메뉴 건너뛰기




Volumn 3 JUN, Issue , 2013, Pages

The paradox of Akt-mTOR interactions

Author keywords

Akt; FoxO; Glucose transport; Insulin IGF signaling; Rictor

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; GLUCOSE TRANSPORTER 4; HEAT SHOCK PROTEIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; INSULIN; INTEGRIN LINKED KINASE; MAMMALIAN TARGET OF RAPAMYCIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3, 4 BISPHOSPHATE; PHOSPHATIDYLINOSITOL 3, 4, 5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PROTEIN KINASE B; SERINE; SIRTUIN 3; SOMATOMEDIN; THREONINE; TRANSCRIPTION FACTOR FOXO; TUBERIN; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84886235912     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2013.00165     Document Type: Article
Times cited : (117)

References (93)
  • 1
    • 0029804116 scopus 로고    scopus 로고
    • Mechanism of activation of protein kinase B by insulin and IGF-1
    • Alessi, D. R., Andjelkovic, M., Caudwell, B., Cron, P., Morrice, N., Cohen, P., et al. (1996). Mechanism of activation of protein kinase B by insulin and IGF-1. EMBO J. 15, 6541-6551.
    • (1996) EMBO J. , vol.15 , pp. 6541-6551
    • Alessi, D.R.1    Andjelkovic, M.2    Caudwell, B.3    Cron, P.4    Morrice, N.5    Cohen, P.6
  • 2
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha
    • doi:10.1016/S0960-9822(06)00122-9
    • Alessi, D. R., James, S. R., Downes, C. P., Holmes, A. B., Gaffney, P. R., Reese, C. B., et al. (1997). Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha. Curr. Biol. 7, 261-269. doi:10.1016/S0960-9822(06)00122-9.
    • (1997) Curr. Biol. , vol.7 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.5    Reese, C.B.6
  • 3
    • 37549002125 scopus 로고    scopus 로고
    • Live-cell molecular analysis of Akt activation reveals roles for activation loop phosphorylation
    • doi:10.1074/jbc.M706227200
    • Ananthanarayanan, B., Fosbrink, M., Rahdar, M., and Zhang, J. (2007). Live-cell molecular analysis of Akt activation reveals roles for activation loop phosphorylation. J. Biol. Chem. 282, 36634-36641. doi:10.1074/jbc.M706227200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36634-36641
    • Ananthanarayanan, B.1    Fosbrink, M.2    Rahdar, M.3    Zhang, J.4
  • 4
    • 0014353859 scopus 로고
    • The energy charge of the adenylate pool as a regulatory parameter. Interaction with feedback modifiers
    • doi:10.1021/bi00851a033
    • Atkinson, D. E. (1968). The energy charge of the adenylate pool as a regulatory parameter. Interaction with feedback modifiers. Biochemistry 7, 4030-4034. doi:10.1021/bi00851a033.
    • (1968) Biochemistry , vol.7 , pp. 4030-4034
    • Atkinson, D.E.1
  • 5
    • 17044393948 scopus 로고    scopus 로고
    • Regulation of Akt/PKB Ser473 phosphorylation
    • doi:10.1016/j.molcel.2005.03.020
    • Bayascas, J. R., and Alessi, D. R. (2005). Regulation of Akt/PKB Ser473 phosphorylation. Mol. Cell 18, 143-145. doi:10.1016/j.molcel.2005.03.020.
    • (2005) Mol. Cell , vol.18 , pp. 143-145
    • Bayascas, J.R.1    Alessi, D.R.2
  • 6
    • 0026095665 scopus 로고
    • A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region
    • doi:10.1126/science.1833819
    • Bellacosa, A., Testa, J. R., Staal, S. P., and Tsichlis, P. N. (1991). A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region. Science 254, 274-277. doi:10.1126/science.1833819.
    • (1991) Science , vol.254 , pp. 274-277
    • Bellacosa, A.1    Testa, J.R.2    Staal, S.P.3    Tsichlis, P.N.4
  • 7
    • 84876525535 scopus 로고    scopus 로고
    • PTEN modulators: a patent review
    • doi:10.1517/13543776.2013.768985
    • Boosani, C. S., and Agrawal, D. K. (2013). PTEN modulators: a patent review. Expert Opin. Ther. Pat. 23, 569-580. doi:10.1517/13543776.2013.768985.
    • (2013) Expert Opin. Ther. Pat. , vol.23 , pp. 569-580
    • Boosani, C.S.1    Agrawal, D.K.2
  • 8
    • 42949165854 scopus 로고    scopus 로고
    • PKBalpha/Akt1 acts downstream of DNA-PK in the DNA double-strand break response and promotes survival
    • doi:10.1016/j.molcel.2008.02.024
    • Bozulic, L., Surucu, B., Hynx, D., and Hemmings, B. A. (2008). PKBalpha/Akt1 acts downstream of DNA-PK in the DNA double-strand break response and promotes survival. Mol. Cell 30, 203-213. doi:10.1016/j.molcel.2008.02.024.
    • (2008) Mol. Cell , vol.30 , pp. 203-213
    • Bozulic, L.1    Surucu, B.2    Hynx, D.3    Hemmings, B.A.4
  • 9
    • 66449106340 scopus 로고    scopus 로고
    • Increased AKT S473 phosphorylation after mTORC1 inhibition is rictor dependent and does not predict tumor cell response to PI3K/mTOR inhibition
    • doi:10.1158/1535-7163.MCT-08-0668
    • Breuleux, M., Klopfenstein, M., Stephan, C., Doughty, C. A., Barys, L., Maira, S. M., et al. (2009). Increased AKT S473 phosphorylation after mTORC1 inhibition is rictor dependent and does not predict tumor cell response to PI3K/mTOR inhibition. Mol. Cancer Ther. 8, 742-753. doi:10.1158/1535-7163.MCT-08-0668.
    • (2009) Mol. Cancer Ther. , vol.8 , pp. 742-753
    • Breuleux, M.1    Klopfenstein, M.2    Stephan, C.3    Doughty, C.A.4    Barys, L.5    Maira, S.M.6
  • 10
    • 34547574720 scopus 로고    scopus 로고
    • A new mutational AKTivation in the PI3K pathway
    • doi:10.1016/j.ccr.2007.07.014
    • Brugge, J., Hung, M. C., and Mills, G. B. (2007). A new mutational AKTivation in the PI3K pathway. Cancer Cell 12, 104-107. doi:10.1016/j.ccr.2007.07.014.
    • (2007) Cancer Cell , vol.12 , pp. 104-107
    • Brugge, J.1    Hung, M.C.2    Mills, G.B.3
  • 11
    • 67349094328 scopus 로고    scopus 로고
    • 3-D structure and dynamics of protein kinase B-new mechanism for the allosteric regulation of an AGC kinase
    • doi:10.1007/s12154-009-0016-8
    • Calleja, V., Laguerre, M., and Larijani, B. (2009a). 3-D structure and dynamics of protein kinase B-new mechanism for the allosteric regulation of an AGC kinase. J. Chem. Biol. 2, 11-25. doi:10.1007/s12154-009-0016-8.
    • (2009) J. Chem. Biol. , vol.2 , pp. 11-25
    • Calleja, V.1    Laguerre, M.2    Larijani, B.3
  • 12
    • 58849120491 scopus 로고    scopus 로고
    • Role of a novel PH-kinase domain interface in PKB/Akt regulation: structural mechanism for allosteric inhibition
    • doi:10.1371/journal.pbio.1000017
    • Calleja, V., Laguerre, M., Parker, P. J., and Larijani, B. (2009b). Role of a novel PH-kinase domain interface in PKB/Akt regulation: structural mechanism for allosteric inhibition. PLoS Biol. 7:e17. doi:10.1371/journal.pbio.1000017.
    • (2009) PLoS Biol. , vol.7
    • Calleja, V.1    Laguerre, M.2    Parker, P.J.3    Larijani, B.4
  • 13
    • 0035936653 scopus 로고    scopus 로고
    • PDK2: a complex tail in one Akt
    • doi:10.1126/stke.2001.66.pe1
    • Chan, T. O., and Tsichlis, P. N. (2001). PDK2: a complex tail in one Akt. Sci. STKE 2001, e1. doi:10.1126/stke.2001.66.pe1.
    • (2001) Sci. STKE , vol.2001
    • Chan, T.O.1    Tsichlis, P.N.2
  • 14
    • 81755163634 scopus 로고    scopus 로고
    • Resistance of Akt kinases to dephosphorylation through ATP-dependent conformational plasticity
    • doi:10.1073/pnas.1109879108
    • Chan, T. O., Zhang, J., Rodeck, U., Pascal, J. M., Armen, R. S., Spring, M., et al. (2011). Resistance of Akt kinases to dephosphorylation through ATP-dependent conformational plasticity. Proc. Natl. Acad. Sci. U.S.A. 108, E1120-E1127. doi:10.1073/pnas.1109879108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108
    • Chan, T.O.1    Zhang, J.2    Rodeck, U.3    Pascal, J.M.4    Armen, R.S.5    Spring, M.6
  • 15
    • 4644254018 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase (PI-3K)/Akt but not PI-3K/p70 S6 kinase signaling mediates IGF-1-promoted lens epithelial cell survival
    • doi:10.1167/iovs.04-0279
    • Chandrasekher, G., and Sailaja, D. (2004). Phosphatidylinositol 3-kinase (PI-3K)/Akt but not PI-3K/p70 S6 kinase signaling mediates IGF-1-promoted lens epithelial cell survival. Invest. Ophthalmol. Vis. Sci. 45, 3577-3588. doi:10.1167/iovs.04-0279.
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.45 , pp. 3577-3588
    • Chandrasekher, G.1    Sailaja, D.2
  • 16
    • 77951911593 scopus 로고    scopus 로고
    • FoxOs inhibit mTORC1 and activate Akt by inducing the expression of Sestrin3 and rictor
    • doi:10.1016/j.devcel.2010.03.008
    • Chen, C. C., Jeon, S. M., Bhaskar, P. T., Nogueira, V., Sundararajan, D., Tonic, I., et al. (2010). FoxOs inhibit mTORC1 and activate Akt by inducing the expression of Sestrin3 and rictor. Dev. Cell 18, 592-604. doi:10.1016/j.devcel.2010.03.008.
    • (2010) Dev. Cell , vol.18 , pp. 592-604
    • Chen, C.C.1    Jeon, S.M.2    Bhaskar, P.T.3    Nogueira, V.4    Sundararajan, D.5    Tonic, I.6
  • 17
    • 0026006501 scopus 로고
    • Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families
    • doi:10.1111/j.1432-1033.1991.tb16305.x
    • Coffer, P. J., and Woodgett, J. R. (1991). Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families. Eur. J. Biochem. 201, 475-481. doi:10.1111/j.1432-1033.1991.tb16305.x.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 475-481
    • Coffer, P.J.1    Woodgett, J.R.2
  • 18
    • 23044467856 scopus 로고    scopus 로고
    • PDK2: the missing piece in the receptor tyrosine kinase signaling pathway puzzle
    • doi:10.1152/ajpendo.00011.2005
    • Dong, L. Q., and Liu, F. (2005). PDK2: the missing piece in the receptor tyrosine kinase signaling pathway puzzle. Am. J. Physiol. Endocrinol. Metab. 289, E187-E196. doi:10.1152/ajpendo.00011.2005.
    • (2005) Am. J. Physiol. Endocrinol. Metab. , vol.289
    • Dong, L.Q.1    Liu, F.2
  • 20
    • 79251587803 scopus 로고    scopus 로고
    • Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy
    • doi:10.1126/science.1196371
    • Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., et al. (2011). Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy. Science 331, 456-461. doi:10.1126/science.1196371.
    • (2011) Science , vol.331 , pp. 456-461
    • Egan, D.F.1    Shackelford, D.B.2    Mihaylova, M.M.3    Gelino, S.4    Kohnz, R.A.5    Mair, W.6
  • 21
    • 77954994889 scopus 로고    scopus 로고
    • PINCH1 regulates Akt1 activation and enhances radioresistance by inhibiting PP1alpha
    • doi:10.1172/JCI41078
    • Eke, I., Koch, U., Hehlgans, S., Sandfort, V., Stanchi, F., Zips, D., et al. (2010). PINCH1 regulates Akt1 activation and enhances radioresistance by inhibiting PP1alpha. J. Clin. Invest. 120, 2516-2527. doi:10.1172/JCI41078.
    • (2010) J. Clin. Invest. , vol.120 , pp. 2516-2527
    • Eke, I.1    Koch, U.2    Hehlgans, S.3    Sandfort, V.4    Stanchi, F.5    Zips, D.6
  • 22
    • 4644359805 scopus 로고    scopus 로고
    • Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase
    • doi:10.1074/jbc.M406731200
    • Feng, J., Park, J., Cron, P., Hess, D., and Hemmings, B. A. (2004). Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase. J. Biol. Chem. 279, 41189-41196. doi:10.1074/jbc.M406731200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41189-41196
    • Feng, J.1    Park, J.2    Cron, P.3    Hess, D.4    Hemmings, B.A.5
  • 23
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • doi:10.1016/0092-8674(95)90534-0
    • Franke, T. F., Yang, S. I., Chan, T. O., Datta, K., Kazlauskas, A., Morrison, D. K., et al. (1995). The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81, 727-736. doi:10.1016/0092-8674(95)90534-0.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.I.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6
  • 24
    • 33748471980 scopus 로고    scopus 로고
    • mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s
    • doi:10.1016/j.cub.2006.08.001
    • Frias, M. A., Thoreen, C. C., Jaffe, J. D., Schroder, W., Sculley, T., Carr, S. A., et al. (2006). mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s. Curr. Biol. 16, 1865-1870. doi:10.1016/j.cub.2006.08.001.
    • (2006) Curr. Biol. , vol.16 , pp. 1865-1870
    • Frias, M.A.1    Thoreen, C.C.2    Jaffe, J.D.3    Schroder, W.4    Sculley, T.5    Carr, S.A.6
  • 25
    • 0031663503 scopus 로고    scopus 로고
    • Phosphoinositide kinases
    • doi:10.1146/annurev.biochem.67.1.481
    • Fruman, D. A., Meyers, R. E., and Cantley, L. C. (1998). Phosphoinositide kinases. Annu. Rev. Biochem. 67, 481-507. doi:10.1146/annurev.biochem.67.1.481.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 481-507
    • Fruman, D.A.1    Meyers, R.E.2    Cantley, L.C.3
  • 26
    • 79952424287 scopus 로고    scopus 로고
    • TBC proteins: GAPs for mammalian small GTPase Rab?
    • doi:10.1042/BSR20100112
    • Fukuda, M. (2011). TBC proteins: GAPs for mammalian small GTPase Rab? Biosci. Rep. 31, 159-168. doi:10.1042/BSR20100112.
    • (2011) Biosci. Rep. , vol.31 , pp. 159-168
    • Fukuda, M.1
  • 27
    • 67349180268 scopus 로고    scopus 로고
    • The level of AKT phosphorylation on threonine 308 but not on serine 473 is associated with high-risk cytogenetics and predicts poor overall survival in acute myeloid leukaemia
    • doi:10.1038/leu.2008.395
    • Gallay, N., Dos Santos, C., Cuzin, L., Bousquet, M., Simmonet Gouy, V., Chaussade, C., et al. (2009). The level of AKT phosphorylation on threonine 308 but not on serine 473 is associated with high-risk cytogenetics and predicts poor overall survival in acute myeloid leukaemia. Leukemia 23, 1029-1038. doi:10.1038/leu.2008.395.
    • (2009) Leukemia , vol.23 , pp. 1029-1038
    • Gallay, N.1    Dos Santos, C.2    Cuzin, L.3    Bousquet, M.4    Simmonet Gouy, V.5    Chaussade, C.6
  • 28
    • 15944406764 scopus 로고    scopus 로고
    • PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth
    • doi:10.1016/j.molcel.2005.03.008
    • Gao, T., Furnari, F., and Newton, A. C. (2005). PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth. Mol. Cell 18, 13-24. doi:10.1016/j.molcel.2005.03.008.
    • (2005) Mol. Cell , vol.18 , pp. 13-24
    • Gao, T.1    Furnari, F.2    Newton, A.C.3
  • 29
    • 79958068761 scopus 로고    scopus 로고
    • mTORC2 is required for proliferation and survival of TSC2-null cells
    • doi:10.1128/MCB.01061-10
    • Goncharova, E. A., Goncharov, D. A., Li, H., Pimtong, W., Lu, S., Khavin, I., et al. (2011). mTORC2 is required for proliferation and survival of TSC2-null cells. Mol. Cell. Biol. 31, 2484-2498. doi:10.1128/MCB.01061-10.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2484-2498
    • Goncharova, E.A.1    Goncharov, D.A.2    Li, H.3    Pimtong, W.4    Lu, S.5    Khavin, I.6
  • 30
    • 79952374430 scopus 로고    scopus 로고
    • Rictor/mTORC2 is essential for maintaining a balance between beta-cell proliferation and cell size
    • doi:10.2337/db10-1194
    • Gu, Y., Lindner, J., Kumar, A., Yuan, W., and Magnuson, M. A. (2011). Rictor/mTORC2 is essential for maintaining a balance between beta-cell proliferation and cell size. Diabetes 60, 827-837. doi:10.2337/db10-1194.
    • (2011) Diabetes , vol.60 , pp. 827-837
    • Gu, Y.1    Lindner, J.2    Kumar, A.3    Yuan, W.4    Magnuson, M.A.5
  • 31
    • 79956188245 scopus 로고    scopus 로고
    • Sphingosine kinase 1 regulates the Akt/FOXO3a/Bim pathway and contributes to apoptosis resistance in glioma cells
    • doi:10.1371/journal.pone.0019946
    • Guan, H., Song, L., Cai, J., Huang, Y., Wu, J., Yuan, J., et al. (2011). Sphingosine kinase 1 regulates the Akt/FOXO3a/Bim pathway and contributes to apoptosis resistance in glioma cells. PLoS ONE 6:e19946. doi:10.1371/journal.pone.0019946.
    • (2011) PLoS ONE , vol.6
    • Guan, H.1    Song, L.2    Cai, J.3    Huang, Y.4    Wu, J.5    Yuan, J.6
  • 32
    • 33751348056 scopus 로고    scopus 로고
    • Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1
    • doi:10.1016/j.devcel.2006.10.007
    • Guertin, D. A., Stevens, D. M., Thoreen, C. C., Burds, A. A., Kalaany, N. Y., Moffat, J., et al. (2006). Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1. Dev. Cell 11, 859-871. doi:10.1016/j.devcel.2006.10.007.
    • (2006) Dev. Cell , vol.11 , pp. 859-871
    • Guertin, D.A.1    Stevens, D.M.2    Thoreen, C.C.3    Burds, A.A.4    Kalaany, N.Y.5    Moffat, J.6
  • 33
    • 33751533918 scopus 로고    scopus 로고
    • The reciprocal stability of FOXO1 and IRS2 creates a regulatory circuit that controls insulin signaling
    • doi:10.1210/me.2006-0092
    • Guo, S., Dunn, S. L., and White, M. F. (2006). The reciprocal stability of FOXO1 and IRS2 creates a regulatory circuit that controls insulin signaling. Mol. Endocrinol. 20, 3389-3399. doi:10.1210/me.2006-0092.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 3389-3399
    • Guo, S.1    Dunn, S.L.2    White, M.F.3
  • 34
    • 80053035284 scopus 로고    scopus 로고
    • AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function
    • doi:10.1101/gad.17420111
    • Hardie, D. G. (2011). AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function. Genes Dev. 25, 1895-1908. doi:10.1101/gad.17420111.
    • (2011) Genes Dev. , vol.25 , pp. 1895-1908
    • Hardie, D.G.1
  • 35
    • 0035542970 scopus 로고    scopus 로고
    • AMP-activated protein kinase: the energy charge hypothesis revisited
    • doi:10.1002/bies.10009
    • Hardie, D. G., and Hawley, S. A. (2001). AMP-activated protein kinase: the energy charge hypothesis revisited. Bioessays 23, 1112-1119. doi:10.1002/bies.10009.
    • (2001) Bioessays , vol.23 , pp. 1112-1119
    • Hardie, D.G.1    Hawley, S.A.2
  • 36
    • 0035854677 scopus 로고    scopus 로고
    • Insulin-stimulated protein kinase B phosphorylation on Ser-473 is independent of its activity and occurs through a staurosporine-insensitive kinase
    • doi:10.1074/jbc.C100174200
    • Hill, M. M., Andjelkovic, M., Brazil, D. P., Ferrari, S., Fabbro, D., and Hemmings, B. A. (2001). Insulin-stimulated protein kinase B phosphorylation on Ser-473 is independent of its activity and occurs through a staurosporine-insensitive kinase. J. Biol. Chem. 276, 25643-25646. doi:10.1074/jbc.C100174200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25643-25646
    • Hill, M.M.1    Andjelkovic, M.2    Brazil, D.P.3    Ferrari, S.4    Fabbro, D.5    Hemmings, B.A.6
  • 37
    • 79953038262 scopus 로고    scopus 로고
    • PTEN loss in the continuum of common cancers, rare syndromes and mouse models
    • doi:10.1038/nrc3037
    • Hollander, M. C., Blumenthal, G. M., and Dennis, P. A. (2011). PTEN loss in the continuum of common cancers, rare syndromes and mouse models. Nat. Rev. Cancer 11, 289-301. doi:10.1038/nrc3037.
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 289-301
    • Hollander, M.C.1    Blumenthal, G.M.2    Dennis, P.A.3
  • 38
    • 84860805552 scopus 로고    scopus 로고
    • Uncaging akt
    • doi:10.1126/scisignal.2003085
    • Humphrey, S. J., and James, D. E. (2012). Uncaging akt. Sci. Signal. 5:e20. doi:10.1126/scisignal.2003085.
    • (2012) Sci. Signal. , vol.5
    • Humphrey, S.J.1    James, D.E.2
  • 39
    • 47949104258 scopus 로고    scopus 로고
    • Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling
    • doi:10.1038/emboj.2008.119
    • Ikenoue, T., Inoki, K., Yang, Q., Zhou, X., and Guan, K. L. (2008). Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling. EMBO J. 27, 1919-1931. doi:10.1038/emboj.2008.119.
    • (2008) EMBO J. , vol.27 , pp. 1919-1931
    • Ikenoue, T.1    Inoki, K.2    Yang, Q.3    Zhou, X.4    Guan, K.L.5
  • 40
    • 0025882091 scopus 로고
    • Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily
    • doi:10.1073/pnas.88.10.4171
    • Jones, P. F., Jakubowicz, T., Pitossi, F. J., Maurer, F., and Hemmings, B. A. (1991). Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily. Proc. Natl. Acad. Sci. U.S.A. 88, 4171-4175. doi:10.1073/pnas.88.10.4171.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4171-4175
    • Jones, P.F.1    Jakubowicz, T.2    Pitossi, F.J.3    Maurer, F.4    Hemmings, B.A.5
  • 41
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • doi:10.1038/ncb2152
    • Kim, J., Kundu, M., Viollet, B., and Guan, K. L. (2011). AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell Biol. 13, 132-141. doi:10.1038/ncb2152.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 42
    • 33646077675 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) activating agents cause dephosphorylation of Akt and glycogen synthase kinase-3
    • doi:10.1016/j.bcp.2006.03.005
    • King, T. D., Song, L., and Jope, R. S. (2006). AMP-activated protein kinase (AMPK) activating agents cause dephosphorylation of Akt and glycogen synthase kinase-3. Biochem. Pharmacol. 71, 1637-1647. doi:10.1016/j.bcp.2006.03.005.
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 1637-1647
    • King, T.D.1    Song, L.2    Jope, R.S.3
  • 43
    • 0029143388 scopus 로고
    • Insulin stimulates the kinase activity of RAC-PK, a pleckstrin homology domain containing ser/thr kinase
    • Kohn, A. D., Kovacina, K. S., and Roth, R. A. (1995). Insulin stimulates the kinase activity of RAC-PK, a pleckstrin homology domain containing ser/thr kinase. EMBO J. 14, 4288-4295.
    • (1995) EMBO J. , vol.14 , pp. 4288-4295
    • Kohn, A.D.1    Kovacina, K.S.2    Roth, R.A.3
  • 44
    • 34548710863 scopus 로고    scopus 로고
    • Knock-in of mutant K-ras in nontumorigenic human epithelial cells as a new model for studying K-ras mediated transformation
    • doi:10.1158/0008-5472.CAN-07-0108
    • Konishi, H., Karakas, B., Abukhdeir, A. M., Lauring, J., Gustin, J. P., Garay, J. P., et al. (2007). Knock-in of mutant K-ras in nontumorigenic human epithelial cells as a new model for studying K-ras mediated transformation. Cancer Res. 67, 8460-8467. doi:10.1158/0008-5472.CAN-07-0108.
    • (2007) Cancer Res. , vol.67 , pp. 8460-8467
    • Konishi, H.1    Karakas, B.2    Abukhdeir, A.M.3    Lauring, J.4    Gustin, J.P.5    Garay, J.P.6
  • 45
    • 77953200528 scopus 로고    scopus 로고
    • Fat cell-specific ablation of rictor in mice impairs insulin-regulated fat cell and whole-body glucose and lipid metabolism
    • doi:10.2337/db09-1061
    • Kumar, A., Lawrence, J. C. Jr., Jung, D. Y., Ko, H. J., Keller, S. R., Kim, J. K., et al. (2010). Fat cell-specific ablation of rictor in mice impairs insulin-regulated fat cell and whole-body glucose and lipid metabolism. Diabetes 59, 1397-1406. doi:10.2337/db09-1061.
    • (2010) Diabetes , vol.59 , pp. 1397-1406
    • Kumar, A.1    Lawrence Jr., J.C.2    Jung, D.Y.3    Ko, H.J.4    Keller, S.R.5    Kim, J.K.6
  • 46
    • 14044266297 scopus 로고    scopus 로고
    • Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter
    • doi:10.1074/jbc.M411534200
    • Kunkel, M. T., Ni, Q., Tsien, R. Y., Zhang, J., and Newton, A. C. (2005). Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter. J. Biol. Chem. 280, 5581-5587. doi:10.1074/jbc.M411534200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5581-5587
    • Kunkel, M.T.1    Ni, Q.2    Tsien, R.Y.3    Zhang, J.4    Newton, A.C.5
  • 47
    • 27744588780 scopus 로고    scopus 로고
    • Tuberous sclerosis: a GAP at the crossroads of multiple signaling pathways
    • doi:10.1093/hmg/ddi260
    • Kwiatkowski, D. J., and Manning, B. D. (2005). Tuberous sclerosis: a GAP at the crossroads of multiple signaling pathways. Hum. Mol. Genet. 14, 251-258. doi:10.1093/hmg/ddi260.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 251-258
    • Kwiatkowski, D.J.1    Manning, B.D.2
  • 48
    • 84859778293 scopus 로고    scopus 로고
    • mTOR signaling in growth control and disease
    • doi:10.1016/j.cell.2012.03.017
    • Laplante, M., and Sabatini, D. M. (2012). mTOR signaling in growth control and disease. Cell 149, 274-293. doi:10.1016/j.cell.2012.03.017.
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 49
    • 84859823056 scopus 로고    scopus 로고
    • mTOR is required for asymmetric division through small GTPases in mouse oocytes
    • doi:10.1002/mrd.22035
    • Lee, S. E., Sun, S. C., Choi, H. Y., Uhm, S. J., and Kim, N. H. (2012). mTOR is required for asymmetric division through small GTPases in mouse oocytes. Mol. Reprod. Dev. 79, 356-366. doi:10.1002/mrd.22035.
    • (2012) Mol. Reprod. Dev. , vol.79 , pp. 356-366
    • Lee, S.E.1    Sun, S.C.2    Choi, H.Y.3    Uhm, S.J.4    Kim, N.H.5
  • 50
    • 84877851087 scopus 로고    scopus 로고
    • AMPK: a contextual oncogene or tumor suppressor?
    • doi:10.1158/0008-5472.CAN-12-3876
    • Liang, J., and Mills, G. B. (2013). AMPK: a contextual oncogene or tumor suppressor? Cancer Res. 73, 2929-2935. doi:10.1158/0008-5472.CAN-12-3876.
    • (2013) Cancer Res. , vol.73 , pp. 2929-2935
    • Liang, J.1    Mills, G.B.2
  • 51
    • 84860823513 scopus 로고    scopus 로고
    • An ATP-site on-off switch that restricts phosphatase accessibility of Akt
    • doi:10.1126/scisignal.2002618
    • Lin, K., Lin, J., Wu, W. I., Ballard, J., Lee, B. B., Gloor, S. L., et al. (2012). An ATP-site on-off switch that restricts phosphatase accessibility of Akt. Sci. Signal. 5, ra37. doi:10.1126/scisignal.2002618.
    • (2012) Sci. Signal. , vol.5
    • Lin, K.1    Lin, J.2    Wu, W.I.3    Ballard, J.4    Lee, B.B.5    Gloor, S.L.6
  • 52
  • 53
    • 0025785215 scopus 로고
    • Improved shuttle vectors for cloning and high-level Cu(2+)-mediated expression of foreign genes in yeast
    • doi:10.1016/0378-1119(91)90474-P
    • Macreadie, I. G., Horaitis, O., Verkuylen, A. J., and Savin, K. W. (1991). Improved shuttle vectors for cloning and high-level Cu(2+)-mediated expression of foreign genes in yeast. Gene 104, 107-111. doi:10.1016/0378-1119(91)90474-P.
    • (1991) Gene , vol.104 , pp. 107-111
    • Macreadie, I.G.1    Horaitis, O.2    Verkuylen, A.J.3    Savin, K.W.4
  • 54
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor
    • doi:10.1074/jbc.273.22.13375
    • Maehama, T., and Dixon, J. E. (1998). The tumor suppressor. J. Biol. Chem. 273, 13375-13378. doi:10.1074/jbc.273.22.13375.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 55
    • 84862103119 scopus 로고    scopus 로고
    • PI3K-independent AKT activation in cancers: a treasure trove for novel therapeutics
    • doi:10.1002/jcp.24065
    • Mahajan, K., and Mahajan, N. P. (2012). PI3K-independent AKT activation in cancers: a treasure trove for novel therapeutics. J. Cell. Physiol. 227, 3178-3184. doi:10.1002/jcp.24065.
    • (2012) J. Cell. Physiol. , vol.227 , pp. 3178-3184
    • Mahajan, K.1    Mahajan, N.P.2
  • 56
    • 40949083412 scopus 로고    scopus 로고
    • Rictor and integrin-linked kinase interact and regulate Akt phosphorylation and cancer cell survival
    • doi:10.1158/0008-5472.CAN-07-5869
    • McDonald, P. C., Oloumi, A., Mills, J., Dobreva, I., Maidan, M., Gray, V., et al. (2008). Rictor and integrin-linked kinase interact and regulate Akt phosphorylation and cancer cell survival. Cancer Res. 68, 1618-1624. doi:10.1158/0008-5472.CAN-07-5869.
    • (2008) Cancer Res. , vol.68 , pp. 1618-1624
    • McDonald, P.C.1    Oloumi, A.2    Mills, J.3    Dobreva, I.4    Maidan, M.5    Gray, V.6
  • 57
    • 84880509894 scopus 로고    scopus 로고
    • Calorie restriction in humans inhibits the PI3K/AKT pathway and induces a younger transcription profile
    • doi:10.1111/acel.12088. [Epub ahead of print].
    • Mercken, E. M., Crosby, S. D., Lamming, D. W., Jebailey, L., Krzysik-Walker, S., Villareal, D., et al. (2013). Calorie restriction in humans inhibits the PI3K/AKT pathway and induces a younger transcription profile. Aging Cell. doi:10.1111/acel.12088. [Epub ahead of print].
    • (2013) Aging Cell
    • Mercken, E.M.1    Crosby, S.D.2    Lamming, D.W.3    Jebailey, L.4    Krzysik-Walker, S.5    Villareal, D.6
  • 58
    • 85027931809 scopus 로고    scopus 로고
    • When overgrowth bumps into cancer: the PTEN-opathies
    • doi:10.1002/ajmg.c.31364
    • Mester, J., and Eng, C. (2013). When overgrowth bumps into cancer: the PTEN-opathies. Am. J. Med. Genet. C Semin. Med. Genet. 163, 114-121. doi:10.1002/ajmg.c.31364.
    • (2013) Am. J. Med. Genet. C Semin. Med. Genet. , vol.163 , pp. 114-121
    • Mester, J.1    Eng, C.2
  • 59
    • 79960149722 scopus 로고    scopus 로고
    • mTORC2-mediated Akt Ser473 phosphorylation is not required for Akt1 activity in human platelets
    • doi:10.1074/jbc.M110.202341
    • Moore, S. F., Hunter, R. W., and Hers, I. (2011). mTORC2-mediated Akt Ser473 phosphorylation is not required for Akt1 activity in human platelets. J. Biol. Chem. 36, 374-387. doi:10.1074/jbc.M110.202341.
    • (2011) J. Biol. Chem. , vol.36 , pp. 374-387
    • Moore, S.F.1    Hunter, R.W.2    Hers, I.3
  • 60
    • 0036185848 scopus 로고    scopus 로고
    • The protein kinase B/Akt signalling pathway in human malignancy
    • doi:10.1016/S0898-6568(01)00271-6
    • Nicholson, K. M., and Anderson, N. G. (2002). The protein kinase B/Akt signalling pathway in human malignancy. Cell. Signal. 14, 381-395. doi:10.1016/S0898-6568(01)00271-6.
    • (2002) Cell. Signal. , vol.14 , pp. 381-395
    • Nicholson, K.M.1    Anderson, N.G.2
  • 61
    • 31444440033 scopus 로고    scopus 로고
    • Frequent elevation of Akt kinase phosphorylation in blood marrow and peripheral blood mononuclear cells from high-risk myelodysplastic syndrome patients
    • doi:10.1038/sj.leu.2404057
    • Nyakern, M., Tazzari, P. L., Finelli, C., Bosi, C., Follo, M. Y., Grafone, T., et al. (2006). Frequent elevation of Akt kinase phosphorylation in blood marrow and peripheral blood mononuclear cells from high-risk myelodysplastic syndrome patients. Leukemia 20, 230-238. doi:10.1038/sj.leu.2404057.
    • (2006) Leukemia , vol.20 , pp. 230-238
    • Nyakern, M.1    Tazzari, P.L.2    Finelli, C.3    Bosi, C.4    Follo, M.Y.5    Grafone, T.6
  • 62
    • 84857687439 scopus 로고    scopus 로고
    • AMPK functions as an adenylate charge-regulated protein kinase
    • doi:10.1016/j.tem.2011.12.006
    • Oakhill, J. S., Scott, J. W., and Kemp, B. E. (2012). AMPK functions as an adenylate charge-regulated protein kinase. Trends Endocrinol. Metab. 23, 125-132. doi:10.1016/j.tem.2011.12.006.
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 125-132
    • Oakhill, J.S.1    Scott, J.W.2    Kemp, B.E.3
  • 63
    • 79959338922 scopus 로고    scopus 로고
    • AMPK is a direct adenylate charge-regulated protein kinase
    • doi:10.1126/science.1200094
    • Oakhill, J. S., Steel, R., Chen, Z. P., Scott, J. W., Ling, N., Tam, S., et al. (2011). AMPK is a direct adenylate charge-regulated protein kinase. Science 332, 1433-1435. doi:10.1126/science.1200094.
    • (2011) Science , vol.332 , pp. 1433-1435
    • Oakhill, J.S.1    Steel, R.2    Chen, Z.P.3    Scott, J.W.4    Ling, N.5    Tam, S.6
  • 64
    • 0035476408 scopus 로고    scopus 로고
    • Tumour necrosis factor-alpha activation of protein kinase B in WEHI-164 cells is accompanied by increased phosphorylation of Ser473, but not Thr308
    • doi:10.1042/0264-6021:3590119
    • O'Toole, A., Moule, S. K., Lockyer, P. J., and Halestrap, A. P. (2001). Tumour necrosis factor-alpha activation of protein kinase B in WEHI-164 cells is accompanied by increased phosphorylation of Ser473, but not Thr308. Biochem. J. 359, 119-127. doi:10.1042/0264-6021:3590119.
    • (2001) Biochem. J. , vol.359 , pp. 119-127
    • O'Toole, A.1    Moule, S.K.2    Lockyer, P.J.3    Halestrap, A.P.4
  • 65
    • 84878305687 scopus 로고    scopus 로고
    • A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels
    • doi:10.1007/s00018-012-1244-6
    • Peserico, A., Chiacchiera, F., Grossi, V., Matrone, A., Latorre, D., Simonatto, M., et al. (2013). A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels. Cell. Mol. Life Sci. 70, 2015-2029. doi:10.1007/s00018-012-1244-6.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 2015-2029
    • Peserico, A.1    Chiacchiera, F.2    Grossi, V.3    Matrone, A.4    Latorre, D.5    Simonatto, M.6
  • 66
    • 84883833752 scopus 로고
    • Adenylate as a metabolic regulator. effect on yeast phosphofructokinase kinetics
    • Ramaiah, A., Hathaway, J. A., and Atkinson, D. E. (1964). Adenylate as a metabolic regulator. effect on yeast phosphofructokinase kinetics. J. Biol. Chem. 239, 3619-3622.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3619-3622
    • Ramaiah, A.1    Hathaway, J.A.2    Atkinson, D.E.3
  • 67
    • 0036154215 scopus 로고    scopus 로고
    • Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes
    • doi:10.1016/S0898-6568(01)00238-8
    • Resjo, S., Goransson, O., Harndahl, L., Zolnierowicz, S., Manganiello, V., and Degerman, E. (2002). Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes. Cell. Signal. 14, 231-238. doi:10.1016/S0898-6568(01)00238-8.
    • (2002) Cell. Signal. , vol.14 , pp. 231-238
    • Resjo, S.1    Goransson, O.2    Harndahl, L.3    Zolnierowicz, S.4    Manganiello, V.5    Degerman, E.6
  • 68
    • 80655126355 scopus 로고    scopus 로고
    • mTOR kinase inhibition causes feedback-dependent biphasic regulation of AKT signaling
    • doi:10.1158/2159-8290.CD-11-0085
    • Rodrik-Outmezguine, V. S., Chandarlapaty, S., Pagano, N. C., Poulikakos, P. I., Scaltriti, M., Moskatel, E., et al. (2012). mTOR kinase inhibition causes feedback-dependent biphasic regulation of AKT signaling. Cancer Discov. 1, 248-259. doi:10.1158/2159-8290.CD-11-0085.
    • (2012) Cancer Discov. , vol.1 , pp. 248-259
    • Rodrik-Outmezguine, V.S.1    Chandarlapaty, S.2    Pagano, N.C.3    Poulikakos, P.I.4    Scaltriti, M.5    Moskatel, E.6
  • 69
    • 74449090245 scopus 로고    scopus 로고
    • Insulin/IGF-1 paradox of aging: regulation via AKT/IKK/NF-kappaB signaling
    • doi:10.1016/j.cellsig.2009.10.006
    • Salminen, A., and Kaarniranta, K. (2013). Insulin/IGF-1 paradox of aging: regulation via AKT/IKK/NF-kappaB signaling. Cell. Signal. 22, 573-577. doi:10.1016/j.cellsig.2009.10.006.
    • (2013) Cell. Signal. , vol.22 , pp. 573-577
    • Salminen, A.1    Kaarniranta, K.2
  • 70
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • doi:10.1126/science.1106148
    • Sarbassov, D. D., Guertin, D. A., Ali, S. M., and Sabatini, D. M. (2005). Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307, 1098-1101. doi:10.1126/science.1106148.
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 71
    • 0036333737 scopus 로고    scopus 로고
    • Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B
    • doi:10.1128/MCB.22.17.6247-6260.2002
    • Scheid, M. P., Marignani, P. A., and Woodgett, J. R. (2002). Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B. Mol. Cell. Biol. 22, 6247-6260. doi:10.1128/MCB.22.17.6247-6260.2002.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6247-6260
    • Scheid, M.P.1    Marignani, P.A.2    Woodgett, J.R.3
  • 72
    • 77958046738 scopus 로고    scopus 로고
    • Requirement for distinct vesicle-associated membrane proteins in insulin- and AMP-activated protein kinase (AMPK)-induced translocation of GLUT4 and CD36 in cultured cardiomyocytes
    • doi:10.1007/s00125-010-1832-7
    • Schwenk, R. W., Dirkx, E., Coumans, W. A., Bonen, A., Klip, A., Glatz, J. F., et al. (2010). Requirement for distinct vesicle-associated membrane proteins in insulin- and AMP-activated protein kinase (AMPK)-induced translocation of GLUT4 and CD36 in cultured cardiomyocytes. Diabetologia 53, 2209-2219. doi:10.1007/s00125-010-1832-7.
    • (2010) Diabetologia , vol.53 , pp. 2209-2219
    • Schwenk, R.W.1    Dirkx, E.2    Coumans, W.A.3    Bonen, A.4    Klip, A.5    Glatz, J.F.6
  • 73
    • 57449115616 scopus 로고    scopus 로고
    • Tumor metabolism: cancer cells give and take lactate
    • doi:10.1172/JCI37373
    • Semenza, G. L. (2008). Tumor metabolism: cancer cells give and take lactate. J. Clin. Invest. 118, 3835-3837. doi:10.1172/JCI37373.
    • (2008) J. Clin. Invest. , vol.118 , pp. 3835-3837
    • Semenza, G.L.1
  • 74
    • 84871184914 scopus 로고    scopus 로고
    • Genome-wide analysis of FoxO1 binding in hepatic chromatin: potential involvement of FoxO1 in linking retinoid signaling to hepatic gluconeogenesis
    • doi:10.1093/nar/gks932
    • Shin, D. J., Joshi, P., Hong, S. H., Mosure, K., Shin, D. G., and Osborne, T. F. (2012). Genome-wide analysis of FoxO1 binding in hepatic chromatin: potential involvement of FoxO1 in linking retinoid signaling to hepatic gluconeogenesis. Nucleic Acids Res. 40, 11499-11509. doi:10.1093/nar/gks932.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 11499-11509
    • Shin, D.J.1    Joshi, P.2    Hong, S.H.3    Mosure, K.4    Shin, D.G.5    Osborne, T.F.6
  • 75
    • 0030799706 scopus 로고    scopus 로고
    • Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B
    • doi:10.1126/science.277.5325.567
    • Stokoe, D., Stephens, L. R., Copeland, T., Gaffney, P. R., Reese, C. B., Painter, G. F., et al. (1997). Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B. Science 277, 567-570. doi:10.1126/science.277.5325.567.
    • (1997) Science , vol.277 , pp. 567-570
    • Stokoe, D.1    Stephens, L.R.2    Copeland, T.3    Gaffney, P.R.4    Reese, C.B.5    Painter, G.F.6
  • 76
    • 81355151361 scopus 로고    scopus 로고
    • DNA-PK mediates AKT activation and apoptosis inhibition in clinically acquired platinum resistance
    • Stronach, E. A., Chen, M., Maginn, E. N., Agarwal, R., Mills, G. B., Wasan, H., et al. (2011). DNA-PK mediates AKT activation and apoptosis inhibition in clinically acquired platinum resistance. Neoplasia 13, 1069-1080.
    • (2011) Neoplasia , vol.13 , pp. 1069-1080
    • Stronach, E.A.1    Chen, M.2    Maginn, E.N.3    Agarwal, R.4    Mills, G.B.5    Wasan, H.6
  • 77
    • 4544224035 scopus 로고    scopus 로고
    • Detection of serine 473 phosphorylated Akt in acute myeloid leukaemia blasts by flow cytometry
    • doi:10.1111/j.1365-2141.2004.05121.x
    • Tazzari, P. L., Cappellini, A., Grafone, T., Mantovani, I., Ricci, F., Billi, A. M., et al. (2004). Detection of serine 473 phosphorylated Akt in acute myeloid leukaemia blasts by flow cytometry. Br. J. Haematol. 126, 675-681. doi:10.1111/j.1365-2141.2004.05121.x.
    • (2004) Br. J. Haematol. , vol.126 , pp. 675-681
    • Tazzari, P.L.1    Cappellini, A.2    Grafone, T.3    Mantovani, I.4    Ricci, F.5    Billi, A.M.6
  • 78
    • 79952552097 scopus 로고    scopus 로고
    • Protein phosphatase 1-dependent dephosphorylation of Akt is the prime signaling event in sphingosine-induced apoptosis in Jurkat cells
    • doi:10.1002/jcb.23033
    • Thayyullathil, F., Chathoth, S., Shahin, A., Kizhakkayil, J., Hago, A., Patel, M., et al. (2011). Protein phosphatase 1-dependent dephosphorylation of Akt is the prime signaling event in sphingosine-induced apoptosis in Jurkat cells. J. Cell. Biochem. 112, 1138-1153. doi:10.1002/jcb.23033.
    • (2011) J. Cell. Biochem. , vol.112 , pp. 1138-1153
    • Thayyullathil, F.1    Chathoth, S.2    Shahin, A.3    Kizhakkayil, J.4    Hago, A.5    Patel, M.6
  • 79
    • 84873328655 scopus 로고    scopus 로고
    • mTORC1 inhibition restricts inflammation-associated gastrointestinal tumorigenesis in mice
    • doi:10.1172/JCI65086
    • Thiem, S., Pierce, T. P., Palmieri, M., Putoczki, T. L., Buchert, M., Preaudet, A., et al. (2013). mTORC1 inhibition restricts inflammation-associated gastrointestinal tumorigenesis in mice. J. Clin. Invest. 123, 767-781. doi:10.1172/JCI65086.
    • (2013) J. Clin. Invest. , vol.123 , pp. 767-781
    • Thiem, S.1    Pierce, T.P.2    Palmieri, M.3    Putoczki, T.L.4    Buchert, M.5    Preaudet, A.6
  • 80
    • 84858066279 scopus 로고    scopus 로고
    • FoxOs integrate pleiotropic actions of insulin in vascular endothelium to protect mice from atherosclerosis
    • doi:10.1016/j.cmet.2012.01.018
    • Tsuchiya, K., Tanaka, J., Shuiqing, Y., Welch, C. L., DePinho, R. A., Tabas, I., et al. (2012). FoxOs integrate pleiotropic actions of insulin in vascular endothelium to protect mice from atherosclerosis. Cell Metab. 15, 372-381. doi:10.1016/j.cmet.2012.01.018.
    • (2012) Cell Metab. , vol.15 , pp. 372-381
    • Tsuchiya, K.1    Tanaka, J.2    Shuiqing, Y.3    Welch, C.L.4    DePinho, R.A.5    Tabas, I.6
  • 81
    • 80755168893 scopus 로고    scopus 로고
    • FoxO feedback control of basal IRS-2 expression in pancreatic beta-cells is distinct from that in hepatocytes
    • doi:10.2337/db11-0340
    • Tsunekawa, S., Demozay, D., Briaud, I., McCuaig, J., Accili, D., Stein, R., et al. (2011). FoxO feedback control of basal IRS-2 expression in pancreatic beta-cells is distinct from that in hepatocytes. Diabetes 60, 2883-2891. doi:10.2337/db11-0340.
    • (2011) Diabetes , vol.60 , pp. 2883-2891
    • Tsunekawa, S.1    Demozay, D.2    Briaud, I.3    McCuaig, J.4    Accili, D.5    Stein, R.6
  • 82
    • 84886375160 scopus 로고    scopus 로고
    • Role of PI3K-AKT-mTOR and Wnt signaling pathways in transition of G1-S phase of cell cycle in cancer cells
    • doi:10.3389/fonc.2013.00085
    • Vadlakonda, L., Pasupuleti, M., and Pallu, R. (2013). Role of PI3K-AKT-mTOR and Wnt signaling pathways in transition of G1-S phase of cell cycle in cancer cells. Front. Oncol. 3:85. doi:10.3389/fonc.2013.00085.
    • (2013) Front. Oncol. , vol.3 , pp. 85
    • Vadlakonda, L.1    Pasupuleti, M.2    Pallu, R.3
  • 83
    • 85027933245 scopus 로고    scopus 로고
    • Akt phosphorylation on Thr308 but not on Ser473 correlates with Akt protein kinase activity in human non-small cell lung cancer
    • doi:10.1038/bjc
    • Vincent, E. E., Elder, D. J., Thomas, E. C., Phillips, L., Morgan, C., Pawade, J., et al. (2011). Akt phosphorylation on Thr308 but not on Ser473 correlates with Akt protein kinase activity in human non-small cell lung cancer. Br. J. Cancer 104, 1755-1761. doi:10.1038/bjc.
    • (2011) Br. J. Cancer , vol.104 , pp. 1755-1761
    • Vincent, E.E.1    Elder, D.J.2    Thomas, E.C.3    Phillips, L.4    Morgan, C.5    Pawade, J.6
  • 84
    • 80052197913 scopus 로고    scopus 로고
    • TBK1 mediates crosstalk between the innate immune response and autophagy
    • doi:10.1126/scisignal.2002355
    • Weidberg, H., and Elazar, Z. (2011). TBK1 mediates crosstalk between the innate immune response and autophagy. Sci. Signal. 4, e39. doi:10.1126/scisignal.2002355.
    • (2011) Sci. Signal. , vol.4
    • Weidberg, H.1    Elazar, Z.2
  • 85
    • 0344305782 scopus 로고    scopus 로고
    • Insulin signaling in health and disease
    • doi:10.1126/science.1092952
    • White, M. F. (2003). Insulin signaling in health and disease. Science 302, 1710-1711. doi:10.1126/science.1092952.
    • (2003) Science , vol.302 , pp. 1710-1711
    • White, M.F.1
  • 86
    • 84875813063 scopus 로고    scopus 로고
    • AMPK-dependent degradation of TXNIP upon energy stress leads to enhanced glucose uptake via GLUT1
    • doi:10.1016/j.molcel.2013.01.035
    • Wu, N., Zheng, B., Shaywitz, A., Dagon, Y., Tower, C., Bellinger, G., et al. (2013). AMPK-dependent degradation of TXNIP upon energy stress leads to enhanced glucose uptake via GLUT1. Mol. Cell 49, 1167-1175. doi:10.1016/j.molcel.2013.01.035.
    • (2013) Mol. Cell , vol.49 , pp. 1167-1175
    • Wu, N.1    Zheng, B.2    Shaywitz, A.3    Dagon, Y.4    Tower, C.5    Bellinger, G.6
  • 87
    • 79955615939 scopus 로고    scopus 로고
    • IkappaB kinase epsilon and TANK-binding kinase 1 activate AKT by direct phosphorylation
    • doi:10.1073/pnas.1016132108
    • Xie, X., Zhang, D., Zhao, B., Lu, M. K., You, M., Condorelli, G., et al. (2011). IkappaB kinase epsilon and TANK-binding kinase 1 activate AKT by direct phosphorylation. Proc. Natl. Acad. Sci. U.S.A. 108, 6474-6479. doi:10.1073/pnas.1016132108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 6474-6479
    • Xie, X.1    Zhang, D.2    Zhao, B.3    Lu, M.K.4    You, M.5    Condorelli, G.6
  • 88
    • 0345707575 scopus 로고    scopus 로고
    • The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells
    • Xu, W., Yuan, X., Jung, Y. J., Yang, Y., Basso, A., Rosen, N., et al. (2003). The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells. Cancer Res. 63, 7777-7784.
    • (2003) Cancer Res. , vol.63 , pp. 7777-7784
    • Xu, W.1    Yuan, X.2    Jung, Y.J.3    Yang, Y.4    Basso, A.5    Rosen, N.6
  • 89
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • doi:10.1016/S1097-2765(02)00550-6
    • Yang, J., Cron, P., Thompson, V., Good, V. M., Hess, D., Hemmings, B. A., et al. (2002). Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Mol. Cell 9, 1227-1240. doi:10.1016/S1097-2765(02)00550-6.
    • (2002) Mol. Cell , vol.9 , pp. 1227-1240
    • Yang, J.1    Cron, P.2    Thompson, V.3    Good, V.M.4    Hess, D.5    Hemmings, B.A.6
  • 90
    • 64349123107 scopus 로고    scopus 로고
    • Autophagy mediates the mitotic senescence transition
    • doi:10.1101/gad.519709
    • Young, A. R., Narita, M., Ferreira, M., Kirschner, K., Sadaie, M., Darot, J. F., et al. (2009). Autophagy mediates the mitotic senescence transition. Genes Dev. 23, 798-803. doi:10.1101/gad.519709.
    • (2009) Genes Dev. , vol.23 , pp. 798-803
    • Young, A.R.1    Narita, M.2    Ferreira, M.3    Kirschner, K.4    Sadaie, M.5    Darot, J.F.6
  • 91
    • 33750040886 scopus 로고    scopus 로고
    • S6K1 regulates GSK3 under conditions of mTOR-dependent feedback inhibition of Akt
    • doi:10.1016/j.molcel.2006.09.019
    • Zhang, H. H., Lipovsky, A. I., Dibble, C. C., Sahin, M., and Manning, B. D. (2006). S6K1 regulates GSK3 under conditions of mTOR-dependent feedback inhibition of Akt. Mol. Cell 24, 185-197. doi:10.1016/j.molcel.2006.09.019.
    • (2006) Mol. Cell , vol.24 , pp. 185-197
    • Zhang, H.H.1    Lipovsky, A.I.2    Dibble, C.C.3    Sahin, M.4    Manning, B.D.5
  • 92
    • 84871749894 scopus 로고    scopus 로고
    • Cardiac PI3K-Akt impairs insulin-stimulated glucose uptake independent of mTORC1 and GLUT4 translocation
    • doi:10.1210/me.2012-1210
    • Zhu, Y., Pereira, R. O., O'Neill, B. T., Riehle, C., Ilkun, O., Wende, A. R., et al. (2013). Cardiac PI3K-Akt impairs insulin-stimulated glucose uptake independent of mTORC1 and GLUT4 translocation. Mol. Endocrinol. 27, 172-184. doi:10.1210/me.2012-1210.
    • (2013) Mol. Endocrinol. , vol.27 , pp. 172-184
    • Zhu, Y.1    Pereira, R.O.2    O'Neill, B.T.3    Riehle, C.4    Ilkun, O.5    Wende, A.R.6
  • 93
    • 63249088840 scopus 로고    scopus 로고
    • Insulin resistance in striated muscle-specific integrin receptor beta1-deficient mice
    • doi:10.1074/jbc.M807408200
    • Zong, H., Bastie, C. C., Xu, J., Fassler, R., Campbell, K. P., Kurland, I. J., et al. (2009). Insulin resistance in striated muscle-specific integrin receptor beta1-deficient mice. J. Biol. Chem. 284, 4679-4688. doi:10.1074/jbc.M807408200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 4679-4688
    • Zong, H.1    Bastie, C.C.2    Xu, J.3    Fassler, R.4    Campbell, K.P.5    Kurland, I.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.