메뉴 건너뛰기




Volumn 72, Issue 17, 2012, Pages 4394-4404

AMPK promotes p53 acetylation via phosphorylation and inactivation of SIRT1 in liver cancer cells

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE ALPHA 2; PROTEIN P53; SIRTUIN 1; THREONINE; UNCLASSIFIED DRUG;

EID: 84865793242     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-12-0429     Document Type: Article
Times cited : (186)

References (34)
  • 1
    • 80053035284 scopus 로고    scopus 로고
    • AMP-activated protein kinase: An energy sensor that regulates all aspects of cell function
    • Hardie DG. AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function. Genes Dev 2011;25:1895-908.
    • (2011) Genes Dev , vol.25 , pp. 1895-1908
    • Hardie, D.G.1
  • 2
  • 3
    • 0345107247 scopus 로고    scopus 로고
    • Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade
    • Hawley SA, Boudeau J, Reid JL, Mustard KJ, Udd L, Makela TP, et al. Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade. J Biol 2003;2:28.
    • (2003) J Biol , vol.2 , pp. 28
    • Hawley, S.A.1    Boudeau, J.2    Reid, J.L.3    Mustard, K.J.4    Udd, L.5    Makela, T.P.6
  • 5
    • 20844449238 scopus 로고    scopus 로고
    • AMP-activated protein kinase induces a p53-dependent metabolic checkpoint
    • Jones RG, Plas DR, Kubek S, Buzzai M, Mu J, Xu Y, et al. AMP-activated protein kinase induces a p53-dependent metabolic checkpoint. Mol Cell 2005;18:283-93.
    • (2005) Mol Cell , vol.18 , pp. 283-293
    • Jones, R.G.1    Plas, D.R.2    Kubek, S.3    Buzzai, M.4    Mu, J.5    Xu, Y.6
  • 6
    • 0034193776 scopus 로고    scopus 로고
    • Sir2 links chromatin silencing, metabolism, and aging
    • Guarente L. Sir2 links chromatin silencing, metabolism, and aging. Genes Dev 2000;14:1021-6.
    • (2000) Genes Dev , vol.14 , pp. 1021-1026
    • Guarente, L.1
  • 7
    • 34547875773 scopus 로고    scopus 로고
    • Sirtuins: Critical regulators at the crossroads between cancer and aging
    • Saunders LR, Verdin E. Sirtuins: critical regulators at the crossroads between cancer and aging. Oncogene 2007;26:5489-504.
    • (2007) Oncogene , vol.26 , pp. 5489-5504
    • Saunders, L.R.1    Verdin, E.2
  • 9
    • 0141817910 scopus 로고    scopus 로고
    • Identification of an auto-inhibitory domain of p21-activated protein kinase 5
    • Ching YP, Leong VY, Wong CM, Kung HF. Identification of an auto-inhibitory domain of p21-activated protein kinase 5. J Biol Chem 2003;278:33621-4.
    • (2003) J Biol Chem , vol.278 , pp. 33621-33624
    • Ching, Y.P.1    Leong, V.Y.2    Wong, C.M.3    Kung, H.F.4
  • 10
    • 0039396186 scopus 로고    scopus 로고
    • A preliminary study of loss of heterozygosity on chromosome 1p in primary hepatocellular carcinoma
    • Shao J, Li H, Liew CT, Wu Q, Liang X, Hou J. [A preliminary study of loss of heterozygosity on chromosome 1p in primary hepatocellular carcinoma]. Zhonghua bing li xue za zhi 1999;28:28-30.
    • (1999) Zhonghua Bing Li Xue Za Zhi , vol.28 , pp. 28-30
    • Shao, J.1    Li, H.2    Liew, C.T.3    Wu, Q.4    Liang, X.5    Hou, J.6
  • 12
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J, Nikolaev AY, Imai S, Chen D, Su F, Shiloh A, et al. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 2001;107:137-48.
    • (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
  • 13
    • 0029665214 scopus 로고    scopus 로고
    • Analysis of the specificity of the AMP-activated protein kinase by site-directed mutagenesis of bacterially expressed 3-hydroxy 3-methylglutaryl-CoA reductase, using a single primer variant of the unique-site-elimination method
    • Ching YP, Davies SP, Hardie DG. Analysis of the specificity of the AMP-activated protein kinase by site-directed mutagenesis of bacterially expressed 3-hydroxy 3-methylglutaryl-CoA reductase, using a single primer variant of the unique-site-elimination method. Eur J Biochem 1996;237:800-8.
    • (1996) Eur J Biochem , vol.237 , pp. 800-808
    • Ching, Y.P.1    Davies, S.P.2    Hardie, D.G.3
  • 15
    • 0036290846 scopus 로고    scopus 로고
    • Protein kinase substrate recognition studied using the recombinant catalytic domain of AMP-activated protein kinase and a model substrate
    • Scott JW, Norman DG, Hawley SA, Kontogiannis L, Hardie DG. Protein kinase substrate recognition studied using the recombinant catalytic domain of AMP-activated protein kinase and a model substrate. J Mol Biol 2002;317:309-23.
    • (2002) J Mol Biol , vol.317 , pp. 309-323
    • Scott, J.W.1    Norman, D.G.2    Hawley, S.A.3    Kontogiannis, L.4    Hardie, D.G.5
  • 17
    • 63849149937 scopus 로고    scopus 로고
    • LKB1 and AMP-activated protein kinase control of mTOR signalling and growth
    • Oxf
    • Shaw RJ. LKB1 and AMP-activated protein kinase control of mTOR signalling and growth. Acta Physiol (Oxf) 2009;196:65-80.
    • (2009) Acta Physiol , vol.196 , pp. 65-80
    • Shaw, R.J.1
  • 18
    • 39049157916 scopus 로고    scopus 로고
    • Phosphatidylinositol ether lipid analogues induce AMP-activated protein kinase-dependent death in LKB1-mutant non small cell lung cancer cells
    • Memmott RM, Gills JJ, Hollingshead M, Powers MC, Chen Z, Kemp B, et al. Phosphatidylinositol ether lipid analogues induce AMP-activated protein kinase-dependent death in LKB1-mutant non small cell lung cancer cells. Cancer Res 2008;68:580-8.
    • (2008) Cancer Res , vol.68 , pp. 580-588
    • Memmott, R.M.1    Gills, J.J.2    Hollingshead, M.3    Powers, M.C.4    Chen, Z.5    Kemp, B.6
  • 19
    • 0035929359 scopus 로고    scopus 로고
    • Cell cycle regulation via p53 phosphorylation by a 50-AMP activated protein kinase activator, 5-aminoimidazole- 4-carboxamide-1-beta-D- ribofuranoside, in a human hepatocellular carcinoma cell line
    • Imamura K, Ogura T, Kishimoto A, Kaminishi M, Esumi H. Cell cycle regulation via p53 phosphorylation by a 50-AMP activated protein kinase activator, 5-aminoimidazole- 4-carboxamide-1-beta-D-ribofuranoside, in a human hepatocellular carcinoma cell line. Biochem Biophys Res Commun 2001;287:562-7.
    • (2001) Biochem Biophys Res Commun , vol.287 , pp. 562-567
    • Imamura, K.1    Ogura, T.2    Kishimoto, A.3    Kaminishi, M.4    Esumi, H.5
  • 20
    • 77953036555 scopus 로고    scopus 로고
    • The regulation of p53 by phosphorylation: A model for how distinct signals integrate into the p53 pathway
    • Albany NY
    • Maclaine NJ, Hupp TR. The regulation of p53 by phosphorylation: a model for how distinct signals integrate into the p53 pathway. Aging (Albany NY) 2009;1:490-502.
    • (2009) Aging , vol.1 , pp. 490-502
    • Maclaine, N.J.1    Hupp, T.R.2
  • 22
    • 0034617261 scopus 로고    scopus 로고
    • Histone deacetylases specifically down-regulate p53-dependent gene activation
    • Juan LJ, Shia WJ, Chen MH, Yang WM, Seto E, Lin YS, et al. Histone deacetylases specifically down-regulate p53-dependent gene activation. J Biol Chem 2000;275:20436-43.
    • (2000) J Biol Chem , vol.275 , pp. 20436-20443
    • Juan, L.J.1    Shia, W.J.2    Chen, M.H.3    Yang, W.M.4    Seto, E.5    Lin, Y.S.6
  • 24
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity
    • Kim EJ, Kho JH, Kang MR, Um SJ. Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity. Mol Cell 2007;28:277-90.
    • (2007) Mol Cell , vol.28 , pp. 277-290
    • Kim, E.J.1    Kho, J.H.2    Kang, M.R.3    Um, S.J.4
  • 26
    • 67349276169 scopus 로고    scopus 로고
    • AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
    • Canto C, Gerhart-Hines Z, Feige JN, Lagouge M, Noriega L, Milne JC, et al. AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature 2009;458:1056-60.
    • (2009) Nature , vol.458 , pp. 1056-1060
    • Canto, C.1    Gerhart-Hines, Z.2    Feige, J.N.3    Lagouge, M.4    Noriega, L.5    Milne, J.C.6
  • 27
    • 0035917536 scopus 로고    scopus 로고
    • Crystal structure of a SIR2 homolog-NAD complex
    • Min J, Landry J, Sternglanz R, Xu RM. Crystal structure of a SIR2 homolog-NAD complex. Cell 2001;105:269-79.
    • (2001) Cell , vol.105 , pp. 269-279
    • Min, J.1    Landry, J.2    Sternglanz, R.3    Xu, R.M.4
  • 29
    • 15244355745 scopus 로고    scopus 로고
    • Mechanism of sirtuin inhibition by nicotinamide: Altering the NAD(+) cosubstrate specificity of a Sir2 enzyme
    • Avalos JL, Bever KM, Wolberger C. Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme. Mol Cell 2005;17:855-68.
    • (2005) Mol Cell , vol.17 , pp. 855-868
    • Avalos, J.L.1    Bever, K.M.2    Wolberger, C.3
  • 30
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W, Roeder RG. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 1997;90:595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 32
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • Tait SW, Green DR. Mitochondria and cell death: outer membrane permeabilization and beyond. Nat Rev Mol Cell Biol 2010;11:621-32.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 33
    • 43049121395 scopus 로고    scopus 로고
    • Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt
    • Fulco M, Cen Y, Zhao P, Hoffman EP, McBurney MW, Sauve AA, et al. Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt. Dev Cell 2008;14:661-73.
    • (2008) Dev Cell , vol.14 , pp. 661-673
    • Fulco, M.1    Cen, Y.2    Zhao, P.3    Hoffman, E.P.4    McBurney, M.W.5    Sauve, A.A.6
  • 34
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • Langley E, Pearson M, Faretta M, Bauer UM, Frye RA, Minucci S, et al. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J 2002;21:2383-96.
    • (2002) EMBO J , vol.21 , pp. 2383-2396
    • Langley, E.1    Pearson, M.2    Faretta, M.3    Bauer, U.M.4    Frye, R.A.5    Minucci, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.