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Volumn 289, Issue 19, 2014, Pages 13132-13141

Cross-talk between sirtuin and mammalian target of rapamycin complex 1 (mTORC1) signaling in the regulation of S6 kinase 1 (S6K1) phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; ENZYMES; PHOSPHORYLATION; SUBSTRATES;

EID: 84900404392     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.520734     Document Type: Article
Times cited : (81)

References (63)
  • 1
    • 81855169682 scopus 로고    scopus 로고
    • Mammalian TOR signaling to the AGC kinases
    • Su, B., and Jacinto, E. (2011) Mammalian TOR signaling to the AGC kinases. Crit. Rev. Biochem. Mol. Biol. 46, 527-547
    • (2011) Crit. Rev. Biochem. Mol. Biol. , vol.46 , pp. 527-547
    • Su, B.1    Jacinto, E.2
  • 2
    • 84055178474 scopus 로고    scopus 로고
    • Regulation and function of ribosomal protein S6 kinase (S6K) within mTOR signalling networks
    • Magnuson, B., Ekim, B., and Fingar, D. C. (2012) Regulation and function of ribosomal protein S6 kinase (S6K) within mTOR signalling networks. Biochem. J. 441, 1-21
    • (2012) Biochem. J. , vol.441 , pp. 1-21
    • Magnuson, B.1    Ekim, B.2    Fingar, D.C.3
  • 5
    • 0033539154 scopus 로고    scopus 로고
    • Characterization of S6K2, a novel kinase homologous to S6K1
    • Lee-Fruman, K. K., Kuo, C. J., Lippincott, J., Terada, N., and Blenis, J. (1999) Characterization of S6K2, a novel kinase homologous to S6K1. Oncogene 18, 5108-5114
    • (1999) Oncogene , vol.18 , pp. 5108-5114
    • Lee-Fruman, K.K.1    Kuo, C.J.2    Lippincott, J.3    Terada, N.4    Blenis, J.5
  • 8
    • 0032518467 scopus 로고    scopus 로고
    • 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro
    • Alessi, D. R., Kozlowski, M. T., Weng, Q. P., Morrice, N., and Avruch, J. (1998) 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro. Curr. Biol. 8, 69-81
    • (1998) Curr. Biol. , vol.8 , pp. 69-81
    • Alessi, D.R.1    Kozlowski, M.T.2    Weng, Q.P.3    Morrice, N.4    Avruch, J.5
  • 11
    • 0037178786 scopus 로고    scopus 로고
    • MTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • Kim, D. H., Sarbassov, D. D., Ali, S. M., King, J. E., Latek, R. R., Erdjument-Bromage, H., Tempst, P., and Sabatini, D. M. (2002) mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110, 163-175
    • (2002) Cell , vol.110 , pp. 163-175
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    King, J.E.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 12
    • 0035882103 scopus 로고    scopus 로고
    • The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB
    • Biondi, R. M., Kieloch, A., Currie, R. A., Deak, M., and Alessi, D. R. (2001) The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB. EMBOJ. 20, 4380-4390
    • (2001) EMBOJ , vol.20 , pp. 4380-4390
    • Biondi, R.M.1    Kieloch, A.2    Currie, R.A.3    Deak, M.4    Alessi, D.R.5
  • 13
    • 0034176579 scopus 로고    scopus 로고
    • The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells
    • Williams, M. R., Arthur, J. S., Balendran, A., van der Kaay, J., Poli, V., Cohen, P., and Alessi, D. R. (2000) The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells. Curr. Biol. 10, 439-448
    • (2000) Curr. Biol. , vol.10 , pp. 439-448
    • Williams, M.R.1    Arthur, J.S.2    Balendran, A.3    Van Der Kaay, J.4    Poli, V.5    Cohen, P.6    Alessi, D.R.7
  • 14
    • 84880877011 scopus 로고    scopus 로고
    • Crystal structures of S6K1 provide insights into the regulation mechanism of S6K1 by the hydrophobic motif
    • Wang, J., Zhong, C, Wang, F., Qu, F., and Ding, J. (2013) Crystal structures of S6K1 provide insights into the regulation mechanism of S6K1 by the hydrophobic motif. Biochem. J. 454, 39-47
    • (2013) Biochem. J. , vol.454 , pp. 39-47
    • Wang, J.1    Zhong, C.2    Wang, F.3    Qu, F.4    Ding, J.5
  • 16
    • 0029828590 scopus 로고    scopus 로고
    • s6k phosphorylation sites, T-229 and T-389, are differentially regulated by rapamycin-insensitive kinase kinases
    • s6k phosphorylation sites, T-229 and T-389, are differentially regulated by rapamycin-insensitive kinase kinases. Mol. Cell. Biol. 16, 6242-6251
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6242-6251
    • Dennis, P.B.1    Pullen, N.2    Kozma, S.C.3    Thomas, G.4
  • 17
    • 0028939115 scopus 로고
    • Multiple independent inputs are required for activation of the p70 S6 kinase
    • Weng, Q. P., Andrabi, K., Kozlowski, M. T., Grove, J. R., and Avruch, J. (1995) Multiple independent inputs are required for activation of the p70 S6 kinase. Mol. Cell. Biol. 15, 2333-2340
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2333-2340
    • Weng, Q.P.1    Andrabi, K.2    Kozlowski, M.T.3    Grove, J.R.4    Avruch, J.5
  • 18
    • 0037117409 scopus 로고    scopus 로고
    • Identification of a conserved motif required for mTOR signaling
    • Schalm, S. S., and Blenis, J. (2002) Identification of a conserved motif required for mTOR signaling. Curr. Biol. 12, 632-639
    • (2002) Curr. Biol. , vol.12 , pp. 632-639
    • Schalm, S.S.1    Blenis, J.2
  • 20
    • 0037507252 scopus 로고    scopus 로고
    • The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif
    • Nojima, H., Tokunaga, C, Eguchi, S., Oshiro, N., Hidayat, S., Yoshino, K., Hara, K., Tanaka, N., Avruch, J., and Yonezawa, K. (2003) The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif. J. Biol. Chem. 278, 15461-15464
    • (2003) J. Biol. Chem. , vol.278 , pp. 15461-15464
    • Nojima, H.1    Tokunaga, C.2    Eguchi, S.3    Oshiro, N.4    Hidayat, S.5    Yoshino, K.6    Hara, K.7    Tanaka, N.8    Avruch, J.9    Yonezawa, K.10
  • 21
    • 0037718389 scopus 로고    scopus 로고
    • TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation and function
    • Schalm, S. S., Fingar, D. C, Sabatini, D. M., and Blenis, J. (2003) TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation and function. Curr. Biol. 13, 797-806
    • (2003) Curr. Biol. , vol.13 , pp. 797-806
    • Schalm, S.S.1    Fingar, D.C.2    Sabatini, D.M.3    Blenis, J.4
  • 22
    • 15744396300 scopus 로고    scopus 로고
    • Characterization of a conserved C-terminal motif (RSPRR) in ribosomal protein S6 kinase 1 required for its mammalian target of rapamycin-dependent regulation
    • Schalm, S. S., Tee, A. R., and Blenis, J. (2005) Characterization of a conserved C-terminal motif (RSPRR) in ribosomal protein S6 kinase 1 required for its mammalian target of rapamycin-dependent regulation. J. Biol. Chem. 280, 11101-11106
    • (2005) J. Biol. Chem. , vol.280 , pp. 11101-11106
    • Schalm, S.S.1    Tee, A.R.2    Blenis, J.3
  • 25
    • 0025948372 scopus 로고
    • Insulin-Activated protein kinases phosphorylate a pseudosubstrate synthetic peptide inhibitor of the p70 S6 kinase
    • Price, D. J., Mukhopadhyay, N. K., and Avruch, J. (1991) Insulin-Activated protein kinases phosphorylate a pseudosubstrate synthetic peptide inhibitor of the p70 S6 kinase. J. Biol. Chem. 266, 16281-16284
    • (1991) J. Biol. Chem. , vol.266 , pp. 16281-16284
    • Price, D.J.1    Mukhopadhyay, N.K.2    Avruch, J.3
  • 26
    • 21244458013 scopus 로고    scopus 로고
    • Structure of S6 kinase 1 determines whether raptor-mTOR or rictor-mTOR phosphorylates its hydrophobic motif site
    • Ali, S. M., and Sabatini, D. M. (2005) Structure of S6 kinase 1 determines whether raptor-mTOR or rictor-mTOR phosphorylates its hydrophobic motif site. J. Biol. Chem. 280, 19445-19448
    • (2005) J. Biol. Chem. , vol.280 , pp. 19445-19448
    • Ali, S.M.1    Sabatini, D.M.2
  • 28
    • 45849137875 scopus 로고    scopus 로고
    • SIRT1 overexpression antagonizes cellular senescence with activated ERK/S6k1 signaling in human diploid fibroblasts
    • Huang, J., Gan, Q., Han, L., Li, J., Zhang, H., Sun, Y., Zhang, Z., and Tong, T. (2008) SIRT1 overexpression antagonizes cellular senescence with activated ERK/S6k1 signaling in human diploid fibroblasts. PLoS One 3, e1710
    • (2008) PLoS One , vol.3
    • Huang, J.1    Gan, Q.2    Han, L.3    Li, J.4    Zhang, H.5    Sun, Y.6    Zhang, Z.7    Tong, T.8
  • 29
    • 77951717549 scopus 로고    scopus 로고
    • SirT1 enhances survival of human osteoarthritic chondrocytes by repressing protein tyrosine phosphatase 1B and activating the insulin-like growth factor receptor pathway
    • Gagarina, V., Gabay, O., Dvir-Ginzberg, M., Lee, E. J., Brady, J. K., Quon, M. J., and Hall, D. J. (2010) SirT1 enhances survival of human osteoarthritic chondrocytes by repressing protein tyrosine phosphatase 1B and activating the insulin-like growth factor receptor pathway. Arthritis Rheum. 62, 1383-1392
    • (2010) Arthritis Rheum. , vol.62 , pp. 1383-1392
    • Gagarina, V.1    Gabay, O.2    Dvir-Ginzberg, M.3    Lee, E.J.4    Brady, J.K.5    Quon, M.J.6    Hall, D.J.7
  • 30
    • 36348974168 scopus 로고    scopus 로고
    • The direct involvement of SirT1 in insulin-induced insulin receptor substrate-2 tyrosine phosphorylation
    • Zhang, J. (2007) The direct involvement of SirT1 in insulin-induced insulin receptor substrate-2 tyrosine phosphorylation. J. Biol. Chem. 282, 34356-34364
    • (2007) J. Biol. Chem. , vol.282 , pp. 34356-34364
    • Zhang, J.1
  • 31
    • 84879637271 scopus 로고    scopus 로고
    • Sirtuin 1 inhibition delays cyst formation in autosomal-dominant polycystic kidney disease
    • Zhou, X., Fan, L. X., Sweeney, W. E., Jr., Denu, J. M., Avner, E. D., and Li, X. (2013) Sirtuin 1 inhibition delays cyst formation in autosomal-dominant polycystic kidney disease. J. Clin. Invest. 123, 3084-3098
    • (2013) J. Clin. Invest. , vol.123 , pp. 3084-3098
    • Zhou, X.1    Fan, L.X.2    Sweeney Jr., W.E.3    Denu, J.M.4    Avner, E.D.5    Li, X.6
  • 32
    • 80052645243 scopus 로고    scopus 로고
    • Sirt1 overexpression in neurons promotes neurite outgrowth and cell survival through inhibition of the mTOR signaling
    • Guo, W., Qian, L., Zhang, J., Zhang, W., Morrison, A., Hayes, P., Wilson, S., Chen, T., and Zhao, J. (2011) Sirt1 overexpression in neurons promotes neurite outgrowth and cell survival through inhibition of the mTOR signaling. J. Neurosci. Res. 89, 1723-1736
    • (2011) J. Neurosci. Res. , vol.89 , pp. 1723-1736
    • Guo, W.1    Qian, L.2    Zhang, J.3    Zhang, W.4    Morrison, A.5    Hayes, P.6    Wilson, S.7    Chen, T.8    Zhao, J.9
  • 33
    • 77950127881 scopus 로고    scopus 로고
    • SIRT1 negatively regulates the mammalian target of rapamycin
    • Ghosh, H. S., McBurney, M., and Robbins, P. D. (2010) SIRT1 negatively regulates the mammalian target of rapamycin. PLoS One 5, e9199
    • (2010) PLoS One , vol.5
    • Ghosh, H.S.1    McBurney, M.2    Robbins, P.D.3
  • 35
    • 77952547233 scopus 로고    scopus 로고
    • Ten years of NAD-dependentSIR2 family deacetylases: Implications for metabolic diseases
    • Imai, S., and Guarente, L. (2010) Ten years of NAD-dependentSIR2 family deacetylases: implications for metabolic diseases. Trends Pharmacol. Sci. 31, 212-220
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 212-220
    • Imai, S.1    Guarente, L.2
  • 36
    • 80054771657 scopus 로고    scopus 로고
    • The role of mammalian sirtuins in the regulation of metabolism, aging, and longevity
    • Satoh, A., Stein, L., and Imai, S. (2011) The role of mammalian sirtuins in the regulation of metabolism, aging, and longevity. Handb. Exp. Pharmacol. 206, 125-162
    • (2011) Handb. Exp. Pharmacol. , vol.206 , pp. 125-162
    • Satoh, A.1    Stein, L.2    Imai, S.3
  • 37
    • 77957903550 scopus 로고    scopus 로고
    • Discovery of 1-(4-(4-propionylpiperazin-1-yl) -3-(trifluoromethyl) phenyl) -9-(quinolin-3-yl) benz o[h][1, 6]naphthyridin-2 (1 H) -one as a highly potent, selective mammalian target of rapamycin (mTOR) inhibitor for the treatment of cancer
    • Liu, Q., Chang, J. W., Wang, J., Kang, S. A., Thoreen, C. C, Markhard, A., Hur, W., Zhang, J., Sim, T., Sabatini, D. M., and Gray, N. S. (2010) Discovery of 1-(4-(4-propionylpiperazin-1-yl)-3-(trifluoromethyl) phenyl)-9-(quinolin-3-yl) benz o[h][1, 6]naphthyridin-2 (1 H)-one as a highly potent, selective mammalian target of rapamycin (mTOR) inhibitor for the treatment of cancer. J. Med. Chem. 53, 7146-7155
    • (2010) J. Med. Chem. , vol.53 , pp. 7146-7155
    • Liu, Q.1    Chang, J.W.2    Wang, J.3    Kang, S.A.4    Thoreen, C.C.5    Markhard, A.6    Hur, W.7    Zhang, J.8    Sim, T.9    Sabatini, D.M.10    Gray, N.S.11
  • 40
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • Luo, J., Nikolaev, A. Y., Imai, S., Chen, D., Su, F., Shiloh, A., Guarente, L., and Gu, W. (2001) Negative control of p53 by Sir2α promotes cell survival under stress. Cell 107, 137-148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 42
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai, S., Armstrong, C. M., Kaeberlein, M., and Guarente, L. (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403, 795-800
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 43
    • 3543038804 scopus 로고    scopus 로고
    • Budding yeast silencing complexes and regulation of Sir2 activity by protein-protein interactions
    • Tanny, J. C, Kirkpatrick, D. S., Gerber, S. A., Gygi, S. P., and Moazed, D. (2004) Budding yeast silencing complexes and regulation of Sir2 activity by protein-protein interactions. Mol. Cell. Biol. 24, 6931-6946
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6931-6946
    • Tanny, J.C.1    Kirkpatrick, D.S.2    Gerber, S.A.3    Gygi, S.P.4    Moazed, D.5
  • 44
    • 55049117907 scopus 로고    scopus 로고
    • The SIRT2 deacetylase regulates autoacetylation of p300
    • Black, J. C, Mosley, A., Kitada, T., Washburn, M., and Carey, M. (2008) The SIRT2 deacetylase regulates autoacetylation of p300. Mol. Cell 32, 449-455
    • (2008) Mol. Cell. , vol.32 , pp. 449-455
    • Black, J.C.1    Mosley, A.2    Kitada, T.3    Washburn, M.4    Carey, M.5
  • 45
    • 78650638268 scopus 로고    scopus 로고
    • SIRT2 down-regulation in HeLa can induce p53 accumulation via p38 MAPK activation-dependent p300 decrease, eventually leading to apoptosis
    • Li, Y., Matsumori, H., Nakayama, Y., Osaki, M., Kojima, H., Kurimasa, A., Ito, H., Mori, S., Katoh, M., Oshimura, M., and Inoue, T. (2011) SIRT2 down-regulation in HeLa can induce p53 accumulation via p38 MAPK activation-dependent p300 decrease, eventually leading to apoptosis. Genes Cells 16, 34-45
    • (2011) Genes Cells , vol.16 , pp. 34-45
    • Li, Y.1    Matsumori, H.2    Nakayama, Y.3    Osaki, M.4    Kojima, H.5    Kurimasa, A.6    Ito, H.7    Mori, S.8    Katoh, M.9    Oshimura, M.10    Inoue, T.11
  • 46
    • 77955278511 scopus 로고    scopus 로고
    • S6K1 is acetylated at lysine 516 in response to growth factor stimulation
    • Fenton, T. R., Gwalter, J., Cramer, R., and Gout, I. T. (2010) S6K1 is acetylated at lysine 516 in response to growth factor stimulation. Biochem. Biophys. Res. Commun. 398, 400-405
    • (2010) Biochem. Biophys. Res. Commun. , vol.398 , pp. 400-405
    • Fenton, T.R.1    Gwalter, J.2    Cramer, R.3    Gout, I.T.4
  • 47
    • 73749083464 scopus 로고    scopus 로고
    • Histone acetyltransferases interact with and acetylate p70 ribosomal S6 kinases in vitro and in vivo
    • Fenton, T. R., Gwalter, J., Ericsson, J., and Gout, I. T. (2010) Histone acetyltransferases interact with and acetylate p70 ribosomal S6 kinases in vitro and in vivo. Int. J. Biochem. Cell Biol. 42, 359-366
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 359-366
    • Fenton, T.R.1    Gwalter, J.2    Ericsson, J.3    Gout, I.T.4
  • 50
    • 79957557182 scopus 로고    scopus 로고
    • Dissecting systemic control of metabolism and aging in the NAD World: The importance of SIRT1 and NAMPT-mediated NAD biosynthesis
    • Imai, S. (2011) Dissecting systemic control of metabolism and aging in the NAD World: the importance of SIRT1 and NAMPT-mediated NAD biosynthesis. FEBS Lett. 585, 1657-1662
    • (2011) FEBS Lett. , vol.585 , pp. 1657-1662
    • Imai, S.1
  • 51
    • 0038491354 scopus 로고    scopus 로고
    • Identification and characterization of a novel p300-mediated p53 acetylation site, lysine 305
    • Wang, Y. H., Tsay, Y. G., Tan, B. C., Lo, W. Y., and Lee, S. C. (2003) Identification and characterization of a novel p300-mediated p53 acetylation site, lysine 305. J. Biol. Chem. 278, 25568-25576
    • (2003) J. Biol. Chem. , vol.278 , pp. 25568-25576
    • Wang, Y.H.1    Tsay, Y.G.2    Tan, B.C.3    Lo, W.Y.4    Lee, S.C.5
  • 53
    • 60749101582 scopus 로고    scopus 로고
    • Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1
    • Westerheide, S. D., Anckar, J., Stevens, S. M., Jr., Sistonen, L., and Morimoto, R. I. (2009) Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 323, 1063-1066
    • (2009) Science , vol.323 , pp. 1063-1066
    • Westerheide, S.D.1    Anckar, J.2    Stevens Jr., S.M.3    Sistonen, L.4    Morimoto, R.I.5
  • 54
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein, M., McVey, M., and Guarente, L. (1999) The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 13, 2570-2580
    • (1999) Genes Dev. , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 55
    • 18744416824 scopus 로고    scopus 로고
    • Longevity regulation by Drosophila Rpd3 deacetylase and caloric restriction
    • Rogina, B., Helfand, S. L., and Frankel, S. (2002) Longevity regulation by Drosophila Rpd3 deacetylase and caloric restriction. Science 298, 1745
    • (2002) Science , vol.298 , pp. 1745
    • Rogina, B.1    Helfand, S.L.2    Frankel, S.3
  • 59
    • 84898011296 scopus 로고    scopus 로고
    • Sorting out functions of sirtuins in cancer
    • Roth, M., and Chen, W. Y. (2014) Sorting out functions of sirtuins in cancer. Oncogene 33, 1609-1620
    • (2014) Oncogene , vol.33 , pp. 1609-1620
    • Roth, M.1    Chen, W.Y.2
  • 60
    • 34548857700 scopus 로고    scopus 로고
    • SIRT1 improves insulin sensitivity under insulin-resistant conditions by repressing PTP1B
    • Sun, C., Zhang, F., Ge, X., Yan, T., Chen, X., Shi, X., and Zhai, Q. (2007) SIRT1 improves insulin sensitivity under insulin-resistant conditions by repressing PTP1B. Cell Metab. 6, 307-319
    • (2007) Cell Metab. , vol.6 , pp. 307-319
    • Sun, C.1    Zhang, F.2    Ge, X.3    Yan, T.4    Chen, X.5    Shi, X.6    Zhai, Q.7
  • 61
    • 52049102233 scopus 로고    scopus 로고
    • PTEN acetylation modulates its interaction with PDZ domain
    • Ikenoue, T., Inoki, K., Zhao, B., and Guan, K. L. (2008) PTEN acetylation modulates its interaction with PDZ domain. Cancer Res. 68, 6908-6912
    • (2008) Cancer Res. , vol.68 , pp. 6908-6912
    • Ikenoue, T.1    Inoki, K.2    Zhao, B.3    Guan, K.L.4
  • 62
    • 77949887674 scopus 로고    scopus 로고
    • Rapamycin ameliorates PKD resulting from conditional inactivation of Pkd1
    • Shillingford, J. M., Piontek, K. B., Germino, G. G., and Weimbs, T. (2010) Rapamycin ameliorates PKD resulting from conditional inactivation of Pkd1. J. Am. Soc. Nephrol. 21, 489-497
    • (2010) J. Am. Soc. Nephrol. , vol.21 , pp. 489-497
    • Shillingford, J.M.1    Piontek, K.B.2    Germino, G.G.3    Weimbs, T.4
  • 63
    • 84883476818 scopus 로고    scopus 로고
    • Sirt1 Extends Life Span and Delays Aging in Mice through the Regulation of Nk2 Homeobox 1 in the DMH and LH
    • Satoh, A., Brace, C. S., Rensing, N., Cliften, P., Wozniak, D. F., Herzog, E. D., Yamada, K. A., and Imai, S. (2013) Sirt1 Extends Life Span and Delays Aging in Mice through the Regulation of Nk2 Homeobox 1 in the DMH and LH. Cell Metab. 18, 416-430
    • (2013) Cell Metab. , vol.18 , pp. 416-430
    • Satoh, A.1    Brace, C.S.2    Rensing, N.3    Cliften, P.4    Wozniak, D.F.5    Herzog, E.D.6    Yamada, K.A.7    Imai, S.8


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