메뉴 건너뛰기




Volumn 1804, Issue 8, 2010, Pages 1658-1665

Function and regulation of the mitochondrial Sirtuin isoform Sirt5 in Mammalia

Author keywords

Deacetylase; Function; Metabolism; Mitochondria; Sirt5; Sirtuin

Indexed keywords

ANTINEOPLASTIC AGENT; CAMBINOL; EX 527; HYDROLASE INHIBITOR; ISOENZYME; ISONICOTINAMIDE; MITOCHONDRIAL ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; RESVERATROL; SIRTUIN 1; SIRTUIN 2; SIRTUIN 3; SIRTUIN 5; SURAMIN; UNCLASSIFIED DRUG;

EID: 77953285831     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.09.011     Document Type: Review
Times cited : (63)

References (66)
  • 3
    • 13944253348 scopus 로고    scopus 로고
    • Calorie restriction-the SIR2 connection
    • Guarente L., and Picard F. Calorie restriction-the SIR2 connection. Cell 120 (2005) 473-482
    • (2005) Cell , vol.120 , pp. 473-482
    • Guarente, L.1    Picard, F.2
  • 4
    • 33845868198 scopus 로고    scopus 로고
    • Sirtuins as potential targets for metabolic syndrome
    • Guarente L. Sirtuins as potential targets for metabolic syndrome. Nature 444 (2006) 868-874
    • (2006) Nature , vol.444 , pp. 868-874
    • Guarente, L.1
  • 5
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey V.G., Faulkner R., and Mirsky A.E. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl. Acad. Sci. U.S.A. 51 (1964) 786-794
    • (1964) Proc. Natl. Acad. Sci. U.S.A. , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 6
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • Glozak M.A., Sengupta N., Zhang X., and Seto E. Acetylation and deacetylation of non-histone proteins. Gene 363 (2005) 15-23
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 7
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: codified crosstalk with other posttranslational modifications
    • Yang X.J., and Seto E. Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol. Cell 31 (2008) 449-461
    • (2008) Mol. Cell , vol.31 , pp. 449-461
    • Yang, X.J.1    Seto, E.2
  • 8
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: molecular mechanisms of action
    • Xu W.S., Parmigiani R.B., and Marks P.A. Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene 26 (2007) 5541-5552
    • (2007) Oncogene , vol.26 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 9
    • 27944433010 scopus 로고    scopus 로고
    • Structure and activity of enzymes that remove histone modifications
    • Holbert M.A., and Marmorstein R. Structure and activity of enzymes that remove histone modifications. Curr. Opin. Struct. Biol. 15 (2005) 673-680
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 673-680
    • Holbert, M.A.1    Marmorstein, R.2
  • 11
    • 65249091951 scopus 로고    scopus 로고
    • Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogs and 32P-NAD
    • J. Du, H. Jiang and H. Lin, Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogs and 32P-NAD, Biochemistry 48 (2009) 2878-2890.
    • (2009) Biochemistry , vol.48 , pp. 2878-2890
    • Du, J.1    Jiang, H.2    Lin, H.3
  • 12
    • 25444484672 scopus 로고    scopus 로고
    • Small molecule regulation of Sir2 protein deacetylases
    • Grubisha O., Smith B.C., and Denu J.M. Small molecule regulation of Sir2 protein deacetylases. FEBS J. 272 (2005) 4607-4616
    • (2005) FEBS J. , vol.272 , pp. 4607-4616
    • Grubisha, O.1    Smith, B.C.2    Denu, J.M.3
  • 14
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein M., McVey M., and Guarente L. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 13 (1999) 2570-2580
    • (1999) Genes Dev. , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 17
    • 33744466971 scopus 로고    scopus 로고
    • Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription
    • Ford E., Voit R., Liszt G., Magin C., Grummt I., and Guarente L. Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription. Genes Dev. 20 (2006) 1075-1080
    • (2006) Genes Dev. , vol.20 , pp. 1075-1080
    • Ford, E.1    Voit, R.2    Liszt, G.3    Magin, C.4    Grummt, I.5    Guarente, L.6
  • 19
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North B.J., Marshall B.L., Borra M.T., Denu J.M., and Verdin E. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol. Cell 11 (2003) 437-444
    • (2003) Mol. Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 20
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita E., Park J.Y., Burneskis J.M., Barrett J.C., and Horikawa I. Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell 16 (2005) 4623-4635
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 21
    • 38649132337 scopus 로고    scopus 로고
    • Mitochondria-a nexus for aging, calorie restriction, and sirtuins?
    • Guarente L. Mitochondria-a nexus for aging, calorie restriction, and sirtuins?. Cell 132 (2008) 171-176
    • (2008) Cell , vol.132 , pp. 171-176
    • Guarente, L.1
  • 22
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban R.S., Nemoto S., and Finkel T. Mitochondria, oxidants, and aging. Cell 120 (2005) 483-495
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 26
    • 33745889628 scopus 로고    scopus 로고
    • Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2
    • Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., and Verdin E. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 10224-10229
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 10224-10229
    • Schwer, B.1    Bunkenborg, J.2    Verdin, R.O.3    Andersen, J.S.4    Verdin, E.5
  • 27
    • 33745931074 scopus 로고    scopus 로고
    • Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
    • Hallows W.C., Lee S., and Denu J.M. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 10230-10235
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 10230-10235
    • Hallows, W.C.1    Lee, S.2    Denu, J.M.3
  • 31
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • Shi T., Wang F., Stieren E., and Tong Q. SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J. Biol. Chem. 280 (2005) 13560-13567
    • (2005) J. Biol. Chem. , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 34
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273 (2000) 793-798
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 35
    • 32944479897 scopus 로고    scopus 로고
    • Assignment of the NAD-dependent deacetylase sirtuin 5 gene (SIRT5) to human chromosome band 6p23 by in situ hybridization
    • Mahlknecht U., Ho A.D., Letzel S., and Voelter-Mahlknecht S. Assignment of the NAD-dependent deacetylase sirtuin 5 gene (SIRT5) to human chromosome band 6p23 by in situ hybridization. Cytogenet. Genome Res. 112 (2006) 208-212
    • (2006) Cytogenet. Genome Res. , vol.112 , pp. 208-212
    • Mahlknecht, U.1    Ho, A.D.2    Letzel, S.3    Voelter-Mahlknecht, S.4
  • 36
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
    • Nakagawa T., Lomb D.J., Haigis M.C., and Guarente L. SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 137 (2009) 560-570
    • (2009) Cell , vol.137 , pp. 560-570
    • Nakagawa, T.1    Lomb, D.J.2    Haigis, M.C.3    Guarente, L.4
  • 37
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • Schwer B., North B.J., Frye R.A., Ott M., and Verdin E. The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J. Cell Biol. 158 (2002) 647-657
    • (2002) J. Cell Biol. , vol.158 , pp. 647-657
    • Schwer, B.1    North, B.J.2    Frye, R.A.3    Ott, M.4    Verdin, E.5
  • 38
    • 37549026223 scopus 로고    scopus 로고
    • Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5
    • Nakamura Y., Ogura M., Tanaka D., and Inagaki N. Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5. Biochem. Biophys. Res. Commun. 366 (2008) 174-179
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 174-179
    • Nakamura, Y.1    Ogura, M.2    Tanaka, D.3    Inagaki, N.4
  • 39
    • 3343024449 scopus 로고    scopus 로고
    • Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases
    • Borra M.T., Langer M.R., Slama J.T., and Denu J.M. Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases. Biochemistry 43 (2004) 9877-9887
    • (2004) Biochemistry , vol.43 , pp. 9877-9887
    • Borra, M.T.1    Langer, M.R.2    Slama, J.T.3    Denu, J.M.4
  • 41
    • 27744569240 scopus 로고    scopus 로고
    • Unstructured conformations are a substrate requirement for the Sir2 family of NAD-dependent protein deacetylases
    • Khan A.N., and Lewis P.N. Unstructured conformations are a substrate requirement for the Sir2 family of NAD-dependent protein deacetylases. J. Biol. Chem. 280 (2005) 36073-36078
    • (2005) J. Biol. Chem. , vol.280 , pp. 36073-36078
    • Khan, A.N.1    Lewis, P.N.2
  • 42
    • 58149339917 scopus 로고    scopus 로고
    • Opposing effects of sirtuins on neuronal survival: SIRT1-mediated neuroprotection is independent of its deacetylase activity
    • Pfister J.A., Ma C., Morrison B.E., and D'Mello S.R. Opposing effects of sirtuins on neuronal survival: SIRT1-mediated neuroprotection is independent of its deacetylase activity. PLoS One 3 (2008) e4090
    • (2008) PLoS One , vol.3
    • Pfister, J.A.1    Ma, C.2    Morrison, B.E.3    D'Mello, S.R.4
  • 43
    • 12244299825 scopus 로고    scopus 로고
    • Caloric restriction increases gluconeogenic and transaminase enzyme activities in mouse liver
    • Hagopian K., Ramsey J.J., and Weindruch R. Caloric restriction increases gluconeogenic and transaminase enzyme activities in mouse liver. Exp. Gerontol. 38 (2003) 267-278
    • (2003) Exp. Gerontol. , vol.38 , pp. 267-278
    • Hagopian, K.1    Ramsey, J.J.2    Weindruch, R.3
  • 44
    • 46049084164 scopus 로고    scopus 로고
    • Alcohol alters hepatic FoxO1, p53, and mitochondrial SIRT5 deacetylation function
    • Lieber C.S., Leo M.A., Wang X., and Decarli L.M. Alcohol alters hepatic FoxO1, p53, and mitochondrial SIRT5 deacetylation function. Biochem. Biophys. Res. Commun. 373 (2008) 246-252
    • (2008) Biochem. Biophys. Res. Commun. , vol.373 , pp. 246-252
    • Lieber, C.S.1    Leo, M.A.2    Wang, X.3    Decarli, L.M.4
  • 45
    • 65649095105 scopus 로고    scopus 로고
    • Alcohol-induced protein hyperacetylation: mechanisms and consequences
    • Shepard B.D., and Tuma P.L. Alcohol-induced protein hyperacetylation: mechanisms and consequences. World J. Gastroenterol. 15 (2009) 1219-1230
    • (2009) World J. Gastroenterol. , vol.15 , pp. 1219-1230
    • Shepard, B.D.1    Tuma, P.L.2
  • 46
    • 25144496904 scopus 로고    scopus 로고
    • The Sir 2 family of protein deacetylases
    • Denu J.M. The Sir 2 family of protein deacetylases. Curr. Opin. Chem. Biol. 9 (2005) 431-440
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 431-440
    • Denu, J.M.1
  • 49
    • 15244355745 scopus 로고    scopus 로고
    • Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme
    • Avalos J.L., Bever K.M., and Wolberger C. Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme. Mol. Cell. 17 (2005) 855-868
    • (2005) Mol. Cell. , vol.17 , pp. 855-868
    • Avalos, J.L.1    Bever, K.M.2    Wolberger, C.3
  • 50
    • 2942534101 scopus 로고    scopus 로고
    • Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases
    • Zhao K., Harshaw R., Chai X., and Marmorstein R. Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 8563-8568
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 8563-8568
    • Zhao, K.1    Harshaw, R.2    Chai, X.3    Marmorstein, R.4
  • 51
    • 0141618441 scopus 로고    scopus 로고
    • Structure and autoregulation of the yeast Hst2 homolog of Sir2
    • Zhao K., Chai X., Clements A., and Marmorstein R. Structure and autoregulation of the yeast Hst2 homolog of Sir2. Nat. Struct. Biol. 10 (2003) 864-871
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 864-871
    • Zhao, K.1    Chai, X.2    Clements, A.3    Marmorstein, R.4
  • 52
    • 42049113213 scopus 로고    scopus 로고
    • Inhibitors of NAD+ dependent histone deacetylases (sirtuins)
    • Neugebauer R.C., Sippl W., and Jung M. Inhibitors of NAD+ dependent histone deacetylases (sirtuins). Curr. Pharm. Des. 14 (2008) 562-573
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 562-573
    • Neugebauer, R.C.1    Sippl, W.2    Jung, M.3
  • 53
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity
    • Kim E.J., Kho J.H., Kang M.R., and Um S.J. Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity. Mol. Cell 28 (2007) 277-290
    • (2007) Mol. Cell , vol.28 , pp. 277-290
    • Kim, E.J.1    Kho, J.H.2    Kang, M.R.3    Um, S.J.4
  • 54
    • 40849135481 scopus 로고    scopus 로고
    • The Sirtuin family: therapeutic targets to treat diseases of aging
    • Milne J.C., and Denu J.M. The Sirtuin family: therapeutic targets to treat diseases of aging. Curr. Opin. Chem. Biol. 12 (2008) 11-17
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 11-17
    • Milne, J.C.1    Denu, J.M.2
  • 57
    • 41649103241 scopus 로고    scopus 로고
    • Structure-activity studies on splitomicin derivatives as sirtuin inhibitors and computational prediction of binding mode
    • Neugebauer R.C., Uchiechowska U., Meier R., Hruby H., Valkov V., Verdin E., Sippl W., and Jung M. Structure-activity studies on splitomicin derivatives as sirtuin inhibitors and computational prediction of binding mode. J. Med. Chem. 51 (2008) 1203-1213
    • (2008) J. Med. Chem. , vol.51 , pp. 1203-1213
    • Neugebauer, R.C.1    Uchiechowska, U.2    Meier, R.3    Hruby, H.4    Valkov, V.5    Verdin, E.6    Sippl, W.7    Jung, M.8
  • 58
    • 56349167518 scopus 로고    scopus 로고
    • Polyanionic drugs and viral oncogenesis: a novel approach to control infection, tumor-associated inflammation and angiogenesis
    • Urbinati C., Chiodelli P., and Rusnati M. Polyanionic drugs and viral oncogenesis: a novel approach to control infection, tumor-associated inflammation and angiogenesis. Molecules 13 (2008) 2758-2785
    • (2008) Molecules , vol.13 , pp. 2758-2785
    • Urbinati, C.1    Chiodelli, P.2    Rusnati, M.3
  • 60
    • 0029123736 scopus 로고
    • Inhibition of rat steroid 5 alpha-reductase (isozyme 1) by suramin
    • Taylor M.F., Bhattacharyya A.K., and Collins D.C. Inhibition of rat steroid 5 alpha-reductase (isozyme 1) by suramin. Steroids 60 (1995) 452-456
    • (1995) Steroids , vol.60 , pp. 452-456
    • Taylor, M.F.1    Bhattacharyya, A.K.2    Collins, D.C.3
  • 61
    • 35548936745 scopus 로고    scopus 로고
    • Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins)
    • Trapp J., Meier R., Hongwiset D., Kassack M.U., Sippl W., and Jung M. Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins). ChemMedChem 2 (2007) 1419-1431
    • (2007) ChemMedChem , vol.2 , pp. 1419-1431
    • Trapp, J.1    Meier, R.2    Hongwiset, D.3    Kassack, M.U.4    Sippl, W.5    Jung, M.6
  • 63
    • 33745962138 scopus 로고    scopus 로고
    • Therapeutic potential of resveratrol: the in vivo evidence
    • Baur J.A., and Sinclair D.A. Therapeutic potential of resveratrol: the in vivo evidence. Nat. Rev. Drug Discov. 5 (2006) 493-506
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 493-506
    • Baur, J.A.1    Sinclair, D.A.2
  • 64
    • 46749136505 scopus 로고    scopus 로고
    • Resveratrol: one molecule, many targets
    • Pirola L., and Frojdo S. Resveratrol: one molecule, many targets. IUBMB Life 60 (2008) 323-332
    • (2008) IUBMB Life , vol.60 , pp. 323-332
    • Pirola, L.1    Frojdo, S.2
  • 65
    • 13944258164 scopus 로고    scopus 로고
    • Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition
    • Sauve A.A., Moir R.D., Schramm V.L., and Willis I.M. Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition. Mol. Cell 17 (2005) 595-601
    • (2005) Mol. Cell , vol.17 , pp. 595-601
    • Sauve, A.A.1    Moir, R.D.2    Schramm, V.L.3    Willis, I.M.4
  • 66
    • 33745534953 scopus 로고    scopus 로고
    • Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide
    • Hoff K.G., Avalos J.L., Sens K., and Wolberger C. Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide. Structure 14 (2006) 1231-1240
    • (2006) Structure , vol.14 , pp. 1231-1240
    • Hoff, K.G.1    Avalos, J.L.2    Sens, K.3    Wolberger, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.