메뉴 건너뛰기




Volumn 20, Issue 1, 2000, Pages 139-148

The phosphoinositide 3-OH kinase/AKT2 pathway as a critical target for farnesyltransferase inhibitor-induced apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

N [[5 [(2 AMINO 3 MERCAPTOPROPYL)AMINO][1,1' BIPHENYL] 2 YL]CARBONYL]METHIONINE METHYL ESTER; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN FARNESYLTRANSFERASE INHIBITOR;

EID: 0033986790     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.1.139-148.2000     Document Type: Article
Times cited : (229)

References (78)
  • 1
    • 0027242129 scopus 로고
    • The proteins encoded by c-akt and v-akt differ in post-translational modification, subcellular localization and oncogenic potential
    • Ahmed, N. N., T. F. Franke, A. Bellacosa, K. Datta, M.-E. Gonzalez-Portal, T. Taguchi, J. R. Testa, and P. N. Tsichlis. 1993. The proteins encoded by c-akt and v-akt differ in post-translational modification, subcellular localization and oncogenic potential. Oncogene 8:1957-1963.
    • (1993) Oncogene , vol.8 , pp. 1957-1963
    • Ahmed, N.N.1    Franke, T.F.2    Bellacosa, A.3    Datta, K.4    Gonzalez-Portal, M.-E.5    Taguchi, T.6    Testa, J.R.7    Tsichlis, P.N.8
  • 3
    • 0031913246 scopus 로고    scopus 로고
    • Mechanism of activation and function of protein kinase B
    • Alessi, D. R., and P. Cohen. 1998. Mechanism of activation and function of protein kinase B. Curr. Opin. Genet. Dev. 8:55-62.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 55-62
    • Alessi, D.R.1    Cohen, P.2
  • 4
    • 0032493105 scopus 로고    scopus 로고
    • Akt2 mRNA is highly expressed in embryonic brown fat and the AKT2 kinase is activated by insulin
    • Altomare, D. A., G. E. Lyons, Y. Mitsuuchi, J. Q. Cheng, and J. R. Testa. 1998. Akt2 mRNA is highly expressed in embryonic brown fat and the AKT2 kinase is activated by insulin. Oncogene 16:2407-2411.
    • (1998) Oncogene , vol.16 , pp. 2407-2411
    • Altomare, D.A.1    Lyons, G.E.2    Mitsuuchi, Y.3    Cheng, J.Q.4    Testa, J.R.5
  • 5
    • 0032545343 scopus 로고    scopus 로고
    • The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells
    • Aman, M. J., T. D. Lamkin, H. Okada, T. Kurosaki, and K. S. Ravichandran. 1998. The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells. J. Biol. Chem. 273:33922-33928.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33922-33928
    • Aman, M.J.1    Lamkin, T.D.2    Okada, H.3    Kurosaki, T.4    Ravichandran, K.S.5
  • 6
    • 0032512587 scopus 로고    scopus 로고
    • Protein kinase C modulates the insulin-stimulated increase in Akt1 and Akt3 activity in 3T3-L1 adipocytes
    • Barthel, A., K. Nakatani, A. A. Dandekar, and R. A. Roth. 1998. Protein kinase C modulates the insulin-stimulated increase in Akt1 and Akt3 activity in 3T3-L1 adipocytes. Biochem. Biophys. Res. Commun. 243:509-513.
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 509-513
    • Barthel, A.1    Nakatani, K.2    Dandekar, A.A.3    Roth, R.A.4
  • 8
    • 0026095665 scopus 로고
    • A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region
    • Bellacosa, A., J. R. Testa, S. P. Staal, and P. N. Tsichlis. 1991. A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region. Science 254:274-277.
    • (1991) Science , vol.254 , pp. 274-277
    • Bellacosa, A.1    Testa, J.R.2    Staal, S.P.3    Tsichlis, P.N.4
  • 9
    • 0032562682 scopus 로고    scopus 로고
    • The activation of p38 and apoptosis by the inhibition of Erk is antagonized by the phosphoinositide 3-kinase/Akt pathway
    • Berra, E., M. T. Diaz-Meco, and J. Moscat. 1998. The activation of p38 and apoptosis by the inhibition of Erk is antagonized by the phosphoinositide 3-kinase/Akt pathway. J. Biol. Chem. 273:10792-10797.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10792-10797
    • Berra, E.1    Diaz-Meco, M.T.2    Moscat, J.3
  • 11
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering, B. M. T., and P. J. Coffer. 1995. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376:599-602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.T.1    Coffer, P.J.2
  • 14
    • 0029979722 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase
    • Chen, H. C., P. A. Appeddu, H. Isoda, and J. L. Guan. 1996. Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase. J. Biol. Chem. 271:26329-26334.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26329-26334
    • Chen, H.C.1    Appeddu, P.A.2    Isoda, H.3    Guan, J.L.4
  • 16
    • 0001457668 scopus 로고    scopus 로고
    • Amplification of AKT2 in human pancreatic cancer cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA
    • Cheng, J. Q., B. Ruggeri, W. M. Klein, G. Sonoda, D. A. Altomare, D. K. Watson, and J. R. Testa. 1996. Amplification of AKT2 in human pancreatic cancer cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA. Proc. Natl. Acad. Sci. USA 93:3636-3641.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3636-3641
    • Cheng, J.Q.1    Ruggeri, B.2    Klein, W.M.3    Sonoda, G.4    Altomare, D.A.5    Watson, D.K.6    Testa, J.R.7
  • 17
    • 0030860466 scopus 로고    scopus 로고
    • Transforming activity and mitosis-dependent expression of the AKT2 oncogene: Evidence suggesting a link between cell cycle regulation and oncogenesis
    • Cheng, J. Q., D. A. Altomare, W. M. Klein, W-C. Lee, G. D. Kruh, N. A. Lissy, and J. R. Testa. 1997. Transforming activity and mitosis-dependent expression of the AKT2 oncogene: evidence suggesting a link between cell cycle regulation and oncogenesis. Oncogene 14:2793-2801.
    • (1997) Oncogene , vol.14 , pp. 2793-2801
    • Cheng, J.Q.1    Altomare, D.A.2    Klein, W.M.3    Lee, W.-C.4    Kruh, G.D.5    Lissy, N.A.6    Testa, J.R.7
  • 18
    • 0030994017 scopus 로고    scopus 로고
    • Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages
    • Choquet, D., D. P. Felsenfeld, M. P. Sheetz. 1997. Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages. Cell 88:39-48.
    • (1997) Cell , vol.88 , pp. 39-48
    • Choquet, D.1    Felsenfeld, D.P.2    Sheetz, M.P.3
  • 19
    • 0030749458 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors and cancer treatment: Targeting simply Ras?
    • Cox, A. D., and C. J. Der. 1997. Farnesyltransferase inhibitors and cancer treatment: targeting simply Ras? Biochim. Biophys. Acta 1333:F51-F71.
    • (1997) Biochim. Biophys. Acta , vol.1333
    • Cox, A.D.1    Der, C.J.2
  • 20
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross, D. A. E., D. R. Alessi, P. Cohen, M. Andjelkovich, and B. A. Hemmings. 1995. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378:785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.E.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 21
    • 0029807471 scopus 로고
    • Akt is a direct target of the phosphatidylinositol 3-kinase
    • Datta, K., A. Bellacosa, T. O. Chan, and P. N. Tsichlis. 1196. Akt is a direct target of the phosphatidylinositol 3-kinase. J. Biol. Chem. 271:30835-30839.
    • (1196) J. Biol. Chem. , vol.271 , pp. 30835-30839
    • Datta, K.1    Bellacosa, A.2    Chan, T.O.3    Tsichlis, P.N.4
  • 22
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta, S. R., H. Dudek, X. Tao, S. Masters, H. Fu, Y. Gotoh, and M. E. Greenberg. 1997. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91:231-241.
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 23
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
    • Delcommenne, M., C. Tan, V. Gray, L. Rue, J. Woodgett, and S. Dedhar. 1998. Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc. Natl. Acad. Sci. USA 95:11211-11216.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11211-11216
    • Delcommenne, M.1    Tan, C.2    Gray, V.3    Rue, L.4    Woodgett, J.5    Dedhar, S.6
  • 24
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • del Peso, L., M. Gonzalez-Garcia, C. Page, R. Herrera, and G. Nunez. 1997. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278:687-689.
    • (1997) Science , vol.278 , pp. 687-689
    • Del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 25
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3β regulates cyclin D1 proteolysis and subcellular localization
    • Diehl, J. A., M. G. Cheng, M. F. Roussel, and C. J. Sherr. 1998. Glycogen synthase kinase 3β regulates cyclin D1 proteolysis and subcellular localization. Genes Dev. 12:3499-3511.
    • (1998) Genes Dev. , vol.12 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.G.2    Roussel, M.F.3    Sherr, C.J.4
  • 26
    • 0033016719 scopus 로고    scopus 로고
    • Cell growth inhibition by farnesyltransferase inhibitors is mediated by gain of geranylgeranylated RhoB
    • Du, W., P. F. Lebowitz, and G. C. Prendergast. 1999. Cell growth inhibition by farnesyltransferase inhibitors is mediated by gain of geranylgeranylated RhoB. Mol. Cell. Biol. 19:1831-1840.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1831-1840
    • Du, W.1    Lebowitz, P.F.2    Prendergast, G.C.3
  • 27
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke, T. F., S. L. Yang, T. O. Chan, K. Datta, A. Kazlauskas, D. K. Morrison, D. R. Kaplan, and P. N. Tsichlis. 1995. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81:727-736.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.L.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6    Kaplan, D.R.7    Tsichlis, P.N.8
  • 28
    • 0030962347 scopus 로고    scopus 로고
    • The potential of farnesyltransferase inhibitors as cancer chemotherapeutics
    • Gibbs, J. B., and A. Oliff. 1997. The potential of farnesyltransferase inhibitors as cancer chemotherapeutics. Annu. Rev. Pharmacol. Toxicol. 37:143-166.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 143-166
    • Gibbs, J.B.1    Oliff, A.2
  • 33
    • 0025882091 scopus 로고
    • Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily
    • Jones, P. F., T. Jakubowicz, F. J. Pitossi, F. Maurer, and B. A. Hemmings. 1991. Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily. Proc. Natl. Acad. Sci. USA 88: 4171-4175.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4171-4175
    • Jones, P.F.1    Jakubowicz, T.2    Pitossi, F.J.3    Maurer, F.4    Hemmings, B.A.5
  • 34
    • 0026270993 scopus 로고
    • Molecular cloning of a second form of rac protein kinase
    • Jones, P. F., T. Jakubowicz, and B. A. Hemmings. 1991. Molecular cloning of a second form of rac protein kinase. Cell Regul. 2:1001-1009.
    • (1991) Cell Regul. , vol.2 , pp. 1001-1009
    • Jones, P.F.1    Jakubowicz, T.2    Hemmings, B.A.3
  • 35
    • 0029670038 scopus 로고    scopus 로고
    • Suppression of interleukin-1β-converting enzyme-mediated cell death by insulin-like growth factor
    • Jung, Y. K., M. Miura, and J. Yuan. 1996. Suppression of interleukin-1β-converting enzyme-mediated cell death by insulin-like growth factor. J. Biol. Chem. 271:5112-5117.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5112-5117
    • Jung, Y.K.1    Miura, M.2    Yuan, J.3
  • 36
    • 0031459917 scopus 로고    scopus 로고
    • Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through PI(3)K
    • Keely, P. J., J. K. Westwick, I. P. Whitehead, C. J. Der, and L. V. Parise. 1997. Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through PI(3)K. Nature 390:632-636.
    • (1997) Nature , vol.390 , pp. 632-636
    • Keely, P.J.1    Westwick, J.K.2    Whitehead, I.P.3    Der, C.J.4    Parise, L.V.5
  • 37
    • 0028800305 scopus 로고
    • Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation
    • Khosravi-Far, R., P. A. Solski, G. J. Clark, M. S. Kinch, and C. J. Der. 1995. Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation. Mol. Cell. Biol. 15:6443-6453.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6443-6453
    • Khosravi-Far, R.1    Solski, P.A.2    Clark, G.J.3    Kinch, M.S.4    Der, C.J.5
  • 38
    • 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., P. Rodriguez-Viciana, S. Wennstrom, P. H. Warne, and J. Downward. 1997. Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway. EMBO J. 16:2783-2793.
    • (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
  • 39
    • 0030839766 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is required for integrin-stimulated AKT and Raf-1/mitogen-activated protein kinase pathway activation
    • King, W. G., M. D. Mattaliano, T. O. Chan, P. N. Tsichlis, and J. S. Brugge. 1997. Phosphatidylinositol 3-kinase is required for integrin-stimulated AKT and Raf-1/mitogen-activated protein kinase pathway activation. Mol. Cell. Biol. 17:4406-4418.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4406-4418
    • King, W.G.1    Mattaliano, M.D.2    Chan, T.O.3    Tsichlis, P.N.4    Brugge, J.S.5
  • 40
    • 0027198412 scopus 로고
    • A region of the 85-kilodalton (kDa) subunit of phosphatidylinositol 3-kinase binds the 110-kDa catalytic subunit in vivo
    • Klippel, A., J. A. Escobedo, Q. Hu, and L. T. Williams. 1993. A region of the 85-kilodalton (kDa) subunit of phosphatidylinositol 3-kinase binds the 110-kDa catalytic subunit in vivo. Mol. Cell. Biol. 13:5560-5566.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5560-5566
    • Klippel, A.1    Escobedo, J.A.2    Hu, Q.3    Williams, L.T.4
  • 41
    • 0031708412 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase is sufficient for cell cycle entry and promotes cellular changes characteristic of oncogenic transformation
    • Klippel, A., M. A. Escobedo, M. S. Wachowicz, G. Apell, T. W. Brown, M. A. Giedlin, W. M. Kavanaugh, and L. T. Williams. 1998. Activation of phosphatidylinositol 3-kinase is sufficient for cell cycle entry and promotes cellular changes characteristic of oncogenic transformation. Mol. Cell. Biol. 18:5699-5711.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5699-5711
    • Klippel, A.1    Escobedo, M.A.2    Wachowicz, M.S.3    Apell, G.4    Brown, T.W.5    Giedlin, M.A.6    Kavanaugh, W.M.7    Williams, L.T.8
  • 42
    • 0028799420 scopus 로고
    • Molecular cloning and characterization of a new member of the Rac protein kinase family: Association of the pleckstrin homology domain of three types of Rac protein kinase with protein kinase C subspecies and βγ subunits of G proteins
    • Konishi, H., S. Kuroda, M. Tanaca, Y. Ono, K. Kameyama, T. Haga, and U. Kikkawa. 1995. Molecular cloning and characterization of a new member of the Rac protein kinase family: association of the pleckstrin homology domain of three types of Rac protein kinase with protein kinase C subspecies and βγ subunits of G proteins. Biochem. Biophys. Res. Commun. 216:526-534.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 526-534
    • Konishi, H.1    Kuroda, S.2    Tanaca, M.3    Ono, Y.4    Kameyama, K.5    Haga, T.6    Kikkawa, U.7
  • 43
    • 0028892646 scopus 로고
    • Evidence that farnesyltransferase inhibitors suppress Ras transformation by interfering with Rho activity
    • Lebowitz, P. F., J. P. Davide, and G. C. Prendergast. 1995. Evidence that farnesyltransferase inhibitors suppress Ras transformation by interfering with Rho activity. Mol. Cell. Biol. 15:6613-6622.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6613-6622
    • Lebowitz, P.F.1    Davide, J.P.2    Prendergast, G.C.3
  • 44
    • 0031050738 scopus 로고    scopus 로고
    • Farnesyl transferase inhibitors induce apoptosis of Ras-transformed cells denied substratum attachment
    • Lebowitz, P. F., D. Sakamuro, and G. C. Prendergast. 1997. Farnesyl transferase inhibitors induce apoptosis of Ras-transformed cells denied substratum attachment. Cancer Res. 57:708-713.
    • (1997) Cancer Res. , vol.57 , pp. 708-713
    • Lebowitz, P.F.1    Sakamuro, D.2    Prendergast, G.C.3
  • 45
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
    • Le Good, J. A., W. H. Ziegler, D. B. Parekh, D. R. Alessi, P. Cohen, and P. J. Parker. 1998. Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science 281:2042-2045.
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 46
    • 0028973293 scopus 로고
    • Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras-Raf complexes
    • Lerner, E. C., Y. Qian, M. A. Blaskovich, R. O. Fossum, A. Vogt, J. Sun, A. D. Cox, C. J. Der, A. D. Hamilton, and S. M. Sebti. 1995. Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras-Raf complexes. J. Biol. Chem. 270:26802-26806.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26802-26806
    • Lerner, E.C.1    Qian, Y.2    Blaskovich, M.A.3    Fossum, R.O.4    Vogt, A.5    Sun, J.6    Cox, A.D.7    Der, C.J.8    Hamilton, A.D.9    Sebti, S.M.10
  • 47
    • 0030952552 scopus 로고    scopus 로고
    • Inhibition of the prenylation of K-Ras, but not H- or N-Ras, is highly resistant to CAAX peptidomimetics and requires both a farnesyltransferase and a geranylgeranyltransferase I inhibitor in human tumor cell lines
    • Lerner, E. C., T. T. Zhang, D. B. Knowles, Y. Qian, A. D. Hamilton, and S. M. Sebti. 1997. Inhibition of the prenylation of K-Ras, but not H- or N-Ras, is highly resistant to CAAX peptidomimetics and requires both a farnesyltransferase and a geranylgeranyltransferase I inhibitor in human tumor cell lines. Oncogene 15:1283-1288.
    • (1997) Oncogene , vol.15 , pp. 1283-1288
    • Lerner, E.C.1    Zhang, T.T.2    Knowles, D.B.3    Qian, Y.4    Hamilton, A.D.5    Sebti, S.M.6
  • 48
    • 0032527913 scopus 로고    scopus 로고
    • AKT2, a member of the protein kinase B family, is activated by growth factors, v-Ha-ras, and v-src through phosphatidylinositol 3-kinase in human ovarian epithelial cancer cells
    • Liu, A.-X., J. R. Testa, T. C. Hamilton, R. Jove, S. V. Nicosia, and J. Q. Cheng. 1998. AKT2, a member of the protein kinase B family, is activated by growth factors, v-Ha-ras, and v-src through phosphatidylinositol 3-kinase in human ovarian epithelial cancer cells. Cancer Res. 58:2973-2977.
    • (1998) Cancer Res. , vol.58 , pp. 2973-2977
    • Liu, A.-X.1    Testa, J.R.2    Hamilton, T.C.3    Jove, R.4    Nicosia, S.V.5    Cheng, J.Q.6
  • 49
    • 0030840413 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase mediates epidermal growth factor-induced activation of the c-Jun N-terminal kinase signaling pathway
    • Logan, S. K., M. Falasca, P. Hu, and J. Schlessinger. 1997. Phosphatidylinositol 3-kinase mediates epidermal growth factor-induced activation of the c-Jun N-terminal kinase signaling pathway. Mol. Cell. Biol. 17:5784-5790.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5784-5790
    • Logan, S.K.1    Falasca, M.2    Hu, P.3    Schlessinger, J.4
  • 50
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama, T., and J. E. Dixon. 1998. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273:13375-13378.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 51
    • 0030727172 scopus 로고    scopus 로고
    • Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bβ
    • Meier, R., D. R. Alessi, P. Cron, M. Andjelkovic, and B. A. Hemmings. 1997. Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bβ. J. Biol. Chem. 272:30491-30497.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30491-30497
    • Meier, R.1    Alessi, D.R.2    Cron, P.3    Andjelkovic, M.4    Hemmings, B.A.5
  • 52
    • 0031004491 scopus 로고    scopus 로고
    • GGTI-298 induces G0-G1 block and apoptosis whereas FTI-277 causes G2-M enrichment in A549 cells
    • Miquel, K., A. Pradines, J. Sun, Y. Qian, A. D. Hamilton, S. M. Sebti, and G. Favre. 1997. GGTI-298 induces G0-G1 block and apoptosis whereas FTI-277 causes G2-M enrichment in A549 cells. Cancer Res. 57:1846-1850.
    • (1997) Cancer Res. , vol.57 , pp. 1846-1850
    • Miquel, K.1    Pradines, A.2    Sun, J.3    Qian, Y.4    Hamilton, A.D.5    Sebti, S.M.6    Favre, G.7
  • 53
    • 0032531274 scopus 로고    scopus 로고
    • Translocation and activation of AKT2 in response to stimulation by insulin
    • Mitsuuchi, Y., S. W. Johnson, S. Moonblatt, and J. R. Testa. 1998. Translocation and activation of AKT2 in response to stimulation by insulin. J. Cell. Biochem. 70:433-441.
    • (1998) J. Cell. Biochem. , vol.70 , pp. 433-441
    • Mitsuuchi, Y.1    Johnson, S.W.2    Moonblatt, S.3    Testa, J.R.4
  • 55
    • 0027320668 scopus 로고
    • Apoptosis of human erythroid colony-forming cells is decreased by stem cell factor and insulin-like growth factor I as well as erythropoietin
    • Muta, K., and S. B. Krantz. 1993. Apoptosis of human erythroid colony-forming cells is decreased by stem cell factor and insulin-like growth factor I as well as erythropoietin. J. Cell. Physiol. 156:264-271.
    • (1993) J. Cell. Physiol. , vol.156 , pp. 264-271
    • Muta, K.1    Krantz, S.B.2
  • 56
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
    • Palecek, S. P., J. C. Loftus, M. H. Ginsberg, D. A. Lauffenburger, and A. F. Horwitz. 1997. Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature 385:537-540.
    • (1997) Nature , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 57
    • 0032541677 scopus 로고    scopus 로고
    • Tyrosine kinase receptor-activated signal transduction pathways which lead to oncogenesis
    • Porter, A. C., and R. R. Vaillancourt. 1998. Tyrosine kinase receptor-activated signal transduction pathways which lead to oncogenesis. Oncogene 17:1343-1352.
    • (1998) Oncogene , vol.17 , pp. 1343-1352
    • Porter, A.C.1    Vaillancourt, R.R.2
  • 58
    • 0028903247 scopus 로고
    • An essential role for Rac in Ras transformation
    • Qiu, R. G., J. Chen, D. Kirn, F. McCormick, and M. Symons. 1995. An essential role for Rac in Ras transformation. Nature 374:457-459.
    • (1995) Nature , vol.374 , pp. 457-459
    • Qiu, R.G.1    Chen, J.2    Kirn, D.3    McCormick, F.4    Symons, M.5
  • 59
    • 0032584160 scopus 로고    scopus 로고
    • Etk/Bmx, a tyrosine kinase with a pleckstrin-homology domain, is an effector of phosphatidylinositol 3′-kinase and is involved in interleukin 6-induced neuroendocrine differentiation of prostate cancer cells
    • Qiu, Y., D. Robinson, T. G. Pretlow, and H. J. Kung. 1998. Etk/Bmx, a tyrosine kinase with a pleckstrin-homology domain, is an effector of phosphatidylinositol 3′-kinase and is involved in interleukin 6-induced neuroendocrine differentiation of prostate cancer cells. Proc. Natl. Acad. Sci. USA 95:3644-3649.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3644-3649
    • Qiu, Y.1    Robinson, D.2    Pretlow, T.G.3    Kung, H.J.4
  • 62
    • 0031936947 scopus 로고    scopus 로고
    • Amplification and overexpression of the AKT2 oncogene in a subset of human pancreatic ductal adenocarcinoma
    • Ruggeri, B., L. Huang, M. Wood, J. Q. Cheng, and J. R. Testa. 1998. Amplification and overexpression of the AKT2 oncogene in a subset of human pancreatic ductal adenocarcinoma. Mol. Carcinog. 21:81-86.
    • (1998) Mol. Carcinog. , vol.21 , pp. 81-86
    • Ruggeri, B.1    Huang, L.2    Wood, M.3    Cheng, J.Q.4    Testa, J.R.5
  • 63
    • 0028122650 scopus 로고
    • Focal adhesion kinase and associated proteins
    • Schaller, M. D., and J. T. Parsons. 1994. Focal adhesion kinase and associated proteins. Curr. Opin. Cell Biol. 6:705-710.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 705-710
    • Schaller, M.D.1    Parsons, J.T.2
  • 64
    • 0030749464 scopus 로고    scopus 로고
    • Inhibition of Ras prenylation: A novel approach to cancer chemotherapy
    • Sebti, S. M., and A. D. Hamilton. 1997. Inhibition of Ras prenylation: a novel approach to cancer chemotherapy. Pharmacol. Ther. 74:103-114.
    • (1997) Pharmacol. Ther. , vol.74 , pp. 103-114
    • Sebti, S.M.1    Hamilton, A.D.2
  • 65
    • 0031456065 scopus 로고    scopus 로고
    • Activation of phosphoinositide 3-OH kinase by the α6β4 integrin promotes carcinoma invasion
    • Shaw, L. M., I. Rabinovitz, H. H. Wang, A. Toker, and A. M. Mercurio. 1997. Activation of phosphoinositide 3-OH kinase by the α6β4 integrin promotes carcinoma invasion. Cell 91:949-960.
    • (1997) Cell , vol.91 , pp. 949-960
    • Shaw, L.M.1    Rabinovitz, I.2    Wang, H.H.3    Toker, A.4    Mercurio, A.M.5
  • 66
    • 0031858633 scopus 로고    scopus 로고
    • Integrin-mediated signaling events in human endothelial cells
    • Short, S. M., G. A. Talbott, and R. L. Juliano. 1998. Integrin-mediated signaling events in human endothelial cells. Mol. Biol. Cell 9:1969-1980.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1969-1980
    • Short, S.M.1    Talbott, G.A.2    Juliano, R.L.3
  • 69
    • 0029023145 scopus 로고
    • Ras CAAX peptidomimetic FTI 276 selectively blocks tumor growth in nude mice of a human lung carcinoma with K-Ras mutation and p53 deletion
    • Sun, J., Y. Qian, A. D. Hamilton, and S. M. Sebti. 1995. Ras CAAX peptidomimetic FTI 276 selectively blocks tumor growth in nude mice of a human lung carcinoma with K-Ras mutation and p53 deletion. Cancer Res. 55:4243-4247.
    • (1995) Cancer Res. , vol.55 , pp. 4243-4247
    • Sun, J.1    Qian, Y.2    Hamilton, A.D.3    Sebti, S.M.4
  • 70
    • 0032546264 scopus 로고    scopus 로고
    • Both farnesyltransferase and geranylgeranyltransferase I inhibitors are required for inhibition of oncogenic K-Ras prenylation but each alone is sufficient to suppress human tumor growth in nude mouse xenografts
    • Sun, J., Y. Qian, A. D. Hamilton, and S. M. Sebti. 1998. Both farnesyltransferase and geranylgeranyltransferase I inhibitors are required for inhibition of oncogenic K-Ras prenylation but each alone is sufficient to suppress human tumor growth in nude mouse xenografts. Oncogene 16:1467-1473.
    • (1998) Oncogene , vol.16 , pp. 1467-1473
    • Sun, J.1    Qian, Y.2    Hamilton, A.D.3    Sebti, S.M.4
  • 71
    • 0032417689 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors induce cytochrome c release and caspase 3 activation preferentially in transformed cells
    • Suzuki, N., J. Urano, and F. Tamanoi. 1998. Farnesyltransferase inhibitors induce cytochrome c release and caspase 3 activation preferentially in transformed cells. Proc. Natl. Acad. Sci. USA 95:15356-15361.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15356-15361
    • Suzuki, N.1    Urano, J.2    Tamanoi, F.3
  • 72
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and C. D'Souza-Schorey. 1997. Rho GTPases and signaling networks. Genes Dev. 11:2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 73
    • 0031948845 scopus 로고    scopus 로고
    • Protein kinase B activation and lamellipodium formation are independent phosphoinositide 3-kinase-mediated events differentially regulated by endogenous Ras
    • van Weering, D. H., J. de Rooij, B. Marte, J. Downward, J. L. Bos, and B. M. Burgering. 1998. Protein kinase B activation and lamellipodium formation are independent phosphoinositide 3-kinase-mediated events differentially regulated by endogenous Ras. Mol. Cell. Biol. 18:1802-1811.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1802-1811
    • Van Weering, D.H.1    De Rooij, J.2    Marte, B.3    Downward, J.4    Bos, J.L.5    Burgering, B.M.6
  • 74
    • 0027200883 scopus 로고
    • Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro
    • Warne, P. H., P. R. Viciana, and J. Downward. 1993. Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature 364:352-355.
    • (1993) Nature , vol.364 , pp. 352-355
    • Warne, P.H.1    Viciana, P.R.2    Downward, J.3
  • 75
    • 0021828496 scopus 로고
    • Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation
    • Whitman, M., D. R. Kaplan, B. Schaffhausen, L. Cantley, and T. M. Roberts. 1985. Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation. Nature 315:239-242.
    • (1985) Nature , vol.315 , pp. 239-242
    • Whitman, M.1    Kaplan, D.R.2    Schaffhausen, B.3    Cantley, L.4    Roberts, T.M.5
  • 77
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F. L., and P. J. Casey. 1996. Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65:241-269.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.