메뉴 건너뛰기




Volumn 76, Issue , 2011, Pages 285-289

Regulation of glycolysis and gluconeogenesis by acetylation of PKM and PEPCK

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP); PYRUVATE KINASE; TRICHOSTATIN A; UBIQUITIN; CHAPERONE; PKM PROTEIN; PROTEASOME; UNCLASSIFIED DRUG;

EID: 84867414358     PISSN: 00917451     EISSN: None     Source Type: Book Series    
DOI: 10.1101/sqb.2011.76.010942     Document Type: Article
Times cited : (95)

References (24)
  • 1
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey VG, Faulkner R, Mirsky AE. 1964. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci 51: 786-794.
    • (1964) Proc Natl Acad Sci , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 3
    • 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, Zhao S, Xiong Y. 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    Zhao, S.6    Xiong, Y.7
  • 5
    • 75149150660 scopus 로고    scopus 로고
    • HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer
    • David CJ, Chen M, Assanah M, Canoll P, Manley JL. 2010. HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer. Nature 463: 364-368.
    • (2010) Nature , vol.463 , pp. 364-368
    • David, C.J.1    Chen, M.2    Assanah, M.3    Canoll, P.4    Manley, J.L.5
  • 6
    • 79551584971 scopus 로고    scopus 로고
    • Regulation of intermediary metabolism by protein acetylation
    • Guan KL, Xiong Y. 2010. Regulation of intermediary metabolism by protein acetylation. Trends in Biochem Sci 36: 108-116.
    • (2010) Trends in Biochem Sci , vol.36 , pp. 108-116
    • Guan, K.L.1    Xiong, Y.2
  • 7
    • 79959906869 scopus 로고    scopus 로고
    • Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase
    • Jiang W, Wang S, Xiao M, Lin Y, Zhou L, Lei Q, Xiong Y, Guan KL, Zhao S. 2011. Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase. Mol Cell 43: 33-44.
    • (2011) Mol Cell , vol.43 , pp. 33-44
    • Jiang, W.1    Wang, S.2    Xiao, M.3    Lin, Y.4    Zhou, L.5    Lei, Q.6    Xiong, Y.7    Guan, K.L.8    Zhao, S.9
  • 9
    • 79955398591 scopus 로고    scopus 로고
    • Otto Warburg's contributions to current concepts of cancer metabolism
    • Koppenol WH, Bounds PL, Dang CV. 2011. Otto Warburg's contributions to current concepts of cancer metabolism. Nat Rev Cancer 11: 325-337.
    • (2011) Nat Rev Cancer , vol.11 , pp. 325-337
    • Koppenol, W.H.1    Bounds, P.L.2    Dang, C.V.3
  • 10
    • 79959371914 scopus 로고    scopus 로고
    • Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth
    • Lv L, Li D, Zhao D, Lin R, Chu Y, Zhang H, Zha Z, Liu Y, Li Z, Xu Y, et al. 2011. Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth. Mol Cell 42: 719-730.
    • (2011) Mol Cell , vol.42 , pp. 719-730
    • Lv, L.1    Li, D.2    Zhao, D.3    Lin, R.4    Chu, Y.5    Zhang, H.6    Zha, Z.7    Liu, Y.8    Li, Z.9    Xu, Y.10
  • 11
    • 23044500915 scopus 로고    scopus 로고
    • Pyruvate kinase type M2 and its role in tumor growth and spreading
    • Mazurek S, Boschek CB, Hugo F, Eigenbrodt E. 2005. Pyruvate kinase type M2 and its role in tumor growth and spreading. Semin Cancer Biol 15: 300-308.
    • (2005) Semin Cancer Biol , vol.15 , pp. 300-308
    • Mazurek, S.1    Boschek, C.B.2    Hugo, F.3    Eigenbrodt, E.4
  • 12
    • 34547858913 scopus 로고    scopus 로고
    • Structure and acetyl-lysine recognition of the bromodomain
    • Mujtaba S, Zeng L, Zhou MM. 2007. Structure and acetyl-lysine recognition of the bromodomain. Oncogene 26: 5521-5527.
    • (2007) Oncogene , vol.26 , pp. 5521-5527
    • Mujtaba, S.1    Zeng, L.2    Zhou, M.M.3
  • 13
    • 0007852927 scopus 로고
    • The presence of acetyl groups of histones
    • Phillips DM. 1963. The presence of acetyl groups of histones. Biochem J 87: 258-263.
    • (1963) Biochem J , vol.87 , pp. 258-263
    • Phillips, D.M.1
  • 14
    • 78649521247 scopus 로고    scopus 로고
    • Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
    • Qiu X, Brown K, Hirschey MD, Verdin E, Chen D. 2010. Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. Cell Metab 12: 662-667.
    • (2010) Cell Metab , vol.12 , pp. 662-667
    • Qiu, X.1    Brown, K.2    Hirschey, M.D.3    Verdin, E.4    Chen, D.5
  • 15
    • 34147156192 scopus 로고    scopus 로고
    • HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53
    • Sasaki T, Gan EC, Wakeham A, Kornbluth S, Mak TW, Okada H. 2007. HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53. Genes Dev 21: 848-861.
    • (2007) Genes Dev , vol.21 , pp. 848-861
    • Sasaki, T.1    Gan, E.C.2    Wakeham, A.3    Kornbluth, S.4    Mak, T.W.5    Okada, H.6
  • 17
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: The metabolic requirements of cell proliferation
    • Vander Heiden MG, Cantley LC, Thompson CB. 2009. Understanding the Warburg effect: The metabolic requirements of cell proliferation. Science 324: 1029-1033.
    • (2009) Science , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1    Cantley, L.C.2    Thompson, C.B.3
  • 18
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Wang Q, Zhang Y, Yang C, Xiong H, Lin Y, Yao J, Li H, Xie L, Zhao W, Yao Y, et al. 2010. Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 327: 1004-1007.
    • (2010) Science , vol.327 , pp. 1004-1007
    • Wang, Q.1    Zhang, Y.2    Yang, C.3    Xiong, H.4    Lin, Y.5    Yao, J.6    Li, H.7    Xie, L.8    Zhao, W.9    Yao, Y.10
  • 19
    • 0001221508 scopus 로고
    • On respiratory impairment in cancer cells
    • Warburg O. 1956. On respiratory impairment in cancer cells. Science 124: 269-270.
    • (1956) Science , vol.124 , pp. 269-270
    • Warburg, O.1
  • 21
    • 70350462145 scopus 로고    scopus 로고
    • What is the metabolic role of phosphoenolpyruvate carboxykinase?
    • Yang J, Kalhan SC, Hanson RW. 2009a. What is the metabolic role of phosphoenolpyruvate carboxykinase? J Biol Chem 284: 27025-27029.
    • (2009) J Biol Chem , vol.284 , pp. 27025-27029
    • Yang, J.1    Kalhan, S.C.2    Hanson, R.W.3
  • 22
    • 70350439883 scopus 로고    scopus 로고
    • Aspects of the control of phosphoenolpyruvate carboxykinase gene transcription
    • Yang J, Reshef L, Cassuto H, Aleman G, Hanson RW. 2009b. Aspects of the control of phosphoenolpyruvate carboxykinase gene transcription. J Biol Chem 284: 27031-27035.
    • (2009) J Biol Chem , vol.84 , pp. 27031-27035
    • Yang, J.1    Reshef, L.2    Cassuto, H.3    Aleman, G.4    Hanson, R.W.5
  • 23
    • 67649395959 scopus 로고    scopus 로고
    • Lysine 88 acetylation negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals
    • Yu W, Lin Y, Yao J, Huang W, Lei Q, Xiong Y, Zhao S, Guan KL. 2009. Lysine 88 acetylation negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals. J Biol Chem 284: 13669-13675.
    • (2009) J Biol Chem , vol.84 , pp. 13669-13675
    • Yu, W.1    Lin, Y.2    Yao, J.3    Huang, W.4    Lei, Q.5    Xiong, Y.6    Zhao, S.7    Guan, K.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.