메뉴 건너뛰기




Volumn 7, Issue 8, 2006, Pages 606-619

The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE INHIBITOR; GEFITINIB; GLUCOSE; GLUCOSE TRANSPORTER 4; INSULIN; INSULIN RECEPTOR; MAMMALIAN TARGET OF RAPAMYCIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROTEIN BAD; PROTEIN INHIBITOR; PROTEIN KINASE B BETA; PROTEIN KINASE C INHIBITOR; PROTEIN KINASE C THETA; PROTEIN KINASE INHIBITOR; PROTEIN P110; PROTEIN P85; RAPAMYCIN; RAPAMYCIN DERIVATIVE; S6 KINASE; SCATTER FACTOR RECEPTOR; SOMATOMEDIN C RECEPTOR; STRESS ACTIVATED PROTEIN KINASE; STRESS ACTIVATED PROTEIN KINASE INHIBITOR; TRANSCRIPTION FACTOR FOXO;

EID: 33746257209     PISSN: 14710056     EISSN: 14710064     Source Type: Journal    
DOI: 10.1038/nrg1879     Document Type: Review
Times cited : (2755)

References (166)
  • 1
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley, L. C. The phosphoinositide 3-kinase pathway. Science 296, 1655-1657 (2002).
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 2
    • 0035190026 scopus 로고    scopus 로고
    • Cellular function of phosphoinositide 3-kinases: Implications for development, homeostasis, and cancer
    • Katso, R. et al. Cellular function of phosphoinositide 3-kinases: implications for development, homeostasis, and cancer. Annu. Rev. Cell Dev. Biol. 17, 615-675 (2001).
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 615-675
    • Katso, R.1
  • 3
    • 0037323892 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase γ: A key modulator in inflammation and allergy
    • Wymann, M. P. et al. Phosphoinositide 3-kinase γ: a key modulator in inflammation and allergy. Biochem. Soc. Trans. 31, 275-280 (2003).
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 275-280
    • Wymann, M.P.1
  • 4
    • 0030887632 scopus 로고    scopus 로고
    • The Gβγsensitivity of a PI3K is dependent upon a tightly associated adaptor, p101
    • Stephens, L. R. et al. The Gβγsensitivity of a PI3K is dependent upon a tightly associated adaptor, p101. Cell 89, 105-114 (1997).
    • (1997) Cell , vol.89 , pp. 105-114
    • Stephens, L.R.1
  • 5
    • 15744363780 scopus 로고    scopus 로고
    • p84, a new Gβγ-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110γ
    • Suire, S. et al. p84, a new Gβγ-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110γ. Curr. Biol. 15, 566-570 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 566-570
    • Suire, S.1
  • 6
    • 33744518663 scopus 로고    scopus 로고
    • PIKAP, a novel regulatory subunit of phosphoinositide 3-kinase γ that is highly expressed in heart and interacts with PDE3B
    • PIKAP, a novel regulatory subunit of phosphoinositide 3-kinase γ that is highly expressed in heart and interacts with PDE3B. J. Biol. Chem. 281, 9977-9986 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 9977-9986
    • Voigt, P.1    Dorner, M.B.2    Schaefer, M.3
  • 7
    • 0035103107 scopus 로고    scopus 로고
    • The class II phosphoinositide 3-kinase C2α is activated by clathrin and regulates clathrin-mediated membrane trafficking
    • Gaidarov, I., Smith, M. E., Domin, J. & Keen, J. H. The class II phosphoinositide 3-kinase C2α is activated by clathrin and regulates clathrin-mediated membrane trafficking. Mol. Cell 7, 443-149 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 443-1149
    • Gaidarov, I.1    Smith, M.E.2    Domin, J.3    Keen, J.H.4
  • 8
    • 0034194152 scopus 로고    scopus 로고
    • Phosphoinositide signaling and the regulation of membrane trafficking in yeast
    • Odorizzi, G., Babst, M. & Emr, S. D. Phosphoinositide signaling and the regulation of membrane trafficking in yeast. Trends Biochem. Sci. 25, 229-235 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 229-235
    • Odorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 9
    • 25444457577 scopus 로고    scopus 로고
    • hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase
    • Byfield, M. P., Murray, J. T. & Backer, J. M. hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase. J. Biol. Chem. 280, 33076-33082 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 33076-33082
    • Byfield, M.P.1    Murray, J.T.2    Backer, J.M.3
  • 10
    • 26444575415 scopus 로고    scopus 로고
    • Amino acids mediate mTOR/raptor signaling through activation of class 3 phosphatidylinositol 3OH-kinase
    • Nobukuni, T. et al. Amino acids mediate mTOR/raptor signaling through activation of class 3 phosphatidylinositol 3OH-kinase. Proc. Natl Acad. Sci. USA 102, 14238-14243 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 14238-14243
    • Nobukuni, T.1
  • 11
    • 0037135980 scopus 로고    scopus 로고
    • Novel PtdIns(3)P-binding protein Etf1 functions as an effector of the Vps34 PtdIns 3-kinase in autophagy
    • Wurmser, A. E. & Emr, S. D. Novel PtdIns(3)P-binding protein Etf1 functions as an effector of the Vps34 PtdIns 3-kinase in autophagy. J. Cell Biol. 158, 761-772 (2002).
    • (2002) J. Cell Biol. , vol.158 , pp. 761-772
    • Wurmser, A.E.1    Emr, S.D.2
  • 12
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae
    • Kihara, A., Noda, T., Ishihara, N. & Ohsumi, Y. Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J. Cell Biol. 152, 519-530 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 13
    • 0034794639 scopus 로고    scopus 로고
    • Prospects of phosphoinositide 3-kinase inhibition as a cancer treatment
    • Stein, R. Prospects of phosphoinositide 3-kinase inhibition as a cancer treatment. Endocr. Relat. Cancer 8, 237-248 (2001).
    • (2001) Endocr. Relat. Cancer , vol.8 , pp. 237-248
    • Stein, R.1
  • 15
    • 0026098352 scopus 로고
    • A novel protein kinase homolog essential for protein sorting to the yeast lysosome-like vacuole
    • Herman, P. K., Stack, J. H., DeModena, J. A. & Emr, S. D. A novel protein kinase homolog essential for protein sorting to the yeast lysosome-like vacuole. Cell 64, 425-437 (1991).
    • (1991) Cell , vol.64 , pp. 425-437
    • Herman, P.K.1    Stack, J.H.2    DeModena, J.A.3    Emr, S.D.4
  • 16
    • 0027256130 scopus 로고
    • A membrane-associated complex containing the Vps15 protein kinase and the Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole
    • Stack, J. H., Herman, P. K., Schu, P. V. & Emr, S. D. A membrane-associated complex containing the Vps15 protein kinase and the Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole. EMBO J. 12, 2195-2204 (1993).
    • (1993) EMBO J. , vol.12 , pp. 2195-2204
    • Stack, J.H.1    Herman, P.K.2    Schu, P.V.3    Emr, S.D.4
  • 17
    • 1542569606 scopus 로고    scopus 로고
    • Membrane recognition and targeting by lipid-binding domains
    • DiNitto, J. P., Cronin, T. C. & Lambright, D. G. Membrane recognition and targeting by lipid-binding domains. Sci. STKE 2003, re16 (2003).
    • (2003) Sci. STKE , vol.2003
    • DiNitto, J.P.1    Cronin, T.C.2    Lambright, D.G.3
  • 18
    • 0029148577 scopus 로고
    • Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells
    • Brown, W. J., DeWald, D. B., Emr, S. D., Plutner, H. & Balch, W. E. Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells. J. Cell Biol. 130, 781-796 (1995).
    • (1995) J. Cell Biol. , vol.130 , pp. 781-796
    • Brown, W.J.1    DeWald, D.B.2    Emr, S.D.3    Plutner, H.4    Balch, W.E.5
  • 19
    • 3342908518 scopus 로고    scopus 로고
    • A novel phosphatidylinositol(3,4,5)P3 pathway in fission yeast
    • Mitra, P. et al. A novel phosphatidylinositol(3,4,5)P3 pathway in fission yeast. J. Cell Biol. 166, 205-211 (2004).
    • (2004) J. Cell Biol. , vol.166 , pp. 205-211
    • Mitra, P.1
  • 20
    • 0023831256 scopus 로고
    • A mutation in the age-1 gene in Caenorhabditis elegans lengthens life and reduces hermaphrodite fertility
    • Friedman, D. B. & Johnson, T. E. A mutation in the age-1 gene in Caenorhabditis elegans lengthens life and reduces hermaphrodite fertility. Genetics 118, 75-86 (1988).
    • (1988) Genetics , vol.118 , pp. 75-86
    • Friedman, D.B.1    Johnson, T.E.2
  • 21
    • 0027771804 scopus 로고
    • A C. elegans mutant that lives twice as long as wild type
    • Kenyon, C., Chang, J., Gensch, E., Rudner, A. & Tabtiang, R. A C. elegans mutant that lives twice as long as wild type. Nature 366, 461-464 (1993).
    • (1993) Nature , vol.366 , pp. 461-464
    • Kenyon, C.1    Chang, J.2    Gensch, E.3    Rudner, A.4    Tabtiang, R.5
  • 22
    • 0346668317 scopus 로고    scopus 로고
    • Insulin receptor substrate and p55 orthologous adaptor proteins function in the Caenorhabditis elegans daf-2/insulin-like signaling pathway
    • Wolkow, C. A., Munoz, M. J., Riddle, D. L. & Ruvkun, G. Insulin receptor substrate and p55 orthologous adaptor proteins function in the Caenorhabditis elegans daf-2/insulin-like signaling pathway. J. Biol. Chem. 277, 49591-49597 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 49591-49597
    • Wolkow, C.A.1    Munoz, M.J.2    Riddle, D.L.3    Ruvkun, G.4
  • 23
    • 0032238299 scopus 로고    scopus 로고
    • The C. elegans PTEN homolog, DAF-18, acts in the insulin receptor-like metabolic signaling pathway
    • Ogg, S. & Ruvkun, G. The C. elegans PTEN homolog, DAF-18, acts in the insulin receptor-like metabolic signaling pathway. Mol. Cell 2, 887-893 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 887-893
    • Ogg, S.1    Ruvkun, G.2
  • 24
    • 0034626747 scopus 로고    scopus 로고
    • Genetic pathways that regulate ageing in model organisms
    • Guarente, L. & Kenyon, C. Genetic pathways that regulate ageing in model organisms. Nature 408, 255-262 (2000).
    • (2000) Nature , vol.408 , pp. 255-262
    • Guarente, L.1    Kenyon, C.2
  • 25
    • 0037306190 scopus 로고    scopus 로고
    • Insulin/IGF and target of rapamycin signaling: A TOR de force in growth control
    • Oldnam, S. & Hafen, E. Insulin/IGF and target of rapamycin signaling: a TOR de force in growth control. Trends Cell Biol. 13, 79-85 (2003).
    • (2003) Trends Cell Biol. , vol.13 , pp. 79-85
    • Oldnam, S.1    Hafen, E.2
  • 26
    • 5344224052 scopus 로고    scopus 로고
    • Temporal control of differentiation by the insulin receptor/tor pathway in Drosophila
    • Bateman, J. M. & McNeill, H. Temporal control of differentiation by the insulin receptor/tor pathway in Drosophila. Cell 119, 87-96 (2004).
    • (2004) Cell , vol.119 , pp. 87-96
    • Bateman, J.M.1    McNeill, H.2
  • 27
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
    • Inoki, K., Li, Y., Zhu, T., Wu, J. & Guan, K. L. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nature Cell Biol. 4, 648-657 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.L.5
  • 28
    • 0036714127 scopus 로고    scopus 로고
    • Akt regulates growth by directly phosphorylating Tsc2
    • Potter, C. J., Pedraza, L. G. & Xu, T. Akt regulates growth by directly phosphorylating Tsc2. Nature Cell Biol. 4, 658-665 (2002). References 27 and 28, along with the study in reference 115, show that AKT regulates mTOR activity by directly phosphorylating tuberin.
    • (2002) Nature Cell Biol. , vol.4 , pp. 658-665
    • Potter, C.J.1    Pedraza, L.G.2    Xu, T.3
  • 29
    • 0242539698 scopus 로고    scopus 로고
    • The Drosophila forkhead transcription factor FOXO mediates the reduction in cell number associated with reduced insulin signaling
    • Junger, M. A. et al. The Drosophila forkhead transcription factor FOXO mediates the reduction in cell number associated with reduced insulin signaling. J. Biol. 2, 20 (2003).
    • (2003) J. Biol. , vol.2 , pp. 20
    • Junger, M.A.1
  • 30
    • 33244464562 scopus 로고    scopus 로고
    • Critical nodes in signalling pathways: Insights into insulin action
    • Taniguchi, C. M., Emanuelli, B. & Kahn, C. R. Critical nodes in signalling pathways: insights into insulin action. Nature Rev. Mol. Cell Biol. 7, 85-96 (2006).
    • (2006) Nature Rev. Mol. Cell Biol. , vol.7 , pp. 85-96
    • Taniguchi, C.M.1    Emanuelli, B.2    Kahn, C.R.3
  • 31
    • 0041845231 scopus 로고    scopus 로고
    • Use of RNA interference-mediated gene silencing and adenoviral overexpression to elucidate the roles of AKT/protein kinase B isoforms in insulin actions
    • Katome, T. et al. Use of RNA interference-mediated gene silencing and adenoviral overexpression to elucidate the roles of AKT/protein kinase B isoforms in insulin actions. J. Biol. Chem. 278, 28312-28323 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 28312-28323
    • Katome, T.1
  • 32
    • 8744305112 scopus 로고    scopus 로고
    • Analysis of insulin signalling by RNAi-based gene silencing
    • Zhou, Q. L. et al. Analysis of insulin signalling by RNAi-based gene silencing. Biochem. Soc. Trans. 32, 817-821 (2004).
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 817-821
    • Zhou, Q.L.1
  • 33
    • 24044468429 scopus 로고    scopus 로고
    • Turning signals on and off: GLUT4 traffic in the insulin-signaling highway
    • Thong, F. S., Dugani, C. B. & Klip, A. Turning signals on and off: GLUT4 traffic in the insulin-signaling highway. Physiology (Bethesda) 20, 271-284 (2005).
    • (2005) Physiology (Bethesda) , vol.20 , pp. 271-284
    • Thong, F.S.1    Dugani, C.B.2    Klip, A.3
  • 34
    • 14144250240 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase catalytic subunit deletion and regulatory subunit deletion have opposite effects on insulin sensitivity in mice
    • Brachmann, S. M., Ueki, K., Engelman, J. A., Kahn, R. C. & Cantley, L. C. Phosphoinositide 3-kinase catalytic subunit deletion and regulatory subunit deletion have opposite effects on insulin sensitivity in mice. Mol. Cell. Biol. 25, 1596-1607 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1596-1607
    • Brachmann, S.M.1    Ueki, K.2    Engelman, J.A.3    Kahn, R.C.4    Cantley, L.C.5
  • 35
    • 33744990592 scopus 로고    scopus 로고
    • Critical role for the p110α phosphoinositide-3-OH kinase in growth and metabolic regulation
    • Foukas, L. C. et al. Critical role for the p110α phosphoinositide-3-OH kinase in growth and metabolic regulation. Nature 441, 366-370 (2006).
    • (2006) Nature , vol.441 , pp. 366-370
    • Foukas, L.C.1
  • 36
    • 14844340146 scopus 로고    scopus 로고
    • Insulin hypersensitivity and resistance to streptozotocin-induced diabetes in mice lacking PTEN in adipose tissue
    • Kurlawalla-Martinez, C. et al. Insulin hypersensitivity and resistance to streptozotocin-induced diabetes in mice lacking PTEN in adipose tissue. Mol. Cell. Biol. 25, 2498-2510 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2498-2510
    • Kurlawalla-Martinez, C.1
  • 37
    • 0346220260 scopus 로고    scopus 로고
    • Positive and negative roles of p85a and p85β regulatory subunits of phosphoinositide 3-kinase in insulin signaling
    • Ueki, K. et al. Positive and negative roles of p85a and p85β regulatory subunits of phosphoinositide 3-kinase in insulin signaling. J. Biol. Chem. 278, 48453-48466 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 48453-48466
    • Ueki, K.1
  • 38
    • 23744456586 scopus 로고    scopus 로고
    • The p85 regulatory subunit of phosphoinositide 3-kinase down-regulates IRS-1 signaling via the formation of a sequestration complex
    • Luo, J., Field, S. J., Lee, J. Y., Engelman, J. A. & Cantley, L. C. The p85 regulatory subunit of phosphoinositide 3-kinase down-regulates IRS-1 signaling via the formation of a sequestration complex. J. Cell Biol. 170, 455-464 (2005).
    • (2005) J. Cell Biol. , vol.170 , pp. 455-464
    • Luo, J.1    Field, S.J.2    Lee, J.Y.3    Engelman, J.A.4    Cantley, L.C.5
  • 39
    • 33646485943 scopus 로고    scopus 로고
    • A PI3K signaling in muscle leads to impaired muscle growth, insulin response, and hyperlipidemia
    • A PI3K signaling in muscle leads to impaired muscle growth, insulin response, and hyperlipidemia. Cell Metab. 3, 355-366 (2006).
    • (2006) Cell Metab. , vol.3 , pp. 355-366
    • Luo, J.1
  • 40
    • 33646148946 scopus 로고    scopus 로고
    • Divergent regulation of hepatic glucose and lipid metabolism by phosphoinositide 3-kinase via Akt and PKCλ/ζ
    • Taniguchi, C. M. et al. Divergent regulation of hepatic glucose and lipid metabolism by phosphoinositide 3-kinase via Akt and PKCλ/ζ. Cell Metab. 3, 343-353 (2006).
    • (2006) Cell Metab. , vol.3 , pp. 343-353
    • Taniguchi, C.M.1
  • 41
    • 0035856949 scopus 로고    scopus 로고
    • Insulin signalling and the regulation of glucose and lipid metabolism
    • Saltiel, A. R. & Kahn, C. R. Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414, 799-806 (2001).
    • (2001) Nature , vol.414 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 42
    • 4544386330 scopus 로고    scopus 로고
    • Unraveling the cellular mechanism of insulin resistance in humans: New insights from magnetic resonance spectroscopy
    • Shulman, G. I. Unraveling the cellular mechanism of insulin resistance in humans: new insights from magnetic resonance spectroscopy. Physiology (Bethesda) 19, 183-190 (2004).
    • (2004) Physiology (Bethesda) , vol.19 , pp. 183-190
    • Shulman, G.I.1
  • 43
    • 0031046812 scopus 로고    scopus 로고
    • Identification of a common amino acid polymorphism in the p85α regulatory subunit of phosphatidylinositol 3-kinase: Effects on glucose disappearance constant, glucose effectiveness, and the insulin sensitivity index
    • Hansen, T. et al. Identification of a common amino acid polymorphism in the p85α regulatory subunit of phosphatidylinositol 3-kinase: effects on glucose disappearance constant, glucose effectiveness, and the insulin sensitivity index. Diabetes 46, 494-501 (1997).
    • (1997) Diabetes , vol.46 , pp. 494-501
    • Hansen, T.1
  • 44
    • 4243062602 scopus 로고    scopus 로고
    • Candidate gene association study in type 1 diabetes indicates a role for genes involved in β-cell function as well as insulin action
    • Barroso, I. et al. Candidate gene association study in type 1 diabetes indicates a role for genes involved in β-cell function as well as insulin action. PLoS Biol. 1, e20 (2003).
    • (2003) PLoS Biol. , vol.1
    • Barroso, I.1
  • 45
    • 1442348156 scopus 로고    scopus 로고
    • Human placental growth hormone increases expression of the p85 regulatory unit of phosphatidylinositol 3-kinase and triggers severe insulin resistance in skeletal muscle
    • Barbour, L. A. et al. Human placental growth hormone increases expression of the p85 regulatory unit of phosphatidylinositol 3-kinase and triggers severe insulin resistance in skeletal muscle. Endocrinology 145, 1144-1150 (2004).
    • (2004) Endocrinology , vol.145 , pp. 1144-1150
    • Barbour, L.A.1
  • 46
    • 27844460627 scopus 로고    scopus 로고
    • Increased p85α is a potent negative regulator of skeletal muscle insulin signaling and induces in vivo insulin resistance associated with growth hormone excess
    • Barbour, L. et al. Increased p85α is a potent negative regulator of skeletal muscle insulin signaling and induces in vivo insulin resistance associated with growth hormone excess. J. Biol. Chem. 280, 37489-37494 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 37489-37494
    • Barbour, L.1
  • 47
    • 4544324637 scopus 로고    scopus 로고
    • Reversal of insulin resistance postpartum is linked to enhanced skeletal muscle insulin signaling
    • Kirwan, J. P. et al. Reversal of insulin resistance postpartum is linked to enhanced skeletal muscle insulin signaling. J. Clin. Endocrinol. Metab. 89, 4678-4684 (2004).
    • (2004) J. Clin. Endocrinol. Metab. , vol.89 , pp. 4678-4684
    • Kirwan, J.P.1
  • 48
    • 23644448924 scopus 로고    scopus 로고
    • Increased p85/55/50 expression and decreased phosphotidylinositol 3-kinase activity in insulin-resistant human skeletal muscle
    • Bandyopadhyay, G., Yu, J., Ofrecio, J. & Olefsky, J. Increased p85/55/50 expression and decreased phosphotidylinositol 3-kinase activity in insulin-resistant human skeletal muscle. Diabetes 54, 2351-2359 (2005).
    • (2005) Diabetes , vol.54 , pp. 2351-2359
    • Bandyopadhyay, G.1    Yu, J.2    Ofrecio, J.3    Olefsky, J.4
  • 49
    • 14544271905 scopus 로고    scopus 로고
    • Positive and negative regulation of insulin signaling through IRS-1 phosphorylation
    • Gual, P., Le Marchand-Brustel, Y. & Tanti, J. Positive and negative regulation of insulin signaling through IRS-1 phosphorylation. Biochimie 87, 99-109 (2005).
    • (2005) Biochimie , vol.87 , pp. 99-109
    • Gual, P.1    Le Marchand-Brustel, Y.2    Tanti, J.3
  • 50
    • 0035368548 scopus 로고    scopus 로고
    • Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKBβ)
    • Cho, H. et al. Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKBβ). Science 292, 1728-1731 (2001).
    • (2001) Science , vol.292 , pp. 1728-1731
    • Cho, H.1
  • 51
    • 2542528670 scopus 로고    scopus 로고
    • A family with severe insulin resistance and diabetes due to a mutation in AKT2
    • George, S. et al. A family with severe insulin resistance and diabetes due to a mutation in AKT2. Science 304, 1325-1328 (2004).
    • (2004) Science , vol.304 , pp. 1325-1328
    • George, S.1
  • 52
    • 33646383684 scopus 로고    scopus 로고
    • A pharmacological map of the PI3-K family defines a role for p110α in insulin signaling
    • Knight, Z. A. et al. A pharmacological map of the PI3-K family defines a role for p110α in insulin signaling. Cell 125, 733-747 (2006).
    • (2006) Cell , vol.125 , pp. 733-747
    • Knight, Z.A.1
  • 54
    • 0027496895 scopus 로고
    • Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r)
    • Liu, J. P., Baker, J., Perkins, A. S., Robertson, E. J. & Efstratiadis, A. Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r). Cell 75, 59-72 (1993).
    • (1993) Cell , vol.75 , pp. 59-72
    • Liu, J.P.1    Baker, J.2    Perkins, A.S.3    Robertson, E.J.4    Efstratiadis, A.5
  • 55
    • 0035742583 scopus 로고    scopus 로고
    • Insulin and insulin-like growth factor I receptors: Similarities and differences in signal transduction
    • Dupont, J. & LeRoith, D. Insulin and insulin-like growth factor I receptors: similarities and differences in signal transduction. Horm. Res. 55 (Suppl. 2), 22-26 (2001).
    • (2001) Horm. Res. , vol.55 , Issue.2 SUPPL. , pp. 22-26
    • Dupont, J.1    LeRoith, D.2
  • 56
    • 10744223902 scopus 로고    scopus 로고
    • The insulin-like growth factor 1 receptor induces physiological heart growth via the phosphoinositide 3-kinase(p110α) pathway
    • McMullen, J. R. et al. The insulin-like growth factor 1 receptor induces physiological heart growth via the phosphoinositide 3-kinase(p110α) pathway. J. Biol. Chem. 279, 4782-4793 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 4782-4793
    • McMullen, J.R.1
  • 57
    • 0034213075 scopus 로고    scopus 로고
    • The conserved phosphoinositide 3-kinase pathway determines heart size in mice
    • Shioi, T. et al. The conserved phosphoinositide 3-kinase pathway determines heart size in mice. EMBO J. 19, 2537-2548 (2000).
    • (2000) EMBO J. , vol.19 , pp. 2537-2548
    • Shioi, T.1
  • 58
    • 0036200937 scopus 로고    scopus 로고
    • Akt/protein kinase B promotes organ growth in transgenic mice
    • Shioi, T. et al. Akt/protein kinase B promotes organ growth in transgenic mice. Mol. Cell. Biol. 22, 2799-2809 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2799-2809
    • Shioi, T.1
  • 59
    • 27144536566 scopus 로고    scopus 로고
    • A phosphoinositide 3-kinase regulates heart size and physiological cardiac hypertrophy
    • A phosphoinositide 3-kinase regulates heart size and physiological cardiac hypertrophy. Mol. Cell. Biol. 25, 9491-9502 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9491-9502
    • Luo, J.1
  • 60
    • 0035733762 scopus 로고    scopus 로고
    • Deletion of Pten in mouse brain causes seizures, ataxia and defects in soma size resembling Lhermitte-Duclos disease
    • Backman, S. A. et al. Deletion of Pten in mouse brain causes seizures, ataxia and defects in soma size resembling Lhermitte-Duclos disease. Nature Genet. 29, 396-403 (2001).
    • (2001) Nature Genet. , vol.29 , pp. 396-403
    • Backman, S.A.1
  • 61
    • 0035824396 scopus 로고    scopus 로고
    • Negative regulation of neural stem/ progenitor cell proliferation by the Pten tumor suppressor gene in vivo
    • Groszer, M. et al. Negative regulation of neural stem/ progenitor cell proliferation by the Pten tumor suppressor gene in vivo. Science 294, 2186-2189 (2001).
    • (2001) Science , vol.294 , pp. 2186-2189
    • Groszer, M.1
  • 62
    • 9344259718 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors
    • Kwon, J. et al. Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. Proc. Natl Acad. Sci. USA 101, 16419-16424 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 16419-16424
    • Kwon, J.1
  • 63
    • 18644372367 scopus 로고    scopus 로고
    • Regulation of myocardial contractility and cell size by distinct PI3K-PTEN signaling pathways
    • Crackower, M. A. et al. Regulation of myocardial contractility and cell size by distinct PI3K-PTEN signaling pathways. Cell 110, 737-749 (2002).
    • (2002) Cell , vol.110 , pp. 737-749
    • Crackower, M.A.1
  • 64
    • 2342466109 scopus 로고    scopus 로고
    • Physiological functions of protein kinase B/Akt
    • Yang, Z. Z. et al. Physiological functions of protein kinase B/Akt. Biochem. Soc. Trans. 32, 350-354 (2004).
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 350-354
    • Yang, Z.Z.1
  • 65
    • 0011168670 scopus 로고
    • Evidence that the Rous sarcoma virus transforming gene product phosphorylates phosphatidylinositol and diacylglycerol
    • Sugimoto, Y., Whitman, M., Cantley, L. C. & Erikson, R. L. Evidence that the Rous sarcoma virus transforming gene product phosphorylates phosphatidylinositol and diacylglycerol. Proc. Natl Acad. Sci. USA 81, 2117-2121 (1984).
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 2117-2121
    • Sugimoto, Y.1    Whitman, M.2    Cantley, L.C.3    Erikson, R.L.4
  • 66
    • 0021828496 scopus 로고
    • Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation
    • Whitman, M., Kaplan, D. R., Schaffhausen, B., Cantley, L. & Roberts, T. M. Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation. Nature 315, 239-242 (1985).
    • (1985) Nature , vol.315 , pp. 239-242
    • Whitman, M.1    Kaplan, D.R.2    Schaffhausen, B.3    Cantley, L.4    Roberts, T.M.5
  • 67
    • 0025027872 scopus 로고
    • Production of novel polyphosphoinositides in vivo is linked to cell transformation by polyomavirus middle T antigen
    • Serunian, L. A., Auger, K. R., Roberts, T. M. & Cantley, L. C. Production of novel polyphosphoinositides in vivo is linked to cell transformation by polyomavirus middle T antigen. J. Virol. 64, 4718-4725 (1990).
    • (1990) J. Virol. , vol.64 , pp. 4718-4725
    • Serunian, L.A.1    Auger, K.R.2    Roberts, T.M.3    Cantley, L.C.4
  • 68
    • 0000440912 scopus 로고    scopus 로고
    • Transformation of chicken cells by the gene encoding the catalytic subunit of PI 3-kinase
    • Chang, H. W. et al. Transformation of chicken cells by the gene encoding the catalytic subunit of PI 3-kinase. Science 276, 1848-1850 (1997).
    • (1997) Science , vol.276 , pp. 1848-1850
    • Chang, H.W.1
  • 69
    • 0030936323 scopus 로고    scopus 로고
    • PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer
    • Li, J. et al. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science 275, 1943-1947 (1997).
    • (1997) Science , vol.275 , pp. 1943-1947
    • Li, J.1
  • 70
    • 17144436629 scopus 로고    scopus 로고
    • Identification of a candidate tumour suppressor gene. MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers
    • Steck, P. A. et al. Identification of a candidate tumour suppressor gene. MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers. Nature Genet. 15, 356-362 (1997). References 69 and 70 identify PTEN as a candidate tumour suppressor.
    • (1997) Nature Genet. , vol.15 , pp. 356-362
    • Steck, P.A.1
  • 71
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • 3.
    • (1998) J. Biol. Chem. , vol.275 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 72
    • 4344602002 scopus 로고    scopus 로고
    • The biology and clinical relevance of the PTEN tumor suppressor pathway
    • Sansal, I. & Sellers, W. R. The biology and clinical relevance of the PTEN tumor suppressor pathway. J. Clin. Oncol. 22, 2954-2963 (2004).
    • (2004) J. Clin. Oncol. , vol.22 , pp. 2954-2963
    • Sansal, I.1    Sellers, W.R.2
  • 73
    • 4243110417 scopus 로고    scopus 로고
    • Pten dose dictates cancer progression in the prostate
    • Trotman, L. C. et al. Pten dose dictates cancer progression in the prostate. PLoS Biol. 1, e59 (2003).
    • (2003) PLoS Biol. , vol.1
    • Trotman, L.C.1
  • 74
    • 1342342989 scopus 로고    scopus 로고
    • Human cancer, PTEN and the PI-3 kinase pathway
    • Parsons, R. Human cancer, PTEN and the PI-3 kinase pathway. Semin. Cell Dev. Biol. 15, 171-176 (2004).
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 171-176
    • Parsons, R.1
  • 75
    • 10744222860 scopus 로고    scopus 로고
    • Prostate-specific deletion of the murine Pten tumor suppressor gene leads to metastatic prostate cancer
    • Wang, S. et al. Prostate-specific deletion of the murine Pten tumor suppressor gene leads to metastatic prostate cancer. Cancer Cell 4, 209-221 (2003).
    • (2003) Cancer Cell , vol.4 , pp. 209-221
    • Wang, S.1
  • 77
    • 0034995242 scopus 로고    scopus 로고
    • T cell-specific loss of Pten leads to defects in central and peripheral tolerance
    • Suzuki, A. et al. T cell-specific loss of Pten leads to defects in central and peripheral tolerance. Immunity 14, 523-554 (2001).
    • (2001) Immunity , vol.14 , pp. 523-554
    • Suzuki, A.1
  • 78
    • 11144358645 scopus 로고    scopus 로고
    • High frequency of mutations of the PIK3CA gene in human cancers
    • Samuels, Y. et al. High frequency of mutations of the PIK3CA gene in human cancers. Science 304, 554 (2004). Reports the discovery that somatic mutations in the PIK3CA gene are a common event in human cancers.
    • (2004) Science , vol.304 , pp. 554
    • Samuels, Y.1
  • 79
    • 28844448182 scopus 로고    scopus 로고
    • Oncogenic PI3K deregulates transcription and translation
    • Bader, A. G., Kang, S., Zhao, L. & Vogt, P. K. Oncogenic PI3K deregulates transcription and translation. Nature Rev. Cancer 5, 921-929 (2005).
    • (2005) Nature Rev. Cancer , vol.5 , pp. 921-929
    • Bader, A.G.1    Kang, S.2    Zhao, L.3    Vogt, P.K.4
  • 80
    • 14144252004 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic
    • Kang, S., Bader, A. G. & Vogt, P. K. Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic. Proc. Natl Acad. Sci. USA 102, 802-807 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 802-807
    • Kang, S.1    Bader, A.G.2    Vogt, P.K.3
  • 81
    • 28244479028 scopus 로고    scopus 로고
    • Breast cancer-associated PIK3CA mutations are oncogenic in mammary epithelial cells
    • Isakoff, S. J. et al. Breast cancer-associated PIK3CA mutations are oncogenic in mammary epithelial cells. Cancer Res. 65, 10992-11000 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 10992-11000
    • Isakoff, S.J.1
  • 82
    • 20444374445 scopus 로고    scopus 로고
    • Mutant PIK3CA promotes cell growth and invasion of human cancer cells
    • Samuels, Y. et al. Mutant PIK3CA promotes cell growth and invasion of human cancer cells. Cancer Cell 7, 561-573 (2005).
    • (2005) Cancer Cell , vol.7 , pp. 561-573
    • Samuels, Y.1
  • 83
    • 29444449785 scopus 로고    scopus 로고
    • The oncogenic properties of p110α and p110β phosphatidylinositol 3-kinases in human mammary epithelial cells
    • Zhao, J. J. et al. The oncogenic properties of p110α and p110β phosphatidylinositol 3-kinases in human mammary epithelial cells. Proc. Natl Acad. Sci. USA 102, 18443-18448 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18443-18448
    • Zhao, J.J.1
  • 84
    • 0029127042 scopus 로고
    • Molecular alterations of the AKT2 oncogene in ovarian and breast carcinomas
    • Bellacosa, A. et al. Molecular alterations of the AKT2 oncogene in ovarian and breast carcinomas. Int. J. Cancer 64, 280-285 (1995).
    • (1995) Int. J. Cancer , vol.64 , pp. 280-285
    • Bellacosa, A.1
  • 85
    • 0001457668 scopus 로고    scopus 로고
    • Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA
    • Cheng, J. et al. Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA. Proc. Natl Acad. Sci. USA 93, 3636-3641 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 3636-3641
    • Cheng, J.1
  • 86
    • 0031936947 scopus 로고    scopus 로고
    • Amplification and overexpression of the AKT2 oncogene in a subset of human pancreatic ductal adenocarcinomas
    • Ruggeri, B., Huang, L., Wood, M., Cheng, J. & Testa, J. Amplification and overexpression of the AKT2 oncogene in a subset of human pancreatic ductal adenocarcinomas. Mol. Carcinog. 21, 81-86 (1998).
    • (1998) Mol. Carcinog. , vol.21 , pp. 81-86
    • Ruggeri, B.1    Huang, L.2    Wood, M.3    Cheng, J.4    Testa, J.5
  • 87
    • 23844445836 scopus 로고    scopus 로고
    • Colorectal cancer: Mutations in a signalling pathway
    • Parsons, D. W. et al. Colorectal cancer: mutations in a signalling pathway. Nature 436, 792 (2005).
    • (2005) Nature , vol.436 , pp. 792
    • Parsons, D.W.1
  • 88
    • 0037108151 scopus 로고    scopus 로고
    • Lethality of Drosophila lacking TSC tumor suppressor function rescued by reducing dS6K signaling
    • Radimerski, T., Montagne, J., Hemmings-Mieszczak, M. & Thomas, G. Lethality of Drosophila lacking TSC tumor suppressor function rescued by reducing dS6K signaling. Genes Dev. 16, 2627-2632 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 2627-2632
    • Radimerski, T.1    Montagne, J.2    Hemmings-Mieszczak, M.3    Thomas, G.4
  • 89
    • 8444224619 scopus 로고    scopus 로고
    • Balancing Akt with S6K: Implications for both metabolic diseases and tumorigenesis
    • Manning, B. D. Balancing Akt with S6K: implications for both metabolic diseases and tumorigenesis. J. Cell Biol. 167, 399-403 (2004).
    • (2004) J. Cell Biol. , vol.167 , pp. 399-403
    • Manning, B.D.1
  • 90
    • 11844304072 scopus 로고    scopus 로고
    • Restraining PI3K: MTOR signalling goes back to the membrane
    • Harrington, L. S., Findlay, G. M. & Lamb, R. F. Restraining PI3K: mTOR signalling goes back to the membrane. Trends Biochem. Sci. 30, 35-42 (2005).
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 35-42
    • Harrington, L.S.1    Findlay, G.M.2    Lamb, R.F.3
  • 92
    • 0037153158 scopus 로고    scopus 로고
    • A central role for JNK in obesity and insulin resistance
    • Hirosumi, J. et al. A central role for JNK in obesity and insulin resistance. Nature 420, 333-336 (2002).
    • (2002) Nature , vol.420 , pp. 333-336
    • Hirosumi, J.1
  • 93
    • 8544244084 scopus 로고    scopus 로고
    • PKC-β knockout mice are protected from fat-induced insulin resistance
    • Kim, J. et al. PKC-β knockout mice are protected from fat-induced insulin resistance. J. Clin. Invest. 114, 823-827 (2004).
    • (2004) J. Clin. Invest. , vol.114 , pp. 823-827
    • Kim, J.1
  • 94
    • 4544220704 scopus 로고    scopus 로고
    • Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
    • Um, S. H. et al. Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity. Nature 431, 200-205 (2004).
    • (2004) Nature , vol.431 , pp. 200-205
    • Um, S.H.1
  • 95
    • 23744516268 scopus 로고    scopus 로고
    • Feedback inhibition of Akt signaling limits the growth of tumors lacking Tsc2
    • Manning, B. D. et al. Feedback inhibition of Akt signaling limits the growth of tumors lacking Tsc2. Genes Dev. 19, 1773-1778 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 1773-1778
    • Manning, B.D.1
  • 96
    • 32944457518 scopus 로고    scopus 로고
    • MTOR inhibition induces upstream receptor tyrosine kinase signaling and activates Akt
    • O'Reilly, K. E. et al. mTOR inhibition induces upstream receptor tyrosine kinase signaling and activates Akt. Cancer Res. 66, 1500-1508 (2006).
    • (2006) Cancer Res. , vol.66 , pp. 1500-1508
    • O'Reilly, K.E.1
  • 97
    • 14844366111 scopus 로고    scopus 로고
    • ErbB-3 mediates phosphoinositide 3-kinase activity in gefitinib-sensitive non-small cell lung cancer cell lines
    • Engelman, J. A. et al. ErbB-3 mediates phosphoinositide 3-kinase activity in gefitinib-sensitive non-small cell lung cancer cell lines. Proc. Natl Acad. Sci. USA 102, 3788-3793 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 3788-3793
    • Engelman, J.A.1
  • 98
    • 7044230885 scopus 로고    scopus 로고
    • Possible novel therapy for diabetes with cell-permeable JNK-inhibitory peptide
    • Kaneto, H. et al. Possible novel therapy for diabetes with cell-permeable JNK-inhibitory peptide. Nature Med. 10, 1128-1132 (2004).
    • (2004) Nature Med. , vol.10 , pp. 1128-1132
    • Kaneto, H.1
  • 99
    • 2342537099 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase γ: Kinase-dependent and -independent activities in cardiovascular function and disease
    • Alloatti, G., Montrucchio, G., Lembo, G. & Hirsch, E. Phosphoinositide 3-kinase γ: kinase-dependent and -independent activities in cardiovascular function and disease. Biochem. Soc. Trans. 32, 383-386 (2004).
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 383-386
    • Alloatti, G.1    Montrucchio, G.2    Lembo, G.3    Hirsch, E.4
  • 100
    • 13844317894 scopus 로고    scopus 로고
    • EGFR mutation and resistance of non-small-cell lung cancer to gefitinib
    • Kobayashi, S. et al. EGFR mutation and resistance of non-small-cell lung cancer to gefitinib. N. Engl. J. Med. 352, 786-792 (2005).
    • (2005) N. Engl. J. Med. , vol.352 , pp. 786-792
    • Kobayashi, S.1
  • 102
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang, Z. et al. SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767-778 (1993).
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1
  • 103
    • 0031887249 scopus 로고    scopus 로고
    • Regulation of the p85/p110 phosphatidylinositol 3′-kinase: Stabilization and inhibition of the p110α catalytic subunit by the p85 regulatory subunit
    • Yu, J. et al. Regulation of the p85/p110 phosphatidylinositol 3′-kinase: stabilization and inhibition of the p110α catalytic subunit by the p85 regulatory subunit. Mol. Cell. Biol. 18, 1379-1387 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1379-1387
    • Yu, J.1
  • 104
    • 0032514801 scopus 로고    scopus 로고
    • Regulation of the p85/p110α phosphatidylinositol 3′-kinase. Distinct roles for the N-terminal and C-terminal SH2 domains
    • Yu, J., Wjasow, C. & Backer, J. M. Regulation of the p85/p110α phosphatidylinositol 3′-kinase. Distinct roles for the N-terminal and C-terminal SH2 domains. J. Biol. Chem. 273, 30199-30203 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 30199-30203
    • Yu, J.1    Wjasow, C.2    Backer, J.M.3
  • 105
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • Franke, T. F., Kaplan, D. R., Cantley, L. C. & Toker, A. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4- bisphosphate. Science 275, 665-668 (1997).
    • (1997) Science , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 106
    • 0031015986 scopus 로고    scopus 로고
    • A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain
    • Klippel, A., Kavanaugh, W. M., Pot, D. & Williams, L. T. A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain. Mol. Cell. Biol. 17, 338-344 (1997). References 105 and 106 report the finding that AKT is activated on binding to the lipid products of PI3K.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 338-344
    • Klippel, A.1    Kavanaugh, W.M.2    Pot, D.3    Williams, L.T.4
  • 107
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov, D. D., Guertin, D. A., Ali, S. M. & Sabatini, D. M. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 301, 1098-1101 (2005). Identifies the mTOR/rictor complex as the kinase that phosphorylates Ser473 of AKT.
    • (2005) Science , vol.301 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 110
    • 0037072780 scopus 로고    scopus 로고
    • The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes
    • Berwick, D., Hers, I., Heesom, K., Moule, S. & Tavare, J. The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes. J. Biol. Chem. 277, 33895-33900 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 33895-33900
    • Berwick, D.1    Hers, I.2    Heesom, K.3    Moule, S.4    Tavare, J.5
  • 112
    • 0038003956 scopus 로고    scopus 로고
    • Decisions on life and death: FOXO forkhead transcription factors are in command when PKB/Akt is off duty
    • Burgering, B. M. & Medema, R. H. Decisions on life and death: FOXO forkhead transcription factors are in command when PKB/Akt is off duty. J. Leukoc. Biol. 73, 689-701 (2003).
    • (2003) J. Leukoc. Biol. , vol.73 , pp. 689-701
    • Burgering, B.M.1    Medema, R.H.2
  • 113
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase AKT pathway in human cancer
    • Vivanco, I. & Sawyers, C. L. The phosphatidylinositol 3-kinase AKT pathway in human cancer. Nature Rev. Cancer 2, 489-501 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 115
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway
    • Manning, B. D., Tee, A. R., Logsdon, M. N., Blenis, J. & Cantley, L. C. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol. Cell 10, 151-162 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 151-162
    • Manning, B.D.1    Tee, A.R.2    Logsdon, M.N.3    Blenis, J.4    Cantley, L.C.5
  • 116
    • 2942724235 scopus 로고    scopus 로고
    • mTOR inhibition reverses Akt-dependent prostate intraepithelial neoplasia through regulation of apoptoticand HIF-1-dependent pathways
    • Majumder, P. K. et al. mTOR inhibition reverses Akt-dependent prostate intraepithelial neoplasia through regulation of apoptoticand HIF-1-dependent pathways. Nature Med. 10, 594-601 (2004).
    • (2004) Nature Med. , vol.10 , pp. 594-601
    • Majumder, P.K.1
  • 117
    • 17944377486 scopus 로고    scopus 로고
    • Enhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR
    • Neshat, M. S. et al. Enhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR. Proc. Natl Acad. Sci. USA 98, 10314-10319 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10314-10319
    • Neshat, M.S.1
  • 120
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta, S. R. et al. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91, 231-241 (1997).
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1
  • 121
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • del Peso, L., Gonzalez-Garcia, M., Page, C., Herrera, R. & Nunez, G. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278, 687-689 (1997).
    • (1997) Science , vol.278 , pp. 687-689
    • Del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 122
    • 0033635235 scopus 로고    scopus 로고
    • 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation
    • Datta, S. R. et al. 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation. Mol. Cell 6, 41-51 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 41-51
    • Datta, S.R.1
  • 124
    • 2342496712 scopus 로고    scopus 로고
    • Foxos at the crossroads of cellular metabolism, differentiation, and transformation
    • Accili, D. & Arden, K. C. Foxos at the crossroads of cellular metabolism, differentiation, and transformation. Cell 117, 421-426 (2004).
    • (2004) Cell , vol.117 , pp. 421-426
    • Accili, D.1    Arden, K.C.2
  • 125
    • 0037438589 scopus 로고    scopus 로고
    • Common mechanism for oncogenic activation of MLL by forkhead family proteins
    • So, C. W. & Cleary, M. L. Common mechanism for oncogenic activation of MLL by forkhead family proteins. Blood 101, 633-639 (2003).
    • (2003) Blood , vol.101 , pp. 633-639
    • So, C.W.1    Cleary, M.L.2
  • 126
    • 27544515272 scopus 로고    scopus 로고
    • Somatic mutation and gain of copy number of PIK3CA in human breast cancer
    • Wu, G. et al. Somatic mutation and gain of copy number of PIK3CA in human breast cancer. Breast Cancer Res. 7, R609-R616 (2005).
    • (2005) Breast Cancer Res. , vol.7
    • Wu, G.1
  • 127
    • 17144382038 scopus 로고    scopus 로고
    • Frequent mutation of the PIK3CA gene in ovarian and breast cancers
    • Levine, D. A. et al. Frequent mutation of the PIK3CA gene in ovarian and breast cancers. Clin. Cancer Res. 11, 2875-2878 (2005).
    • (2005) Clin. Cancer Res. , vol.11 , pp. 2875-2878
    • Levine, D.A.1
  • 128
    • 20044388328 scopus 로고    scopus 로고
    • PIK3CA gene is frequently mutated in breast carcinomas and hepatocellular carcinomas
    • Lee, J.W. et al. PIK3CA gene is frequently mutated in breast carcinomas and hepatocellular carcinomas. Oncogene 24, 1477-1480 (2005).
    • (2005) Oncogene , vol.24 , pp. 1477-1480
    • Lee, J.W.1
  • 129
    • 16644393213 scopus 로고    scopus 로고
    • The PIK3CA gene is mutated with high frequency in human breast cancers
    • Bachman, K. E. et al. The PIK3CA gene is mutated with high frequency in human breast cancers. Cancer Biol. Ther. 3, 772-775 (2004).
    • (2004) Cancer Biol. Ther. , vol.3 , pp. 772-775
    • Bachman, K.E.1
  • 130
    • 7444250290 scopus 로고    scopus 로고
    • Mutation of the PIK3CA gene in ovarian and breast cancer
    • Campbell, I. G. et al. Mutation of the PIK3CA gene in ovarian and breast cancer. Cancer Res. 64, 7678-7681 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 7678-7681
    • Campbell, I.G.1
  • 131
    • 20144387695 scopus 로고    scopus 로고
    • PIK3CA mutations correlate with hormone receptors, node metastasis, and ERBB2, and are mutually exclusive with PTEN loss in human breast carcinoma
    • Saal, L. H. et al. PIK3CA mutations correlate with hormone receptors, node metastasis, and ERBB2, and are mutually exclusive with PTEN loss in human breast carcinoma. Cancer Res. 65, 2554-2559 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 2554-2559
    • Saal, L.H.1
  • 132
    • 22144452507 scopus 로고    scopus 로고
    • The prevalence of PIK3CA mutations in gastric and colon cancer
    • Velho, S. et al. The prevalence of PIK3CA mutations in gastric and colon cancer. Eur. J. Cancer 41, 1649-1654 (2005).
    • (2005) Eur. J. Cancer , vol.41 , pp. 1649-1654
    • Velho, S.1
  • 134
    • 25144522599 scopus 로고    scopus 로고
    • Genetic alteration and expression of the phosphoinositol-3-kinase/Akt pathway genes PIK3CA and PIKE in human glioblastomas
    • Knobbe, C. B., Trampe-Kieslich, A. & Reifenberger, G. Genetic alteration and expression of the phosphoinositol-3-kinase/Akt pathway genes PIK3CA and PIKE in human glioblastomas. Neuropathol. Appl. Neurobiol. 31, 486-490 (2005).
    • (2005) Neuropathol. Appl. Neurobiol. , vol.31 , pp. 486-490
    • Knobbe, C.B.1    Trampe-Kieslich, A.2    Reifenberger, G.3
  • 135
    • 22144491262 scopus 로고    scopus 로고
    • Mutations of PIK3CA in gastric adenocarcinoma
    • Li, V. S. et al. Mutations of PIK3CA in gastric adenocarcinoma. BMC Cancer 5, 29 (2005).
    • (2005) BMC Cancer , vol.5 , pp. 29
    • Li, V.S.1
  • 136
    • 13244265590 scopus 로고    scopus 로고
    • Frequent genetic and biochemical alterations of the PI 3-K/AKT/PTEN pathway in head and neck squamous cell carcinoma
    • Pedrero, J. M. et al. Frequent genetic and biochemical alterations of the PI 3-K/AKT/PTEN pathway in head and neck squamous cell carcinoma. Int. J. Cancer 114, 242-248 (2005).
    • (2005) Int. J. Cancer , vol.114 , pp. 242-248
    • Pedrero, J.M.1
  • 137
    • 0036841057 scopus 로고    scopus 로고
    • Genomic gain of PIK3CA and increased expression of p110α are associated with progression of dysplasia into invasive squamous cell carcinoma
    • Woenckhaus, J. et al. Genomic gain of PIK3CA and increased expression of p110α are associated with progression of dysplasia into invasive squamous cell carcinoma. J. Pathol. 198, 335-342 (2002).
    • (2002) J. Pathol. , vol.198 , pp. 335-342
    • Woenckhaus, J.1
  • 138
    • 23844446683 scopus 로고    scopus 로고
    • Uncommon mutation, but common amplifications, of the PIK3CA gene in thyroid tumors
    • Wu, G. et al. Uncommon mutation, but common amplifications, of the PIK3CA gene in thyroid tumors. J. Clin. Endocrinol. Metab. 90, 4688-4693 (2005).
    • (2005) J. Clin. Endocrinol. Metab. , vol.90 , pp. 4688-4693
    • Wu, G.1
  • 139
    • 0036645101 scopus 로고    scopus 로고
    • Genomic copy number analysis of non-small cell lung cancer using array comparative genomic hybridization: Implications of the phosphatidylinositol 3-kinase pathway
    • Massion, P. P. et al. Genomic copy number analysis of non-small cell lung cancer using array comparative genomic hybridization: implications of the phosphatidylinositol 3-kinase pathway. Cancer Res. 62, 3636-3640 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 3636-3640
    • Massion, P.P.1
  • 140
    • 0344734060 scopus 로고    scopus 로고
    • DNA gains in 3q occur frequently in squamous cell carcinoma of the lung, but not in adenocarcinoma
    • Bjorkqvist, A. M. et al. DNA gains in 3q occur frequently in squamous cell carcinoma of the lung, but not in adenocarcinoma. Genes Chromosomes Cancer 22, 79-82 (1998).
    • (1998) Genes Chromosomes Cancer , vol.22 , pp. 79-82
    • Bjorkqvist, A.M.1
  • 141
    • 0037431435 scopus 로고    scopus 로고
    • Frequent monoallelic deletion of PTEN and its reciprocal association with PIK3CA amplification in gastric carcinoma
    • Byun, D. S. et al. Frequent monoallelic deletion of PTEN and its reciprocal association with PIK3CA amplification in gastric carcinoma. Int. J. Cancer 104, 318-327 (2003).
    • (2003) Int. J. Cancer , vol.104 , pp. 318-327
    • Byun, D.S.1
  • 142
    • 0142250376 scopus 로고    scopus 로고
    • Gene amplification in esophageal adenocarcinomas and Barrett's with high-grade dysplasia
    • Miller, C. T. et al. Gene amplification in esophageal adenocarcinomas and Barrett's with high-grade dysplasia. Clin. Cancer Res. 9, 4819-4825 (2003).
    • (2003) Clin. Cancer Res. , vol.9 , pp. 4819-4825
    • Miller, C.T.1
  • 143
    • 0034713390 scopus 로고    scopus 로고
    • PIK3CA as an oncogene in cervical cancer
    • Ma, Y. Y. et al. PIK3CA as an oncogene in cervical cancer. Oncogene 19, 2739-2744 (2000).
    • (2000) Oncogene , vol.19 , pp. 2739-2744
    • Ma, Y.Y.1
  • 144
    • 0032576872 scopus 로고    scopus 로고
    • PTEN/MMAC1 mutations in primary glioblastomas and short-term cultures of malignant gliomas
    • Chiariello, E., Roz, L., Albarosa, R., Magnani, I. & Finocchiaro, G. PTEN/MMAC1 mutations in primary glioblastomas and short-term cultures of malignant gliomas. Oncogene 16, 541-545 (1998).
    • (1998) Oncogene , vol.16 , pp. 541-545
    • Chiariello, E.1    Roz, L.2    Albarosa, R.3    Magnani, I.4    Finocchiaro, G.5
  • 145
    • 0030799909 scopus 로고    scopus 로고
    • Somatic mutations of PTEN in glioblastoma multiforme
    • Wang, S. I. et al. Somatic mutations of PTEN in glioblastoma multiforme. Cancer Res. 57, 4183-4186 (1997).
    • (1997) Cancer Res. , vol.57 , pp. 4183-4186
    • Wang, S.I.1
  • 146
    • 0035880788 scopus 로고    scopus 로고
    • PTEN mutation, EGFR amplification, and outcome in patients with anaplastic astrocytoma and glioblastoma multiforme
    • Smith, J. S. et al. PTEN mutation, EGFR amplification, and outcome in patients with anaplastic astrocytoma and glioblastoma multiforme. J. Natl Cancer Inst. 93, 1246-1256 (2001).
    • (2001) J. Natl Cancer Inst. , vol.93 , pp. 1246-1256
    • Smith, J.S.1
  • 147
    • 15444349266 scopus 로고    scopus 로고
    • Frequent inactivation of PTEN/MMAC1 in primary prostate cancer
    • Cairns, P. et al. Frequent inactivation of PTEN/MMAC1 in primary prostate cancer. Cancer Res. 57, 4997-5000 (1997).
    • (1997) Cancer Res. , vol.57 , pp. 4997-5000
    • Cairns, P.1
  • 148
    • 0032473921 scopus 로고    scopus 로고
    • Analysis of PTEN and the 10q23 region in primary prostate carcinomas
    • Feilotter, H. E., Nagai, M. A., Boag, A. H., Eng, C. & Mulligan, L. M. Analysis of PTEN and the 10q23 region in primary prostate carcinomas. Oncogene 16, 1743-1748 (1998).
    • (1998) Oncogene , vol.16 , pp. 1743-1748
    • Feilotter, H.E.1    Nagai, M.A.2    Boag, A.H.3    Eng, C.4    Mulligan, L.M.5
  • 149
    • 0032482369 scopus 로고    scopus 로고
    • PTEN/MMAC1/TEP1 involvement in primary prostate cancers
    • Pesche, S. et al. PTEN/MMAC1/TEP1 involvement in primary prostate cancers. Oncogene 16, 2879-2883 (1998).
    • (1998) Oncogene , vol.16 , pp. 2879-2883
    • Pesche, S.1
  • 150
    • 0031762207 scopus 로고    scopus 로고
    • Mutation and expression analysis of the putative prostate tumour-suppressor gene PTEN
    • Gray, I. C. et al. Mutation and expression analysis of the putative prostate tumour-suppressor gene PTEN. Br. J. Cancer 78, 1296-1300 (1998).
    • (1998) Br. J. Cancer , vol.78 , pp. 1296-1300
    • Gray, I.C.1
  • 151
    • 0031922369 scopus 로고    scopus 로고
    • Homozygous deletion of the PTEN tumor suppressor gene in a subset of prostate adenocarcinomas
    • Wang, S. I., Parsons, R. & Ittmann, M. Homozygous deletion of the PTEN tumor suppressor gene in a subset of prostate adenocarcinomas. Clin. Cancer Res. 4, 811-815 (1998).
    • (1998) Clin. Cancer Res. , vol.4 , pp. 811-815
    • Wang, S.I.1    Parsons, R.2    Ittmann, M.3
  • 152
    • 0033003079 scopus 로고    scopus 로고
    • Analysis of the 10q23 chromosomal region and the PTEN gene in human sporadic breast carcinoma
    • Feilotter, H. E. et al. Analysis of the 10q23 chromosomal region and the PTEN gene in human sporadic breast carcinoma. Br. J. Cancer 79, 718-723 (1999).
    • (1999) Br. J. Cancer , vol.79 , pp. 718-723
    • Feilotter, H.E.1
  • 153
    • 0033001584 scopus 로고    scopus 로고
    • Exclusion of a major role for the PTEN tumour-suppressor gene in breast carcinomas
    • Freihoff, D. et al. Exclusion of a major role for the PTEN tumour-suppressor gene in breast carcinomas. Br. J. Cancer 79, 754-758 (1999).
    • (1999) Br. J. Cancer , vol.79 , pp. 754-758
    • Freihoff, D.1
  • 154
    • 0036933371 scopus 로고    scopus 로고
    • PTEN inactivation is rare in melanoma tumours but occurs frequently in melanoma cell lines
    • Pollock, P. M. et al. PTEN inactivation is rare in melanoma tumours but occurs frequently in melanoma cell lines. Melanoma Res. 12, 565-575 (2002).
    • (2002) Melanoma Res. , vol.12 , pp. 565-575
    • Pollock, P.M.1
  • 155
    • 0034086867 scopus 로고    scopus 로고
    • Mutation and allelic loss of the PTEN/MMAC1 gene in primary and metastatic melanoma biopsies
    • Birck, A., Ahrenkiel, V., Zeuthen, J., Hou-Jensen, K. & Guldberg, P. Mutation and allelic loss of the PTEN/MMAC1 gene in primary and metastatic melanoma biopsies. J. Invest. Dermatol. 114, 277-280 (2000).
    • (2000) J. Invest. Dermatol. , vol.114 , pp. 277-280
    • Birck, A.1    Ahrenkiel, V.2    Zeuthen, J.3    Hou-Jensen, K.4    Guldberg, P.5
  • 156
    • 0033833298 scopus 로고    scopus 로고
    • Identification of PTEN mutations in metastatic melanoma specimens
    • Celebi, J. T., Shendrik, I., Silvers, D. N. & Peacocke, M. Identification of PTEN mutations in metastatic melanoma specimens. J. Med. Genet. 37, 653-657 (2000).
    • (2000) J. Med. Genet. , vol.37 , pp. 653-657
    • Celebi, J.T.1    Shendrik, I.2    Silvers, D.N.3    Peacocke, M.4
  • 157
    • 0012746941 scopus 로고    scopus 로고
    • Allelic losses on chromosome arm 10q and mutation of the PTEN (MMAC1) tumour suppressor gene in primary and metastatic malignant melanomas
    • Reifenberger, J. et al. Allelic losses on chromosome arm 10q and mutation of the PTEN (MMAC1) tumour suppressor gene in primary and metastatic malignant melanomas. Virchows Arch. 436, 487-493 (2000).
    • (2000) Virchows Arch. , vol.436 , pp. 487-493
    • Reifenberger, J.1
  • 158
    • 7144223432 scopus 로고    scopus 로고
    • PTEN mutations in gliomas and glioneuronal tumors
    • Duerr, E. M. et al. PTEN mutations in gliomas and glioneuronal tumors. Oncogene 16, 2259-2264 (1998).
    • (1998) Oncogene , vol.16 , pp. 2259-2264
    • Duerr, E.M.1
  • 159
    • 0030817576 scopus 로고    scopus 로고
    • PTEN gene mutations are seen in high-grade but not in low-grade gliomas
    • Rasheed, B. K. et al. PTEN gene mutations are seen in high-grade but not in low-grade gliomas. Cancer Res. 57, 4187-4190 (1997).
    • (1997) Cancer Res. , vol.57 , pp. 4187-4190
    • Rasheed, B.K.1
  • 160
  • 161
    • 0032574718 scopus 로고    scopus 로고
    • Inactivation of the tumor suppressor PTEN/MMAC1 in advanced human prostate cancer through loss of expression
    • Whang, Y. E. et al. Inactivation of the tumor suppressor PTEN/MMAC1 in advanced human prostate cancer through loss of expression. Proc. Natl Acad. Sci. USA 95, 5246-5250 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5246-5250
    • Whang, Y.E.1
  • 162
    • 0032474749 scopus 로고    scopus 로고
    • Identification of PTEN/MMAC1 alterations in uncultured melanomas and melanoma cell lines
    • Tsao, H., Zhang, X., Benoit, E. & Haluska, F. G. Identification of PTEN/MMAC1 alterations in uncultured melanomas and melanoma cell lines. Oncogene 16, 3397-3402 (1998).
    • (1998) Oncogene , vol.16 , pp. 3397-3402
    • Tsao, H.1    Zhang, X.2    Benoit, E.3    Haluska, F.G.4
  • 163
    • 0026667730 scopus 로고
    • AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/ threonine kinases, is amplified in human ovarian carcinomas
    • Cheng, J. Q. et al. AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/ threonine kinases, is amplified in human ovarian carcinomas. Proc. Natl Acad. Sci. USA 89, 9267-9271 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 9267-9271
    • Cheng, J.Q.1
  • 164
    • 0001582482 scopus 로고
    • Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: Amplification of AKT1 in a primary human gastric adenocarcinoma
    • Staal, S. P. Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma. Proc. Natl Acad. Sci. USA 84, 5034-5037 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 5034-5037
    • Staal, S.P.1
  • 165
    • 0035886016 scopus 로고    scopus 로고
    • The phosphatidylinositol 3′-kinase p85α gene is an oncogene in human ovarian and colon tumors
    • Philp, A. J. et al. The phosphatidylinositol 3′-kinase p85α gene is an oncogene in human ovarian and colon tumors. Cancer Res. 61, 7426-7429 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 7426-7429
    • Philp, A.J.1
  • 166
    • 33746233360 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase regulatory subunit p85a suppresses insulin action via positive regulation of PTEN
    • in the press
    • Taniguchi, C. M. et al. Phosphoinositide 3-kinase regulatory subunit p85a suppresses insulin action via positive regulation of PTEN. Proc. Natl Acad. Sci. USA (in the press).
    • Proc. Natl Acad. Sci. USA
    • Taniguchi, C.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.