메뉴 건너뛰기




Volumn 9, Issue 8, 2014, Pages

Overexpression of mitochondrial sirtuins alters glycolysis and mitochondrial function in HEK293 cells

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; SIRTUIN; SIRTUIN 3; SIRTUIN 4; SIRTUIN 5; GLUCOSE; MITOCHONDRIAL PROTEIN; SIRT3 PROTEIN, HUMAN; SIRT4 PROTEIN, HUMAN; SIRT5 PROTEIN, HUMAN;

EID: 84919921312     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0106028     Document Type: Article
Times cited : (48)

References (41)
  • 1
    • 84875906572 scopus 로고    scopus 로고
    • Mitochondrial dynamics in the regulation of nutrient utilization and energy expenditure
    • Liesa M, Shirihai OS (2013) Mitochondrial dynamics in the regulation of nutrient utilization and energy expenditure. Cell Metab 17: 491-506.
    • (2013) Cell Metab , vol.17 , pp. 491-506
    • Liesa, M.1    Shirihai, O.S.2
  • 2
    • 64849104330 scopus 로고    scopus 로고
    • Matching cellular metabolic supply and demand in energy-stressed animals
    • Staples JF, Buck LT (2009) Matching cellular metabolic supply and demand in energy-stressed animals. Comp Biochem Physiol A Mol Integr Physiol 153: 95- 105.
    • (2009) Comp Biochem Physiol a Mol Integr Physiol , vol.153 , pp. 95-105
    • Staples, J.F.1    Buck, L.T.2
  • 3
    • 33846320060 scopus 로고    scopus 로고
    • Mechanisms of mitochondrial response to variations in energy demand in eukaryotic cells
    • DOI 10.1152/ajpcell.00208.2006
    • Devin A, Rigoulet M (2007) Mechanisms of mitochondrial response to variations in energy demand in eukaryotic cells. Am J Physiol Cell Physiol 292: C52-58. (Pubitemid 46115121)
    • (2007) American Journal of Physiology - Cell Physiology , vol.292 , Issue.1
    • Devin, A.1    Rigoulet, M.2
  • 4
    • 84867594869 scopus 로고    scopus 로고
    • Mitochondrial protein acetylation regulates metabolism
    • Anderson KA, Hirschey MD (2012) Mitochondrial protein acetylation regulates metabolism. Essays Biochem 52: 23-35.
    • (2012) Essays Biochem , vol.52 , pp. 23-35
    • Anderson, K.A.1    Hirschey, M.D.2
  • 5
    • 84860192261 scopus 로고    scopus 로고
    • Identification of a molecular component of the mitochondrial acetyltransferase programme: A novel role for GCN5L1
    • Scott I, Webster BR, Li JH, Sack MN (2012) Identification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1. Biochem J 443: 655-661.
    • (2012) Biochem J , vol.443 , pp. 655-661
    • Scott, I.1    Webster, B.R.2    Li, J.H.3    Sack, M.N.4
  • 6
    • 84885155285 scopus 로고    scopus 로고
    • Widespread and enzyme-independent Nepsilon-acetylation and Nepsilon-succinylation of proteins in the chemical conditions of the mitochondrial matrix
    • Wagner GR, Payne RM (2013) Widespread and enzyme-independent Nepsilon-acetylation and Nepsilon-succinylation of proteins in the chemical conditions of the mitochondrial matrix. J Biol Chem 288: 29036-29045.
    • (2013) J Biol Chem , vol.288 , pp. 29036-29045
    • Wagner, G.R.1    Payne, R.M.2
  • 7
    • 84898012702 scopus 로고    scopus 로고
    • Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases
    • Wagner GR, Hirschey MD (2014) Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases. Mol Cell 54: 5-16.
    • (2014) Mol Cell , vol.54 , pp. 5-16
    • Wagner, G.R.1    Hirschey, M.D.2
  • 8
    • 84871107379 scopus 로고    scopus 로고
    • Mitochondrial protein acylation and intermediary metabolism: Regulation by sirtuins and implications for metabolic disease
    • Newman JC, He W, Verdin E (2012) Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease. J Biol Chem 287: 42436-42443.
    • (2012) J Biol Chem , vol.287 , pp. 42436-42443
    • Newman, J.C.1    He, W.2    Verdin, E.3
  • 9
    • 81055122671 scopus 로고    scopus 로고
    • Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase
    • Du J, Zhou Y, Su X, Yu JJ, Khan S, et al. (2011) Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science 334: 806-809.
    • (2011) Science , vol.334 , pp. 806-809
    • Du, J.1    Zhou, Y.2    Su, X.3    Yu, J.J.4    Khan, S.5
  • 10
    • 84897565291 scopus 로고    scopus 로고
    • Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
    • Tan M, Peng C, Anderson KA, Chhoy P, Xie Z, et al. (2014) Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. Cell Metab 19: 605-617.
    • (2014) Cell Metab , vol.19 , pp. 605-617
    • Tan, M.1    Peng, C.2    Anderson, K.A.3    Chhoy, P.4    Xie, Z.5
  • 11
    • 84880791239 scopus 로고    scopus 로고
    • SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
    • Park J, Chen Y, Tishkoff DX, Peng C, Tan M, et al. (2013) SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways. Mol Cell 50: 919- 930.
    • (2013) Mol Cell , vol.50 , pp. 919-930
    • Park, J.1    Chen, Y.2    Tishkoff, D.X.3    Peng, C.4    Tan, M.5
  • 12
    • 84889636259 scopus 로고    scopus 로고
    • SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks
    • Rardin MJ, He W, Nishida Y, Newman JC, Carrico C, et al. (2013) SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks. Cell Metab 18: 920-933.
    • (2013) Cell Metab , vol.18 , pp. 920-933
    • Rardin, M.J.1    He, W.2    Nishida, Y.3    Newman, J.C.4    Carrico, C.5
  • 14
    • 65249091951 scopus 로고    scopus 로고
    • Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogues and 32P-NAD
    • Du J, Jiang H, Lin H (2009) Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogues and 32P-NAD. Biochemistry 48: 2878-2890.
    • (2009) Biochemistry , vol.48 , pp. 2878-2890
    • Du, J.1    Jiang, H.2    Lin, H.3
  • 15
    • 84878891625 scopus 로고    scopus 로고
    • SIRT4 coordinates the balance between lipid synthesis and catabolism by repressing malonyl CoA decarboxylase
    • Laurent G, German NJ, Saha AK, de Boer VC, Davies M, et al. (2013) SIRT4 coordinates the balance between lipid synthesis and catabolism by repressing malonyl CoA decarboxylase. Mol Cell 50: 686-698.
    • (2013) Mol Cell , vol.50 , pp. 686-698
    • Laurent, G.1    German, N.J.2    Saha, A.K.3    De Boer, V.C.4    Davies, M.5
  • 16
    • 84908500033 scopus 로고    scopus 로고
    • Bioenergetic Analysis of Intact Mammalian Cells Using the Seahorse XF24 Extracellular Flux Analyzer and a Luciferase ATP Assay
    • de Moura MB, Van Houten B (2014) Bioenergetic Analysis of Intact Mammalian Cells Using the Seahorse XF24 Extracellular Flux Analyzer and a Luciferase ATP Assay. Methods Mol Biol 1105: 589-602.
    • (2014) Methods Mol Biol , vol.1105 , pp. 589-602
    • De Moura, M.B.1    Van Houten, B.2
  • 17
    • 84867128553 scopus 로고    scopus 로고
    • Importance of glycolysis and oxidative phosphorylation in advanced melanoma
    • Ho J, de Moura MB, Lin Y, Vincent G, Thorne S, et al. (2012) Importance of glycolysis and oxidative phosphorylation in advanced melanoma. Mol Cancer 11: 76.
    • (2012) Mol Cancer , vol.11 , pp. 76
    • Ho, J.1    De Moura, M.B.2    Lin, Y.3    Vincent, G.4    Thorne, S.5
  • 18
    • 77955266829 scopus 로고    scopus 로고
    • Alterations in bioenergetics due to changes in mitochondrial DNA copy number
    • Qian W, Van Houten B (2010) Alterations in bioenergetics due to changes in mitochondrial DNA copy number. Methods 51: 452-457.
    • (2010) Methods , vol.51 , pp. 452-457
    • Qian, W.1    Van Houten, B.2
  • 19
    • 84874694989 scopus 로고    scopus 로고
    • Mitochondrial hyperfusion induced by loss of the fission protein Drp1 causes ATM-dependent G2/M arrest and aneuploidy through DNA replication stress
    • Qian W, Choi S, Gibson GA, Watkins SC, Bakkenist CJ, et al. (2012) Mitochondrial hyperfusion induced by loss of the fission protein Drp1 causes ATM-dependent G2/M arrest and aneuploidy through DNA replication stress. J Cell Sci 125: 5745-5757.
    • (2012) J Cell Sci , vol.125 , pp. 5745-5757
    • Qian, W.1    Choi, S.2    Gibson, G.A.3    Watkins, S.C.4    Bakkenist, C.J.5
  • 20
    • 0031596992 scopus 로고    scopus 로고
    • Multiwell 14CO2-capture assay for evaluation of substrate oxidation rates of cells in culture
    • Collins CL, Bode BP, Souba WW, Abcouwer SF (1998) Multiwell 14CO2- capture assay for evaluation of substrate oxidation rates of cells in culture. Biotechniques 24: 803-808. (Pubitemid 28211344)
    • (1998) BioTechniques , vol.24 , Issue.5 , pp. 803-808
    • Collins, C.L.1    Bode, B.P.2    Souba, W.W.3    Abcouwer, S.F.4
  • 21
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG, Dyer WJ (1959) A rapid method of total lipid extraction and purification. Can J Biochem Physiol 37: 911-917.
    • (1959) Can J Biochem Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 22
    • 79957979314 scopus 로고    scopus 로고
    • Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS
    • Chen Y, Zhang J, Lin Y, Lei Q, Guan KL, et al. (2011) Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS. EMBO Rep 12: 534-541.
    • (2011) EMBO Rep , vol.12 , pp. 534-541
    • Chen, Y.1    Zhang, J.2    Lin, Y.3    Lei, Q.4    Guan, K.L.5
  • 23
    • 84891503453 scopus 로고    scopus 로고
    • SIRT4 regulates ATP homeostasis and mediates a retrograde signaling via AMPK
    • Ho L, Titus AS, Banerjee KK, George S, Lin W, et al. (2013) SIRT4 regulates ATP homeostasis and mediates a retrograde signaling via AMPK. Aging (Albany NY) 5: 835-849.
    • (2013) Aging (Albany NY) , vol.5 , pp. 835-849
    • Ho, L.1    Titus, A.S.2    Banerjee, K.K.3    George, S.4    Lin, W.5
  • 24
    • 78049299600 scopus 로고    scopus 로고
    • Characterization of murine SIRT3 transcript variants and corresponding protein products
    • Yang Y, Hubbard BP, Sinclair DA, Tong Q (2010) Characterization of murine SIRT3 transcript variants and corresponding protein products. J Cell Biochem 111: 1051-1058.
    • (2010) J Cell Biochem , vol.111 , pp. 1051-1058
    • Yang, Y.1    Hubbard, B.P.2    Sinclair, D.A.3    Tong, Q.4
  • 25
    • 78751700840 scopus 로고    scopus 로고
    • Distinct regulation of mitochondrial localization and stability of two human Sirt5 isoforms
    • Matsushita N, Yonashiro R, Ogata Y, Sugiura A, Nagashima S, et al. (2011) Distinct regulation of mitochondrial localization and stability of two human Sirt5 isoforms. Genes Cells 16: 190-202.
    • (2011) Genes Cells , vol.16 , pp. 190-202
    • Matsushita, N.1    Yonashiro, R.2    Ogata, Y.3    Sugiura, A.4    Nagashima, S.5
  • 26
    • 79953180902 scopus 로고    scopus 로고
    • Assessing mitochondrial dysfunction in cells
    • Brand MD, Nicholls DG (2011) Assessing mitochondrial dysfunction in cells. Biochem J 435: 297-312.
    • (2011) Biochem J , vol.435 , pp. 297-312
    • Brand, M.D.1    Nicholls, D.G.2
  • 27
    • 0023339989 scopus 로고
    • Control of electron flux through the respiratory chain in mitochondria and cells
    • Brand MD, Murphy MP (1987) Control of electron flux through the respiratory chain in mitochondria and cells. Biol Rev Camb Philos Soc 62: 141-193.
    • (1987) Biol Rev Camb Philos Soc , vol.62 , pp. 141-193
    • Brand, M.D.1    Murphy, M.P.2
  • 28
    • 0014082605 scopus 로고
    • The redox state of free nicotinamideadenine dinucleotide in the cytoplasm and mitochondria of rat liver
    • Williamson DH, Lund P, Krebs HA (1967) The redox state of free nicotinamideadenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem J 103: 514-527.
    • (1967) Biochem J , vol.103 , pp. 514-527
    • Williamson, D.H.1    Lund, P.2    Krebs, H.A.3
  • 29
    • 77950806433 scopus 로고    scopus 로고
    • SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
    • Hirschey MD, Shimazu T, Goetzman E, Jing E, Schwer B, et al. (2010) SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. Nature 464: 121-125.
    • (2010) Nature , vol.464 , pp. 121-125
    • Hirschey, M.D.1    Shimazu, T.2    Goetzman, E.3    Jing, E.4    Schwer, B.5
  • 30
    • 84880328473 scopus 로고    scopus 로고
    • NAD and ADP-ribose metabolism in mitochondria
    • Dolle C, Rack JG, Ziegler M (2013) NAD and ADP-ribose metabolism in mitochondria. FEBS J 280: 3530-3541.
    • (2013) FEBS J , vol.280 , pp. 3530-3541
    • Dolle, C.1    Rack, J.G.2    Ziegler, M.3
  • 31
    • 33847711060 scopus 로고    scopus 로고
    • The power to reduce: Pyridine nucleotides - Small molecules with a multitude of functions
    • DOI 10.1042/BJ20061638
    • Pollak N, Dolle C, Ziegler M (2007) The power to reduce: pyridine nucleotides- small molecules with a multitude of functions. Biochem J 402: 205-218. (Pubitemid 46383418)
    • (2007) Biochemical Journal , vol.402 , Issue.2 , pp. 205-218
    • Pollak, N.1    Dolle, C.2    Ziegler, M.3
  • 33
    • 84884163378 scopus 로고    scopus 로고
    • An acetylome peptide microarray reveals specificities and deacetylation substrates for all human sirtuin isoforms
    • Rauh D, Fischer F, Gertz M, Lakshminarasimhan M, Bergbrede T, et al. (2013) An acetylome peptide microarray reveals specificities and deacetylation substrates for all human sirtuin isoforms. Nat Commun 4: 2327.
    • (2013) Nat Commun , vol.4 , pp. 2327
    • Rauh, D.1    Fischer, F.2    Gertz, M.3    Lakshminarasimhan, M.4    Bergbrede, T.5
  • 34
    • 78650248160 scopus 로고    scopus 로고
    • Sirt3- mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress
    • Tao R, Coleman MC, Pennington JD, Ozden O, Park SH, et al. (2010) Sirt3- mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress. Mol Cell 40: 893-904.
    • (2010) Mol Cell , vol.40 , pp. 893-904
    • Tao, R.1    Coleman, M.C.2    Pennington, J.D.3    Ozden, O.4    Park, S.H.5
  • 35
    • 84870352685 scopus 로고    scopus 로고
    • SIRT3 weighs heavily in the metabolic balance: A new role for SIRT3 in metabolic syndrome
    • Green MF, Hirschey MD (2013) SIRT3 weighs heavily in the metabolic balance: a new role for SIRT3 in metabolic syndrome. J Gerontol A Biol Sci Med Sci 68: 105-107.
    • (2013) J Gerontol a Biol Sci Med Sci , vol.68 , pp. 105-107
    • Green, M.F.1    Hirschey, M.D.2
  • 36
    • 84886993387 scopus 로고    scopus 로고
    • SIRT4 Represses Peroxisome Proliferator-Activated Receptor alpha Activity To Suppress Hepatic Fat Oxidation
    • Laurent G, de Boer VC, Finley LW, Sweeney M, Lu H, et al. (2013) SIRT4 Represses Peroxisome Proliferator-Activated Receptor alpha Activity To Suppress Hepatic Fat Oxidation. Mol Cell Biol 33: 4552-4561.
    • (2013) Mol Cell Biol , vol.33 , pp. 4552-4561
    • Laurent, G.1    De Boer, V.C.2    Finley, L.W.3    Sweeney, M.4    Lu, H.5
  • 37
    • 84876359638 scopus 로고    scopus 로고
    • SIRT4 has tumor-suppressive activity and regulates the cellular metabolic response to DNA damage by inhibiting mitochondrial glutamine metabolism
    • Jeong SM, Xiao C, Finley LW, Lahusen T, Souza AL, et al. (2013) SIRT4 has tumor-suppressive activity and regulates the cellular metabolic response to DNA damage by inhibiting mitochondrial glutamine metabolism. Cancer Cell 23: 450-463.
    • (2013) Cancer Cell , vol.23 , pp. 450-463
    • Jeong, S.M.1    Xiao, C.2    Finley, L.W.3    Lahusen, T.4    Souza, A.L.5
  • 39
    • 84903697938 scopus 로고    scopus 로고
    • SIRT5 is under the control of PGC-1alpha and AMPK and is involved in regulation of mitochondrial energy metabolism
    • Buler M, Aatsinki SM, Izzi V, Uusimaa J, Hakkola J (2014) SIRT5 is under the control of PGC-1alpha and AMPK and is involved in regulation of mitochondrial energy metabolism. FASEB J.
    • (2014) FASEB J
    • Buler, M.1    Aatsinki, S.M.2    Izzi, V.3    Uusimaa, J.4    Hakkola, J.5
  • 40
    • 84861019195 scopus 로고    scopus 로고
    • Measuring energy metabolism in cultured cells, including human pluripotent stem cells and differentiated cells
    • Zhang J, Nuebel E, Wisidagama DR, Setoguchi K, Hong JS, et al. (2012) Measuring energy metabolism in cultured cells, including human pluripotent stem cells and differentiated cells. Nat Protoc 7: 1068-1085.
    • (2012) Nat Protoc , vol.7 , pp. 1068-1085
    • Zhang, J.1    Nuebel, E.2    Wisidagama, D.R.3    Setoguchi, K.4    Hong, J.S.5
  • 41
    • 84896756082 scopus 로고    scopus 로고
    • Sirtuin-3 (SIRT3), a therapeutic target with oncogenic and tumor-suppressive function in cancer
    • Chen Y, Fu LL, Wen X, Wang XY, Liu J, et al. (2014) Sirtuin-3 (SIRT3), a therapeutic target with oncogenic and tumor-suppressive function in cancer. Cell Death Dis 5: e1047. Diseases
    • (2014) Cell Death Dis , vol.5
    • Chen, Y.1    Fu, L.L.2    Wen, X.3    Wang, X.Y.4    Liu, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.