress-activated protein kinase activities
    • Akamatsu M., Aota S., Suwa A., Ueda K., Amachi T., Yamada K.M., Akiyama S.K., and Kioka N. Vinexin forms a signaling complex with Sos and modulates epidermal growth factor-induced c-Jun N-terminal kinase/stress-activated protein kinase activities. J. Biol. Chem. 274 (1999) 35933-35937
    • (1999) J. Biol. Chem. , vol.274 , pp. 35933-35937
    • Akamatsu, M.1    Aota, S.2    Suwa, A.3    Ueda, K.4    Amachi, T.5    Yamada, K.M.6    Akiyama, S.K.7    Kioka, N.8
  • 23
    • 0037066734 scopus 로고    scopus 로고
    • Vinexin beta regulates the anchorage dependence of ERK2 activation stimulated by epidermal growth factor
    • Suwa A., Mitsushima M., Ito T., Akamatsu M., Ueda K., Amachi T., and Kioka N. Vinexin beta regulates the anchorage dependence of ERK2 activation stimulated by epidermal growth factor. J. Biol. Chem. 277 (2002) 13053-13058
    • (2002) J. Biol. Chem. , vol.277 , pp. 13053-13058
    • Suwa, A.1    Mitsushima, M.2    Ito, T.3    Akamatsu, M.4    Ueda, K.5    Amachi, T.6    Kioka, N.7
  • 24
    • 4544227784 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin
    • Mitsushima M., Suwa A., Amachi T., Ueda K., and Kioka N. Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin. J. Biol. Chem. 279 (2004) 34570-34577
    • (2004) J. Biol. Chem. , vol.279 , pp. 34570-34577
    • Mitsushima, M.1    Suwa, A.2    Amachi, T.3    Ueda, K.4    Kioka, N.5
  • 27
    • 35848931706 scopus 로고    scopus 로고
    • Essential roles of ERK-mediated phosphorylation of vinexin in cell spreading, migration and anchorage-independent growth
    • Mizutani K., Ito H., Iwamoto I., Morishita R., Deguchi T., Nozawa Y., Asano T., and Nagata K.I. Essential roles of ERK-mediated phosphorylation of vinexin in cell spreading, migration and anchorage-independent growth. Oncogene 26 (2007) 7122-7131
    • (2007) Oncogene , vol.26 , pp. 7122-7131
    • Mizutani, K.1    Ito, H.2    Iwamoto, I.3    Morishita, R.4    Deguchi, T.5    Nozawa, Y.6    Asano, T.7    Nagata, K.I.8
  • 28
    • 34247501623 scopus 로고    scopus 로고
    • Involvement of phosphatases in the anchorage-dependent regulation of ERK2 activation
    • Mitsushima M., Ueda K., and Kioka N. Involvement of phosphatases in the anchorage-dependent regulation of ERK2 activation. Exp. Cell Res. 313 (2007) 1830-1838
    • (2007) Exp. Cell Res. , vol.313 , pp. 1830-1838
    • Mitsushima, M.1    Ueda, K.2    Kioka, N.3
  • 29
    • 0035157990 scopus 로고    scopus 로고
    • Hyaluronan activates cell motility of v-Src-transformed cells via Ras-mitogen-activated protein kinase and phosphoinositide 3-kinase-Akt in a tumor-specific manner
    • Sohara Y., Ishiguro N., Machida K., Kurata H., Thant A.A., Senga T., Matsuda S., Kimata K., Iwata H., and Hamaguchi M. Hyaluronan activates cell motility of v-Src-transformed cells via Ras-mitogen-activated protein kinase and phosphoinositide 3-kinase-Akt in a tumor-specific manner. Mol. Biol. Cell 12 (2001) 1859-1868
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1859-1868
    • Sohara, Y.1    Ishiguro, N.2    Machida, K.3    Kurata, H.4    Thant, A.A.5    Senga, T.6    Matsuda, S.7    Kimata, K.8    Iwata, H.9    Hamaguchi, M.10
  • 30
    • 0037821783 scopus 로고    scopus 로고
    • Interaction of lp-dlg/KIAA0583, a membrane-associated guanylate kinase family protein, with vinexin and beta-catenin at sites of cell-cell contact
    • Wakabayashi M., Ito T., Mitsushima M., Aizawa S., Ueda K., Amachi T., and Kioka N. Interaction of lp-dlg/KIAA0583, a membrane-associated guanylate kinase family protein, with vinexin and beta-catenin at sites of cell-cell contact. J. Biol. Chem. 278 (2003) 21709-21714
    • (2003) J. Biol. Chem. , vol.278 , pp. 21709-21714
    • Wakabayashi, M.1    Ito, T.2    Mitsushima, M.3    Aizawa, S.4    Ueda, K.5    Amachi, T.6    Kioka, N.7
  • 31
    • 0027081145 scopus 로고
    • Potent and specific inhibition of p60v-src protein kinase both in vivo and in vitro by radicicol
    • Kwon H.J., Yoshida M., Fukui Y., Horinouchi S., and Beppu T. Potent and specific inhibition of p60v-src protein kinase both in vivo and in vitro by radicicol. Cancer Res. 52 (1992) 6926-6930
    • (1992) Cancer Res. , vol.52 , pp. 6926-6930
    • Kwon, H.J.1    Yoshida, M.2    Fukui, Y.3    Horinouchi, S.4    Beppu, T.5
  • 32
    • 0032554763 scopus 로고    scopus 로고
    • Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol
    • Sharma S.V., Agatsuma T., and Nakano H. Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol. Oncogene 16 (1998) 2639-2645
    • (1998) Oncogene , vol.16 , pp. 2639-2645
    • Sharma, S.V.1    Agatsuma, T.2    Nakano, H.3
  • 33
    • 0032978365 scopus 로고    scopus 로고
    • Transformation by v-Src: Ras-MAPK and PI3K-mTOR mediate parallel pathways
    • Penuel E., and Martin G.S. Transformation by v-Src: Ras-MAPK and PI3K-mTOR mediate parallel pathways. Mol. Biol. Cell 10 (1999) 1693-1703
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1693-1703
    • Penuel, E.1    Martin, G.S.2
  • 34
    • 0034660524 scopus 로고    scopus 로고
    • Active ERK/MAP kinase is targeted to newly forming cell-matrix adhesions by integrin engagement and v-Src
    • Fincham V.J., James M., Frame M.C., and Winder S.J. Active ERK/MAP kinase is targeted to newly forming cell-matrix adhesions by integrin engagement and v-Src. EMBO J. 19 (2000) 2911-2923
    • (2000) EMBO J. , vol.19 , pp. 2911-2923
    • Fincham, V.J.1    James, M.2    Frame, M.C.3    Winder, S.J.4
  • 35
    • 0036257343 scopus 로고    scopus 로고
    • Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction
    • Kioka N., Ueda K., and Amachi T. Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction. Cell Struct. Funct. 27 (2002) 1-7
    • (2002) Cell Struct. Funct. , vol.27 , pp. 1-7
    • Kioka, N.1    Ueda, K.2    Amachi, T.3
  • 37
    • 33747473628 scopus 로고    scopus 로고
    • Vinexin beta regulates the phosphorylation of epidermal growth factor receptor on the cell surface
    • Mitsushima M., Ueda K., and Kioka N. Vinexin beta regulates the phosphorylation of epidermal growth factor receptor on the cell surface. Genes Cells 11 (2006) 971-982
    • (2006) Genes Cells , vol.11 , pp. 971-982
    • Mitsushima, M.1    Ueda, K.2    Kioka, N.3
  • 38
    • 0037442804 scopus 로고    scopus 로고
    • Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl
    • Soubeyran P., Barac A., Szymkiewicz I., and Dikic I. Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl. Biochem. J. 370 (2003) 29-34
    • (2003) Biochem. J. , vol.370 , pp. 29-34
    • Soubeyran, P.1    Barac, A.2    Szymkiewicz, I.3    Dikic, I.4
  • 39
    • 33751103910 scopus 로고    scopus 로고
    • CAP interacts with cytoskeletal proteins and regulates adhesion-mediated ERK activation and motility
    • Zhang M., Liu J., Cheng A., Deyoung S.M., Chen X., Dold L.H., and Saltiel A.R. CAP interacts with cytoskeletal proteins and regulates adhesion-mediated ERK activation and motility. EMBO J. 25 (2006) 5284-5293
    • (2006) EMBO J. , vol.25 , pp. 5284-5293
    • Zhang, M.1    Liu, J.2    Cheng, A.3    Deyoung, S.M.4    Chen, X.5    Dold, L.H.6    Saltiel, A.R.7
  • 43
    • 0031953831 scopus 로고    scopus 로고
    • Stat3 activation by Src induces specific gene regulation and is required for cell transformation
    • Turkson J., Bowman T., Garcia R., Caldenhoven E., De Groot R.P., and Jove R. Stat3 activation by Src induces specific gene regulation and is required for cell transformation. Mol. Cell Biol. 18 (1998) 2545-2552
    • (1998) Mol. Cell Biol. , vol.18 , pp. 2545-2552
    • Turkson, J.1    Bowman, T.2    Garcia, R.3    Caldenhoven, E.4    De Groot, R.P.5    Jove, R.6
  • 44
    • 0033968596 scopus 로고    scopus 로고
    • Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR
    • Yokogami K., Wakisaka S., Avruch J., and Reeves S.A. Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR. Curr. Biol. 10 (2000) 47-50
    • (2000) Curr. Biol. , vol.10 , pp. 47-50
    • Yokogami, K.1    Wakisaka, S.2    Avruch, J.3    Reeves, S.A.4
  • 45
    • 33751348056 scopus 로고    scopus 로고
    • Ablation in mice of the mTORC components raptor, rector, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1
    • Guertin D.A., Stevens D.M., Thoreen C.C., Burds A.A., Kalaany N.Y., Moffat J., Brown M., Fitzgerald K.J., and Sabatini D.M. Ablation in mice of the mTORC components raptor, rector, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1. Dev. Cell 11 (2006) 859-871
    • (2006) Dev. Cell , vol.11 , pp. 859-871
    • Guertin, D.A.1    Stevens, D.M.2    Thoreen, C.C.3    Burds, A.A.4    Kalaany, N.Y.5    Moffat, J.6    Brown, M.7    Fitzgerald, K.J.8    Sabatini, D.M.9
  • 46
    • 1642349839 scopus 로고    scopus 로고
    • Calpain activity is generally elevated during transformation but has oncogene-specific biological functions
    • Carragher N.O., Fonseca B.D., and Frame M.C. Calpain activity is generally elevated during transformation but has oncogene-specific biological functions. Neoplasia 6 (2004) 53-73
    • (2004) Neoplasia , vol.6 , pp. 53-73
    • Carragher, N.O.1    Fonseca, B.D.2    Frame, M.C.3
  • 47
    • 0344629442 scopus 로고    scopus 로고
    • Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components
    • Taveau M., Bourg N., Sillon G., Roudaut C., Bartoli M., and Richard I. Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components. Mol. Cell Biol. 23 (2003) 9127-9135
    • (2003) Mol. Cell Biol. , vol.23 , pp. 9127-9135
    • Taveau, M.1    Bourg, N.2    Sillon, G.3    Roudaut, C.4    Bartoli, M.5    Richard, I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.