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Volumn 289, Issue 9, 2014, Pages 6054-6066

Sirt2 deacetylase is a novel AKT Binding partner critical for AKT activation by insulin

Author keywords

[No Author keywords available]

Indexed keywords

AMP-ACTIVATED KINASE; CANCER PATHOGENESIS; DOWNSTREAM TARGET; INSULIN RESISTANCE; METABOLIC DISORDERS; PHARMACOLOGICAL INHIBITION; PHOSPHATIDYLINOSITOL 3-KINASE; PLECKSTRIN HOMOLOGY;

EID: 84896901019     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.537266     Document Type: Article
Times cited : (111)

References (48)
  • 1
    • 79961004321 scopus 로고    scopus 로고
    • Signalling by insulin and IGF receptors. Supporting acts and new players
    • Siddle, K. (2011) Signalling by insulin and IGF receptors. Supporting acts and new players. J. Mol. Endocrinol. 47, R1-R10
    • (2011) J. Mol. Endocrinol. , vol.47
    • Siddle, K.1
  • 2
    • 51849084360 scopus 로고    scopus 로고
    • The PTEN-PI3K pathway. Of feedbacks and cross-talks
    • Carracedo, A., and Pandolfi, P. P. (2008) The PTEN-PI3K pathway. Of feedbacks and cross-talks. Oncogene 27, 5527-5541
    • (2008) Oncogene , vol.27 , pp. 5527-5541
    • Carracedo, A.1    Pandolfi, P.P.2
  • 5
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling. Navigating downstream
    • Manning, B. D., and Cantley, L. C. (2007) AKT/PKB signaling. Navigating downstream. Cell 129, 1261-1274
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 8
    • 84876852762 scopus 로고    scopus 로고
    • Diverse mechanisms of AKT pathway activation in human malignancy
    • Cheung, M., and Testa, J. R. (2013) Diverse mechanisms of AKT pathway activation in human malignancy. Curr. Cancer Drug Targets 13, 234-244
    • (2013) Curr. Cancer Drug Targets , vol.13 , pp. 234-244
    • Cheung, M.1    Testa, J.R.2
  • 10
    • 84874650275 scopus 로고    scopus 로고
    • Development of PI3K inhibitors. Lessons learned from early clinical trials
    • Rodon, J., Dienstmann, R., Serra, V., and Tabernero, J. (2013) Development of PI3K inhibitors. Lessons learned from early clinical trials. Nat. Rev. Clin. Oncol. 10, 143-153
    • (2013) Nat. Rev. Clin. Oncol. , vol.10 , pp. 143-153
    • Rodon, J.1    Dienstmann, R.2    Serra, V.3    Tabernero, J.4
  • 12
    • 84865139517 scopus 로고    scopus 로고
    • Diabetes. Insulin signal meets SIRT1 at AKT
    • Horio, Y. (2012) Diabetes. Insulin signal meets SIRT1 at AKT. Nat. Rev. Endocrinol. 8, 131-132
    • (2012) Nat. Rev. Endocrinol. , vol.8 , pp. 131-132
    • Horio, Y.1
  • 13
    • 77952547233 scopus 로고    scopus 로고
    • Ten years of NAD-dependent SIR2 family deacetylases. Implications for metabolic diseases
    • Imai, S., and Guarente, L. (2010) Ten years of NAD-dependent SIR2 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
  • 14
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins. Biological insights and disease relevance
    • Haigis, M. C., and Sinclair, D. A. (2010) Mammalian sirtuins. Biological insights and disease relevance. Annu. Rev. Pathol. 5, 253-295
    • (2010) Annu. Rev. Pathol. , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 15
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: Insights into their biological function
    • DOI 10.1042/BJ20070140
    • Michan, S., and Sinclair, D. (2007) Sirtuins in mammals. Insights into their biological function. Biochem. J. 404, 1-13 (Pubitemid 46788079)
    • (2007) Biochemical Journal , vol.404 , Issue.1 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 16
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • DOI 10.1091/mbc.E05-01-0033
    • Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C., and Horikawa, I. (2005) Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell 16, 4623-4635 (Pubitemid 41416446)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.10 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 24
    • 34547397081 scopus 로고    scopus 로고
    • SIRT2 Regulates Adipocyte Differentiation through FoxO1 Acetylation/Deacetylation
    • DOI 10.1016/j.cmet.2007.07.003, PII S155041310700191X
    • Jing, E., Gesta, S., and Kahn, C. R. (2007) SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab. 6, 105-114 (Pubitemid 47163621)
    • (2007) Cell Metabolism , vol.6 , Issue.2 , pp. 105-114
    • Jing, E.1    Gesta, S.2    Kahn, C.R.3
  • 25
    • 84866620575 scopus 로고    scopus 로고
    • Acetylation regulates subcellular localization of eukaryotic translation initiation factor 5A (eIF5A)
    • Ishfaq, M., Maeta, K., Maeda, S., Natsume, T., Ito, A., and Yoshida, M. (2012) Acetylation regulates subcellular localization of eukaryotic translation initiation factor 5A (eIF5A). FEBS Lett. 586, 3236-3241
    • (2012) FEBS Lett. , vol.586 , pp. 3236-3241
    • Ishfaq, M.1    Maeta, K.2    Maeda, S.3    Natsume, T.4    Ito, A.5    Yoshida, M.6
  • 26
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • DOI 10.1111/j.1474-9726.2007.00304.x
    • Wang, F., Nguyen, M., Qin, F. X., and Tong, Q. (2007) SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 6, 505-514 (Pubitemid 47087055)
    • (2007) Aging Cell , vol.6 , Issue.4 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.-F.3    Tong, Q.4
  • 27
    • 64049089450 scopus 로고    scopus 로고
    • SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARγ
    • Wang, F., and Tong, Q. (2009) SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARγ. Mol. Biol. Cell 20, 801-808
    • (2009) Mol. Biol. Cell , vol.20 , pp. 801-808
    • Wang, F.1    Tong, Q.2
  • 29
    • 84874394209 scopus 로고    scopus 로고
    • Glucose and SIRT2 reciprocally mediate the regulation of keratin 8 by lysine acetylation
    • Snider, N. T., Leonard, J. M., Kwan, R., Griggs, N. W., Rui, L., and Omary, M. B. (2013) Glucose and SIRT2 reciprocally mediate the regulation of keratin 8 by lysine acetylation. J. Cell Biol. 200, 241-247
    • (2013) J. Cell Biol. , vol.200 , pp. 241-247
    • Snider, N.T.1    Leonard, J.M.2    Kwan, R.3    Griggs, N.W.4    Rui, L.5    Omary, M.B.6
  • 30
    • 84866529842 scopus 로고    scopus 로고
    • SIRT2 ablation has no effect on tubulin acetylation in brain, cholesterol biosynthesis or the progression of Huntington's disease phenotypes in vivo
    • Bobrowska, A., Donmez, G., Weiss, A., Guarente, L., and Bates, G. (2012) SIRT2 ablation has no effect on tubulin acetylation in brain, cholesterol biosynthesis or the progression of Huntington's disease phenotypes in vivo. PLoS One 7, e34805
    • (2012) PLoS One , vol.7
    • Bobrowska, A.1    Donmez, G.2    Weiss, A.3    Guarente, L.4    Bates, G.5
  • 31
    • 84898011296 scopus 로고    scopus 로고
    • Sorting out functions of sirtuins in cancer
    • 10.1038/onc.2013.120
    • Roth, M., and Chen, W. Y. (2013) Sorting out functions of sirtuins in cancer. Oncogene 10.1038/onc.2013.120
    • (2013) Oncogene
    • Roth, M.1    Chen, W.Y.2
  • 35
    • 80555146753 scopus 로고    scopus 로고
    • Hepatic Sirt1 deficiency in mice impairs mTorc2/Akt signaling and results in hyperglycemia, oxidative damage, and insulin resistance
    • Wang, R. H., Kim, H. S., Xiao, C., Xu, X., Gavrilova, O., and Deng, C. X. (2011) Hepatic Sirt1 deficiency in mice impairs mTorc2/Akt signaling and results in hyperglycemia, oxidative damage, and insulin resistance. J. Clin. Invest. 121, 4477-4490
    • (2011) J. Clin. Invest. , vol.121 , pp. 4477-4490
    • Wang, R.H.1    Kim, H.S.2    Xiao, C.3    Xu, X.4    Gavrilova, O.5    Deng, C.X.6
  • 38
    • 1942437437 scopus 로고    scopus 로고
    • PIKE (Phosphatidylinositol 3-Kinase Enhancer)-A GTPase Stimulates Akt Activity and Mediates Cellular Invasion
    • DOI 10.1074/jbc.M312175200
    • Ahn, J. Y., Rong, R., Kroll, T. G., Van Meir, E. G., Snyder, S. H., and Ye, K. (2004) PIKE (phosphatidylinositol 3-kinase enhancer)-A GTPase stimulates Akt activity and mediates cellular invasion. J. Biol. Chem. 279, 16441-16451 (Pubitemid 38509342)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.16 , pp. 16441-16451
    • Ahn, J.-Y.1    Rong, R.2    Kroll, T.G.3    Van Meir, E.G.4    Snyder, S.H.5    Ye, K.6
  • 39
    • 26244432962 scopus 로고    scopus 로고
    • Identification of Raf-1 S471 as a novel phosphorylation site critical for Raf-1 and B-Raf kinase activities and for MEK binding
    • DOI 10.1091/mbc.E05-02-0090
    • Zhu, J., Balan, V., Bronisz, A., Balan, K., Sun, H., Leicht, D. T., Luo, Z., Qin, J., Avruch, J., and Tzivion, G. (2005) Identification of Raf-1 S471 as a novel phosphorylation site critical for Raf-1 and B-Raf kinase activities and for MEK binding. Mol. Biol. Cell 16, 4733-4744 (Pubitemid 41416456)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.10 , pp. 4733-4744
    • Zhu, J.1    Balan, V.2    Bronisz, A.3    Balan, K.4    Sun, H.5    Leicht, D.T.6    Luo, Z.7    Qin, J.8    Avruch, J.9    Tzivion, G.10
  • 40
    • 25444524850 scopus 로고    scopus 로고
    • Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity
    • DOI 10.1074/jbc.M502876200
    • Hahn-Windgassen, A., Nogueira, V., Chen, C. C., Skeen, J. E., Sonenberg, N., and Hay, N. (2005) Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity. J. Biol. Chem. 280, 32081-32089 (Pubitemid 41361813)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.37 , pp. 32081-32089
    • Hahn-Windgassen, A.1    Nogueira, V.2    Chen, C.-C.3    Skeen, J.E.4    Sonenberg, N.5    Hay, N.6
  • 41
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signalling interactions using short sequence motifs
    • DOI 10.1093/nar/gkg584
    • Obenauer, J. C., Cantley, L. C., and Yaffe, M. B. (2003) Scansite 2.0. Proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res. 31, 3635-3641 (Pubitemid 37442212)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 43
    • 84859447698 scopus 로고    scopus 로고
    • The role of sirtuin 2 activation by nicotinamide phosphoribosyltransferase in the aberrant proliferation and survival of myeloid leukemia cells
    • Dan, L., Klimenkova, O., Klimiankou, M., Klusman, J. H., van den Heuvel- Eibrink, M. M., Reinhardt, D., Welte, K., and Skokowa, J. (2012) The role of sirtuin 2 activation by nicotinamide phosphoribosyltransferase in the aberrant proliferation and survival of myeloid leukemia cells. Haematologica 97, 551-559
    • (2012) Haematologica , vol.97 , pp. 551-559
    • Dan, L.1    Klimenkova, O.2    Klimiankou, M.3    Klusman, J.H.4    Van Den Heuvel- Eibrink, M.M.5    Reinhardt, D.6    Welte, K.7    Skokowa, J.8
  • 44
    • 0037405043 scopus 로고    scopus 로고
    • Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle
    • DOI 10.1128/MCB.23.9.3173-3185.2003
    • Dryden, S. C., Nahhas, F. A., Nowak, J. E., Goustin, A. S., and Tainsky, M. A. (2003) Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol. Cell. Biol. 23, 3173-3185 (Pubitemid 36459231)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.9 , pp. 3173-3185
    • Dryden, S.C.1    Nahhas, F.A.2    Nowak, J.E.3    Goustin, A.-S.4    Tainsky, M.A.5
  • 45
    • 34547098165 scopus 로고    scopus 로고
    • Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation
    • DOI 10.1074/jbc.M702990200
    • North, B. J., and Verdin, E. (2007) Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation. J. Biol. Chem. 282, 19546-19555 (Pubitemid 47100062)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.27 , pp. 19546-19555
    • North, B.J.1    Verdin, E.2
  • 48
    • 80054782483 scopus 로고    scopus 로고
    • The dual role of sirtuins in cancer
    • Bosch-Presegué, L., and Vaquero, A. (2011) The dual role of sirtuins in cancer. Genes Cancer 2, 648-662
    • (2011) Genes Cancer , vol.2 , pp. 648-662
    • Bosch-Presegué, L.1    Vaquero, A.2


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