메뉴 건너뛰기




Volumn 37, Issue 5, 2014, Pages 709-714

Aberrant protein acylation is a common observation in inborn errors of acyl-CoA metabolism

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A; ACYL COENZYME A DEHYDROGENASE; FATTY ACID; LYSINE; PROTEIN;

EID: 84893704306     PISSN: 01418955     EISSN: 15732665     Source Type: Journal    
DOI: 10.1007/s10545-014-9684-9     Document Type: Article
Times cited : (63)

References (30)
  • 1
    • 78751676934 scopus 로고    scopus 로고
    • KAT(ching) metabolism by the tail: insight into the links between lysine acetyltransferases and metabolism
    • COI: 1:CAS:528:DC%2BC3MXmsFWisg%3D%3D, PID: 21243716
    • Albaugh BN, Arnold KM, Denu JM (2011) KAT(ching) metabolism by the tail: insight into the links between lysine acetyltransferases and metabolism. Chembiochem 12:290–298
    • (2011) Chembiochem , vol.12 , pp. 290-298
    • Albaugh, B.N.1    Arnold, K.M.2    Denu, J.M.3
  • 2
    • 84862022077 scopus 로고    scopus 로고
    • The NAD+ precursor nicotinamide riboside enhances oxidative metabolism and protects against high-fat diet-induced obesity
    • COI: 1:CAS:528:DC%2BC38Xot12ltb0%3D, PID: 22682224
    • Canto C, Houtkooper RH, Pirinen E et al (2012) The NAD+ precursor nicotinamide riboside enhances oxidative metabolism and protects against high-fat diet-induced obesity. Cell Metab 15:838–847
    • (2012) Cell Metab , vol.15 , pp. 838-847
    • Canto, C.1    Houtkooper, R.H.2    Pirinen, E.3
  • 3
    • 0038204415 scopus 로고    scopus 로고
    • The diverse functions of histone acetyltransferase complexes
    • Carrozza MJ, Utley RT, Workman JL, Cote J (2003) The diverse functions of histone acetyltransferase complexes. Trends Genet 19:321–329
    • (2003) Trends Genet , vol.19 , pp. 321-329
    • Carrozza, M.J.1    Utley, R.T.2    Workman, J.L.3    Cote, J.4
  • 4
    • 34248640428 scopus 로고    scopus 로고
    • Lysine propionylation and butyrylation are novel post-translational modifications in histones
    • COI: 1:CAS:528:DC%2BD2sXlsV2ktLs%3D, PID: 17267393
    • Chen Y, Sprung R, Tang Y et al (2007) Lysine propionylation and butyrylation are novel post-translational modifications in histones. Mol Cell Proteomics 6:812–819
    • (2007) Mol Cell Proteomics , vol.6 , pp. 812-819
    • Chen, Y.1    Sprung, R.2    Tang, Y.3
  • 5
    • 59149086584 scopus 로고    scopus 로고
    • Molecular characterization of propionyllysines in non-histone proteins
    • COI: 1:CAS:528:DC%2BD1MXpsFeqsg%3D%3D, PID: 18753126
    • Cheng Z, Tang Y, Chen Y et al (2009) Molecular characterization of propionyllysines in non-histone proteins. Mol Cell Proteomics 8:45–52
    • (2009) Mol Cell Proteomics , vol.8 , pp. 45-52
    • Cheng, Z.1    Tang, Y.2    Chen, Y.3
  • 6
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • COI: 1:CAS:528:DC%2BD1MXps1Ogt70%3D, PID: 19608861
    • Choudhary C, Kumar C, Gnad F et al (2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325:834–840
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3
  • 7
    • 81055122671 scopus 로고    scopus 로고
    • Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase
    • COI: 1:CAS:528:DC%2BC3MXhsVagtrnI, PID: 22076378
    • Du J, Zhou Y, Su X 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
  • 8
    • 84886686038 scopus 로고    scopus 로고
    • Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins
    • Feldman JL, Baeza J, Denu JM (2013) Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins. J Biol Chem 288:31350–31356
    • (2013) J Biol Chem , vol.288 , pp. 31350-31356
    • Feldman, J.L.1    Baeza, J.2    Denu, J.M.3
  • 9
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: biological insights and disease relevance
    • COI: 1:CAS:528:DC%2BC3cXivFekt7c%3D, PID: 20078221
    • Haigis MC, Sinclair DA (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
  • 10
    • 78651468707 scopus 로고    scopus 로고
    • Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction
    • COI: 1:CAS:528:DC%2BC3MXhtVWqtbs%3D, PID: 21255725
    • Hallows WC, Yu W, Smith BC et al (2011) Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction. Mol Cell 41:139–149
    • (2011) Mol Cell , vol.41 , pp. 139-149
    • Hallows, W.C.1    Yu, W.2    Smith, B.C.3
  • 11
    • 77950806433 scopus 로고    scopus 로고
    • SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
    • COI: 1:CAS:528:DC%2BC3cXislahsLY%3D, PID: 20203611
    • Hirschey MD, Shimazu T, Goetzman E 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
  • 12
    • 84881348520 scopus 로고    scopus 로고
    • Mitochondrial complex I deficiency increases protein acetylation and accelerates heart failure
    • COI: 1:CAS:528:DC%2BC3sXht1emtrjK, PID: 23931755
    • Karamanlidis G, Lee CF, Garcia-Menendez L et al (2013) Mitochondrial complex I deficiency increases protein acetylation and accelerates heart failure. Cell Metab 18:239–250
    • (2013) Cell Metab , vol.18 , pp. 239-250
    • Karamanlidis, G.1    Lee, C.F.2    Garcia-Menendez, L.3
  • 13
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • COI: 1:CAS:528:DC%2BD28Xpt1Snurk%3D, PID: 16916647
    • Kim SC, Sprung R, Chen Y et al (2006) Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 23:607–618
    • (2006) Mol Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3
  • 14
    • 84862573534 scopus 로고    scopus 로고
    • Protein lysine acylation and cysteine succination by intermediates of energy metabolism
    • COI: 1:CAS:528:DC%2BC38XmslGqsb0%3D, PID: 22571489
    • Lin H, Su X, He B (2012) Protein lysine acylation and cysteine succination by intermediates of energy metabolism. ACS Chem Biol 7:947–960
    • (2012) ACS Chem Biol , vol.7 , pp. 947-960
    • Lin, H.1    Su, X.2    He, B.3
  • 15
    • 84871107379 scopus 로고    scopus 로고
    • Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease
    • COI: 1:CAS:528:DC%2BC38XhvVeksb%2FN, PID: 23086951
    • 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
  • 16
    • 84880791239 scopus 로고    scopus 로고
    • SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
    • COI: 1:CAS:528:DC%2BC3sXhtVWlsLrI, PID: 23806337
    • Park J, Chen Y, Tishkoff DX 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
  • 17
    • 84889636259 scopus 로고    scopus 로고
    • SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks
    • COI: 1:CAS:528:DC%2BC3sXhvFOlsb3N, PID: 24315375
    • Rardin MJ, He W, Nishida Y 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
  • 18
    • 0034912742 scopus 로고    scopus 로고
    • Histone acetyltransferases
    • COI: 1:CAS:528:DC%2BD3MXlsVehtrc%3D, PID: 11395403
    • Roth SY, Denu JM, Allis CD (2001) Histone acetyltransferases. Annu Rev Biochem 70:81–120
    • (2001) Annu Rev Biochem , vol.70 , pp. 81-120
    • Roth, S.Y.1    Denu, J.M.2    Allis, C.D.3
  • 20
    • 33747167133 scopus 로고    scopus 로고
    • Secondary mitochondrial dysfunction in propionic aciduria: a pathogenic role for endogenous mitochondrial toxins
    • Schwab MA, Sauer SW, Okun JG et al (2006) Secondary mitochondrial dysfunction in propionic aciduria: a pathogenic role for endogenous mitochondrial toxins. Biochem J 398:107–112
    • (2006) Biochem J , vol.398 , pp. 107-112
    • Schwab, M.A.1    Sauer, S.W.2    Okun, J.G.3
  • 21
    • 73949123433 scopus 로고    scopus 로고
    • Calorie restriction alters mitochondrial protein acetylation
    • COI: 1:CAS:528:DC%2BD1MXht1Kkur7K, PID: 19594485
    • Schwer B, Eckersdorff M, Li Y et al (2009) Calorie restriction alters mitochondrial protein acetylation. Aging Cell 8:604–606
    • (2009) Aging Cell , vol.8 , pp. 604-606
    • Schwer, B.1    Eckersdorff, M.2    Li, Y.3
  • 22
    • 78649509214 scopus 로고    scopus 로고
    • SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production
    • COI: 1:CAS:528:DC%2BC3cXhsVyhs7jI, PID: 21109197
    • Shimazu T, Hirschey MD, Hua L et al (2010) SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production. Cell Metab 12:654–661
    • (2010) Cell Metab , vol.12 , pp. 654-661
    • Shimazu, T.1    Hirschey, M.D.2    Hua, L.3
  • 23
    • 84891848670 scopus 로고    scopus 로고
    • Small-molecule allosteric activators of sirtuins
    • Sinclair DA, Guarente L (2014) Small-molecule allosteric activators of sirtuins. Annu Rev Pharmacol Toxicol 54:363–380
    • (2014) Annu Rev Pharmacol Toxicol , vol.54 , pp. 363-380
    • Sinclair, D.A.1    Guarente, L.2
  • 24
    • 78651468722 scopus 로고    scopus 로고
    • Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction
    • COI: 1:CAS:528:DC%2BC3cXhsVygsLfI, PID: 21094524
    • Someya S, Yu W, Hallows WC et al (2010) Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction. Cell 143:802–812
    • (2010) Cell , vol.143 , pp. 802-812
    • Someya, S.1    Yu, W.2    Hallows, W.C.3
  • 25
    • 78649328799 scopus 로고    scopus 로고
    • Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling
    • COI: 1:CAS:528:DC%2BC3cXhsVGnsrjE, PID: 20863707
    • Verdin E, Hirschey MD, Finley LWS, Haigis MC (2010) Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling. Trends Biochem Sci 35:669–675
    • (2010) Trends Biochem Sci , vol.35 , pp. 669-675
    • Verdin, E.1    Hirschey, M.D.2    Finley, L.W.S.3    Haigis, M.C.4
  • 26
    • 84885155285 scopus 로고    scopus 로고
    • Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix
    • COI: 1:CAS:528:DC%2BC3sXhsFKqsbzP, PID: 23946487
    • Wagner GR, Payne RM (2013) Widespread and enzyme-independent Nε-acetylation and Nε-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
  • 27
    • 84883307077 scopus 로고    scopus 로고
    • Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation
    • COI: 1:CAS:528:DC%2BC3sXht12isL%2FL, PID: 23954790
    • Weinert BT, Schölz C, Wagner SA et al (2013) Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Rep 4:842–851. doi:10.1016/j.celrep.2013.07.024
    • (2013) Cell Rep , vol.4 , pp. 842-851
    • Weinert, B.T.1    Schölz, C.2    Wagner, S.A.3
  • 29
    • 84861163510 scopus 로고    scopus 로고
    • Lysine succinylation and lysine malonylation in histones
    • COI: 1:CAS:528:DC%2BC38XotlWls78%3D, PID: 22389435
    • Xie Z, Dai J, Dai L et al (2012) Lysine succinylation and lysine malonylation in histones. Mol Cell Proteomics 11:100–107
    • (2012) Mol Cell Proteomics , vol.11 , pp. 100-107
    • Xie, Z.1    Dai, J.2    Dai, L.3
  • 30
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • COI: 1:CAS:528:DC%2BC3cXitVSjtbo%3D, PID: 20167786
    • Zhao S, Xu W, Jiang W et al (2010) Regulation of cellular metabolism by protein lysine acetylation. Science 327:1000–1004
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1    Xu, W.2    Jiang, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.