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Volumn 20, Issue 5, 2000, Pages 1507-1514

Caveolin 1-mediated regulation of receptor tyrosine kinase-associated phosphatidylinositol 3-kinase activity by ceramide

Author keywords

[No Author keywords available]

Indexed keywords

CAVEOLIN; CERAMIDE; PHOSPHATIDYLINOSITOL KINASE; PROTEIN TYROSINE KINASE;

EID: 0033965898     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.5.1507-1514.2000     Document Type: Article
Times cited : (166)

References (65)
  • 2
    • 0029551217 scopus 로고
    • Platelet-derived growth factor. Distinct signal transduction pathways associated with migration versus proliferation
    • Bornfeldt, K. E., E. W. Raines, L. M. Graves, M. P. Skinner, E. G. Krebs, and R. Ross. 1995. Platelet-derived growth factor. Distinct signal transduction pathways associated with migration versus proliferation. Ann. N. Y. Acad. Sci. 766:416-430.
    • (1995) Ann. N. Y. Acad. Sci. , vol.766 , pp. 416-430
    • Bornfeldt, K.E.1    Raines, E.W.2    Graves, L.M.3    Skinner, M.P.4    Krebs, E.G.5    Ross, R.6
  • 3
    • 0029148660 scopus 로고
    • Ceramide synthase mediates daunorubicin-induced apoptosis: An alternative mechanism for generating death signals
    • Bose, R., M. Verheij, A. Haimovitz-Friedman, K. Scotto, Z. Fuks, and R. Kolesnick. 1995. Ceramide synthase mediates daunorubicin-induced apoptosis: an alternative mechanism for generating death signals. Cell 82:405-414.
    • (1995) Cell , vol.82 , pp. 405-414
    • Bose, R.1    Verheij, M.2    Haimovitz-Friedman, A.3    Scotto, K.4    Fuks, Z.5    Kolesnick, R.6
  • 6
    • 0031944521 scopus 로고    scopus 로고
    • Down-regulation of Fas gene expression in colon cancer is not a result of allelic loss or gene rearrangement
    • Butler, L. M., P. J. Hewett, W. J. Butler, and P. A. Cowled. 1998. Down-regulation of Fas gene expression in colon cancer is not a result of allelic loss or gene rearrangement. Br. J. Cancer 77:1454-1459.
    • (1998) Br. J. Cancer , vol.77 , pp. 1454-1459
    • Butler, L.M.1    Hewett, P.J.2    Butler, W.J.3    Cowled, P.A.4
  • 7
    • 0033551070 scopus 로고    scopus 로고
    • New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway
    • Cantley, L. C., and B. G. Neel. 1999. New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc. Natl. Acad. Sci. USA 96:4240-4245.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4240-4245
    • Cantley, L.C.1    Neel, B.G.2
  • 10
    • 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
  • 11
    • 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
  • 12
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization
    • Diehl, J. A., M. Cheng, M. F. Roussel, and C. J. Sherr. 1998. Glycogen synthase kinase-3beta 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.2    Roussel, M.F.3    Sherr, C.J.4
  • 13
    • 0032577647 scopus 로고    scopus 로고
    • Caveolin-mediated regulation of signaling along the p42/44 MAP kinase cascade in vivo. A role for the caveolin-scaffolding domain
    • Engelman, J. A., C. Chu, A. Lin, H. Jo, T. Ikezu, T. Okamoto, D. S. Kohtz, and M. P. Lisanti. 1998. Caveolin-mediated regulation of signaling along the p42/44 MAP kinase cascade in vivo. A role for the caveolin-scaffolding domain. FEBS Lett. 428:205-211.
    • (1998) FEBS Lett. , vol.428 , pp. 205-211
    • Engelman, J.A.1    Chu, C.2    Lin, A.3    Jo, H.4    Ikezu, T.5    Okamoto, T.6    Kohtz, D.S.7    Lisanti, M.P.8
  • 14
    • 0026652899 scopus 로고
    • Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways
    • Fantl, W. J., J. A. Escobedo, G. A. Martin, C. W. Turck, M. del Rosario, F. McCormick, and L. T. Williams. 1992. Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways. Cell 69:413-423.
    • (1992) Cell , vol.69 , pp. 413-423
    • Fantl, W.J.1    Escobedo, J.A.2    Martin, G.A.3    Turck, C.W.4    Del Rosario, M.5    McCormick, F.6    Williams, L.T.7
  • 15
    • 0030753816 scopus 로고    scopus 로고
    • Lipid domains in the membrane: Thermotropic properties of sphingomyelin vesicles containing GM1 ganglioside and cholesterol
    • Ferraretto, A., M. Pitto, P. Palestini, and M. Masserini. 1997. Lipid domains in the membrane: thermotropic properties of sphingomyelin vesicles containing GM1 ganglioside and cholesterol. Biochemistry 36:9232-9236.
    • (1997) Biochemistry , vol.36 , pp. 9232-9236
    • Ferraretto, A.1    Pitto, M.2    Palestini, P.3    Masserini, M.4
  • 17
    • 0026033808 scopus 로고
    • Phosphatidylinositol-3 kinase is activated in v-src, v-yes, and v-fps transformed chicken embryo fibroblasts
    • Fukui, Y., A. R. Saltiel, and H. Hanafusa. 1991. Phosphatidylinositol-3 kinase is activated in v-src, v-yes, and v-fps transformed chicken embryo fibroblasts. Oncogene 6:407-411.
    • (1991) Oncogene , vol.6 , pp. 407-411
    • Fukui, Y.1    Saltiel, A.R.2    Hanafusa, H.3
  • 19
    • 0032516835 scopus 로고    scopus 로고
    • Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK)
    • Furuchi, T., and R. G. Anderson. 1998. Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK). J. Biol. Chem. 273:21099-21104.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21099-21104
    • Furuchi, T.1    Anderson, R.G.2
  • 20
    • 0032515945 scopus 로고    scopus 로고
    • Identification, sequence and developmental expression of invertebrate flotillins from Drosophila melanogaster
    • Galbiati, F., D. Volonte, J. S. Goltz, Z. Steele, J. Sen, J. Juresak, D. Stein, L. Stevens, and M. P. Lisanti. 1998. Identification, sequence and developmental expression of invertebrate flotillins from Drosophila melanogaster. Gene 210:229-237.
    • (1998) Gene , vol.210 , pp. 229-237
    • Galbiati, F.1    Volonte, D.2    Goltz, J.S.3    Steele, Z.4    Sen, J.5    Juresak, J.6    Stein, D.7    Stevens, L.8    Lisanti, M.P.9
  • 21
    • 0032538790 scopus 로고    scopus 로고
    • Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade
    • Galbiati, F., D. Volonte, J. A. Engelman, G. Watanabe, R. Burk, R. G. Pestell, and M. P. Lisanti. 1998. Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade. EMBO J. 17:6633-6648.
    • (1998) EMBO J. , vol.17 , pp. 6633-6648
    • Galbiati, F.1    Volonte, D.2    Engelman, J.A.3    Watanabe, G.4    Burk, R.5    Pestell, R.G.6    Lisanti, M.P.7
  • 22
    • 0033067693 scopus 로고    scopus 로고
    • The Npcl mutation causes an altered expression of caveolin-I, annexin II and protein kinases and phosphorylation of caveolin-I and annexin II in murine livers
    • Garver, W. S., G. S. Hossain, M. M. Winscott, and R. A. Heidenreich. 1999. The Npcl mutation causes an altered expression of caveolin-I, annexin II and protein kinases and phosphorylation of caveolin-I and annexin II in murine livers. Biochim. Biophys. Acta 1453:193-206.
    • (1999) Biochim. Biophys. Acta , vol.1453 , pp. 193-206
    • Garver, W.S.1    Hossain, G.S.2    Winscott, M.M.3    Heidenreich, R.A.4
  • 23
    • 0029844095 scopus 로고    scopus 로고
    • The E5 gene product of rhesus papillomavirus is an activator of endogenous Ras and phosphatidylinositol-3′-kinase in NIH 3T3 cells
    • Ghai, J., R. S. Ostrow, J. Tolar, R. C. McGlennen, T. D. Lemke, D. Tobolt, Z. Liu, and A. J. Faras. 1996. The E5 gene product of rhesus papillomavirus is an activator of endogenous Ras and phosphatidylinositol-3′-kinase in NIH 3T3 cells. Proc. Natl. Acad. Sci. USA 93:12879-12884.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12879-12884
    • Ghai, J.1    Ostrow, R.S.2    Tolar, J.3    McGlennen, R.C.4    Lemke, T.D.5    Tobolt, D.6    Liu, Z.7    Faras, A.J.8
  • 24
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: Emerging patterns from divergent signals
    • Giaccia, A. J., and M. B. Kastan. 1998. The complexity of p53 modulation: emerging patterns from divergent signals. Genes Dev. 12:2973-2983.
    • (1998) Genes Dev. , vol.12 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 25
    • 0028932435 scopus 로고
    • Association of phosphatidylinositol 3-kinase with SHC in chronic myelogcneous leukemia cells
    • Harrison-Findik, D., M. Susa, and L. Varticovski. 1995. Association of phosphatidylinositol 3-kinase with SHC in chronic myelogcneous leukemia cells. Oncogene 10:1385-1391.
    • (1995) Oncogene , vol.10 , pp. 1385-1391
    • Harrison-Findik, D.1    Susa, M.2    Varticovski, L.3
  • 28
    • 0023665111 scopus 로고
    • Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity
    • Kaplan, D. R., M. Whitman, B. Schaffhausen, D. C. Pallas, M. White, L. Cantley, and T. M. Roberts. 1987. Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity. Cell 50:1021-1029.
    • (1987) Cell , vol.50 , pp. 1021-1029
    • Kaplan, D.R.1    Whitman, M.2    Schaffhausen, B.3    Pallas, D.C.4    White, M.5    Cantley, L.6    Roberts, T.M.7
  • 30
    • 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
  • 31
    • 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
  • 32
    • 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
  • 33
    • 0031919157 scopus 로고    scopus 로고
    • Regulation of ceramide production and apoptosis
    • Kolesnick, R. N., and M. Kronke. 1998. Regulation of ceramide production and apoptosis. Annu. Rev. Physiol. 60:643-665.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 643-665
    • Kolesnick, R.N.1    Kronke, M.2
  • 35
    • 0031034574 scopus 로고    scopus 로고
    • Antiapoptolic signalling by the insulin-like growth factor I receptor, phosphatidylinositol 3-kinase, and Akt
    • Kulik, G., A. Klippel, and M. J. Weber. 1997. Antiapoptolic signalling by the insulin-like growth factor I receptor, phosphatidylinositol 3-kinase, and Akt. Mol. Cell. Biol. 17:1595-1606.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1595-1606
    • Kulik, G.1    Klippel, A.2    Weber, M.J.3
  • 36
    • 0023697978 scopus 로고
    • Tumor necrosis factor can induce both apoptic and necrotic forms of cell lysis
    • Laster, S. M., J. G. Wood, and L. R. Gooding. 1988. Tumor necrosis factor can induce both apoptic and necrotic forms of cell lysis. J. Immunol. 141: 2629-2634.
    • (1988) J. Immunol. , vol.141 , pp. 2629-2634
    • Laster, S.M.1    Wood, J.G.2    Gooding, L.R.3
  • 38
    • 0028784298 scopus 로고
    • Compartmentalized production of ceramide at the cell surface
    • Liu, P., and R. G. Anderson. 1995. Compartmentalized production of ceramide at the cell surface. J. Biol. Chem. 270:27179-27185.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27179-27185
    • Liu, P.1    Anderson, R.G.2
  • 39
    • 0029879507 scopus 로고    scopus 로고
    • Localization of platelet-derived growth factor-stimulated phosphorylation cascade to caveolae
    • Liu, P., Y. Ying, Y. G. Ko, and R. G. Anderson. 1996. Localization of platelet-derived growth factor-stimulated phosphorylation cascade to caveolae. J. Biol. Chem. 271:10299-10303.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10299-10303
    • Liu, P.1    Ying, Y.2    Ko, Y.G.3    Anderson, R.G.4
  • 40
    • 0027451668 scopus 로고
    • p53-dependent apoptosis modulates the cytotoxicity of anticancer agents
    • Lowe, S.W., H. E. Ruley, T. Jacks, and D. E. Housman. 1993. p53-dependent apoptosis modulates the cytotoxicity of anticancer agents. Cell 74:957-967.
    • (1993) Cell , vol.74 , pp. 957-967
    • Lowe, S.W.1    Ruley, H.E.2    Jacks, T.3    Housman, D.E.4
  • 41
    • 0030869787 scopus 로고    scopus 로고
    • Induction of vascular endothelial growth factor by hypoxia is modulated hy a phosphatidylinositol 3-kinase/Akt signaling pathway in Ha-ras-transformcd cells through a hypoxia inducible factor-1 transcriptional element
    • Mazure, N. M., E. Y. Chen, K. R. Laderoute, and A. J. Giaccia. 1997. Induction of vascular endothelial growth factor by hypoxia is modulated hy a phosphatidylinositol 3-kinase/Akt signaling pathway in Ha-ras-transformcd cells through a hypoxia inducible factor-1 transcriptional element. Blood 90:3322-3331.
    • (1997) Blood , vol.90 , pp. 3322-3331
    • Mazure, N.M.1    Chen, E.Y.2    Laderoute, K.R.3    Giaccia, A.J.4
  • 42
    • 0019350039 scopus 로고
    • Effect of low dose ionizing radiation on the murine pericryptal fibroblast sheath: Radiation damage in a mesenchymal system in vivo
    • Neal, J. V., and C. S. Potten. 1981. Effect of low dose ionizing radiation on the murine pericryptal fibroblast sheath: radiation damage in a mesenchymal system in vivo. Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. 39:175-183.
    • (1981) Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. , vol.39 , pp. 175-183
    • Neal, J.V.1    Potten, C.S.2
  • 44
    • 0030604280 scopus 로고    scopus 로고
    • Potent inhibition of angiogenesis by wortmannin, a fungal metabolite
    • Oikawa, T., and M. Shimamura. 1996. Potent inhibition of angiogenesis by wortmannin, a fungal metabolite. Eur. J. Pharmacol. 318:93-96.
    • (1996) Eur. J. Pharmacol. , vol.318 , pp. 93-96
    • Oikawa, T.1    Shimamura, M.2
  • 45
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins. A family of scaffolding proteins for organizing "preassemhled signaling complexes" at the plasma membrane
    • Okamoto, T., A. Schlegel, P. E. Scherer, and M. P. Lisanti. 1998. Caveolins. a family of scaffolding proteins for organizing "preassemhled signaling complexes" at the plasma membrane. J. Biol. Chem. 273:5419-5422.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 46
    • 0016681826 scopus 로고
    • Epidermal apoptosis: Cell deletion by phagocytosis
    • Olson, R. L., and M. A. Everett. 1975. Epidermal apoptosis: cell deletion by phagocytosis. J. Cutan. Pathol. 2:53-57.
    • (1975) J. Cutan. Pathol. , vol.2 , pp. 53-57
    • Olson, R.L.1    Everett, M.A.2
  • 47
    • 0032493729 scopus 로고    scopus 로고
    • Role of glycogen synthase kinase-3 in the phosphatidylinosilol 3-Kinase/Akt cell survival pathway
    • Pap, M., and G. M. Cooper. 1998. Role of glycogen synthase kinase-3 in the phosphatidylinosilol 3-Kinase/Akt cell survival pathway. J. Biol. Chem. 273: 19929-19932.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19929-19932
    • Pap, M.1    Cooper, G.M.2
  • 48
    • 0032497837 scopus 로고    scopus 로고
    • The role of ceramide in cell signaling
    • Perry, D. K., and Y. A. Hannun. 1998. The role of ceramide in cell signaling. Biochem. Biophys. Acta 1436:233-243.
    • (1998) Biochem. Biophys. Acta , vol.1436 , pp. 233-243
    • Perry, D.K.1    Hannun, Y.A.2
  • 49
    • 0032125580 scopus 로고    scopus 로고
    • Increased levels of phosphatidylinositol 3-kinase activity in colorectal tumors
    • Phillips, W. A., F. St. Clair, A. D. Munday, R. J. Thomas, and C. A. Mitchell. 1998. Increased levels of phosphatidylinositol 3-kinase activity in colorectal tumors. Cancer 83:41-47.
    • (1998) Cancer , vol.83 , pp. 41-47
    • Phillips, W.A.1    St. Clair, F.2    Munday, A.D.3    Thomas, R.J.4    Mitchell, C.A.5
  • 50
    • 0032575524 scopus 로고    scopus 로고
    • Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormone-stimulated phosphatidylinositol turnover
    • Pike, L. J., and J. M. Miller. 1998. Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormone-stimulated phosphatidylinositol turnover. J. Biol. Chem. 273:22298-22304.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22298-22304
    • Pike, L.J.1    Miller, J.M.2
  • 51
    • 0025602953 scopus 로고
    • Interaction of cholesterol with various glycerophospholipids and sphingomyelin
    • Sankaram, M. B., and T. E. Thompson. 1990. Interaction of cholesterol with various glycerophospholipids and sphingomyelin. Biochemistry 29:10670-10675.
    • (1990) Biochemistry , vol.29 , pp. 10670-10675
    • Sankaram, M.B.1    Thompson, T.E.2
  • 53
    • 0031765341 scopus 로고    scopus 로고
    • Role of plasmalemmal caveolae in signal transduction
    • Shaul, P. W., and R. G. Anderson. 1998. Role of plasmalemmal caveolae in signal transduction. Am. J. Physiol. 275:L843-L851.
    • (1998) Am. J. Physiol. , vol.275
    • Shaul, P.W.1    Anderson, R.G.2
  • 54
    • 0031456065 scopus 로고    scopus 로고
    • Activation of phosphoinositide 3-OH kinase by the alpha6heta4 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 alpha6heta4 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
  • 55
    • 0032143284 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: The key switch mechanism in insulin signalling
    • Shepherd, P. R., D. J. Withers, and K. Siddle. 1998. Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling. Biochem. J. 333:471-490.
    • (1998) Biochem. J. , vol.333 , pp. 471-490
    • Shepherd, P.R.1    Withers, D.J.2    Siddle, K.3
  • 58
    • 0031841949 scopus 로고    scopus 로고
    • Regulation of insulin-stimulated glucose transporter GLUT4 translocation and Akt kinase activity by ceramide
    • Summers, S. A., L. A. Garza, H. Zhou, and M. J. Birnbaum. 1998. Regulation of insulin-stimulated glucose transporter GLUT4 translocation and Akt kinase activity by ceramide. Mol. Cell. Biol. 18:5457-5464.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5457-5464
    • Summers, S.A.1    Garza, L.A.2    Zhou, H.3    Birnbaum, M.J.4
  • 59
    • 0024435351 scopus 로고
    • Phosphorylation of middle T by pp60c-src: A switch for binding of phosphatidylinositol 3-kinase and optimal tumorigenesis
    • Talmage, D. A., R. Freund, A. T. Young, J. Dahl, C. J. Dawe, and T. L. Benjamin. 1989. Phosphorylation of middle T by pp60c-src: a switch for binding of phosphatidylinositol 3-kinase and optimal tumorigenesis. Cell 59:55-65.
    • (1989) Cell , vol.59 , pp. 55-65
    • Talmage, D.A.1    Freund, R.2    Young, A.T.3    Dahl, J.4    Dawe, C.J.5    Benjamin, T.L.6
  • 61
    • 0028089005 scopus 로고
    • Membrane ruffling and chemotaxis transduced by the PDGF beta-receptor require the binding site for phosphatidylinositol 3′ kinase
    • Wennstrom, S., A. Siegbahn, K. Yokote, A. K. Arvidsson, C. H. Heldin, S. Mon, and L. Claesson-Welsh. 1994. Membrane ruffling and chemotaxis transduced by the PDGF beta-receptor require the binding site for phosphatidylinositol 3′ kinase. Oncogene 9:651-660.
    • (1994) Oncogene , vol.9 , pp. 651-660
    • Wennstrom, S.1    Siegbahn, A.2    Yokote, K.3    Arvidsson, A.K.4    Heldin, C.H.5    Mon, S.6    Claesson-Welsh, L.7
  • 62
    • 0023425731 scopus 로고
    • Evidence for two distinct phosphatidylinositol kinases in fibroblasts. Implications for cellular regulation
    • Whitman, M., D. Kaplan, T. Roberts, and L. Cantley. 1987. Evidence for two distinct phosphatidylinositol kinases in fibroblasts. Implications for cellular regulation. Biochem. J. 247:165-174.
    • (1987) Biochem. J. , vol.247 , pp. 165-174
    • Whitman, M.1    Kaplan, D.2    Roberts, T.3    Cantley, L.4
  • 63
    • 0028963084 scopus 로고
    • Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor
    • Yao, R., and G. M. Cooper. 1995. Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor. Science 267: 2003-2006.
    • (1995) Science , vol.267 , pp. 2003-2006
    • Yao, R.1    Cooper, G.M.2
  • 64
    • 0032569026 scopus 로고    scopus 로고
    • Inhibition of Akt kinase by cell-permeable ceramide and its implications for ceramide-induced apoptosis
    • Zhou, H., S. A. Summers, M. J. Birnbaum, and R. N. Pittman. 1998 Inhibition of Akt kinase by cell-permeable ceramide and its implications for ceramide-induced apoptosis. J. Biol. Chem. 273:16568-16575.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16568-16575
    • Zhou, H.1    Summers, S.A.2    Birnbaum, M.J.3    Pittman, R.N.4
  • 65
    • 0032128301 scopus 로고    scopus 로고
    • Inhibition of the anti-apoptotic PI(3)K/ Akt/Bad pathway by stress
    • Zundel, W., and A. Giaccia. 1998. Inhibition of the anti-apoptotic PI(3)K/ Akt/Bad pathway by stress. Genes Dev. 12:1941-1946.
    • (1998) Genes Dev. , vol.12 , pp. 1941-1946
    • Zundel, W.1    Giaccia, A.2


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