메뉴 건너뛰기




Volumn 126, Issue 5, 2006, Pages 941-954

SIRT4 Inhibits Glutamate Dehydrogenase and Opposes the Effects of Calorie Restriction in Pancreatic β Cells

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; ADENOSINE TRIPHOSPHATE; AMINO ACID; GLUTAMATE DEHYDROGENASE; GLUTAMIC ACID; GLUTAMINE; INSULIN; MITOCHONDRIAL ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; PHOSPHODIESTERASE; SIRT4 PROTEIN; SIRTUIN; UNCLASSIFIED DRUG;

EID: 33748316536     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2006.06.057     Document Type: Article
Times cited : (1030)

References (55)
  • 1
    • 0036229718 scopus 로고    scopus 로고
    • Mutations in Saccharomyces cerevisiae gene SIR2 can have differential effects on in vivo silencing phenotypes and in vitro histone deacetylation activity
    • Armstrong C.M., Kaeberlein M., Imai S.I., and Guarente L. Mutations in Saccharomyces cerevisiae gene SIR2 can have differential effects on in vivo silencing phenotypes and in vitro histone deacetylation activity. Mol. Biol. Cell 13 (2002) 1427-1438
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1427-1438
    • Armstrong, C.M.1    Kaeberlein, M.2    Imai, S.I.3    Guarente, L.4
  • 2
    • 33744976074 scopus 로고    scopus 로고
    • C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span
    • Berdichevsky A., Viswanathan M., Horvitz R., and Guarente L. C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span. Cell 125 (2006) 1165-1177
    • (2006) Cell , vol.125 , pp. 1165-1177
    • Berdichevsky, A.1    Viswanathan, M.2    Horvitz, R.3    Guarente, L.4
  • 3
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander G., and Guarente L. The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 73 (2004) 417-435
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 7
    • 28844469898 scopus 로고    scopus 로고
    • Increase in activity during calorie restriction requires Sirt1
    • Chen D., Steele A.D., Lindquist S., and Guarente L. Increase in activity during calorie restriction requires Sirt1. Science 310 (2005) 1641
    • (2005) Science , vol.310 , pp. 1641
    • Chen, D.1    Steele, A.D.2    Lindquist, S.3    Guarente, L.4
  • 10
    • 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., Grummet 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    Grummet, I.5    Guarente, L.6
  • 11
    • 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
  • 12
    • 0035914304 scopus 로고    scopus 로고
    • Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening
    • Grozinger C.M., Chao E.D., Blackwell H.E., Moazed D., and Schreiber S.L. Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening. J. Biol. Chem. 276 (2001) 38837-38843
    • (2001) J. Biol. Chem. , vol.276 , pp. 38837-38843
    • Grozinger, C.M.1    Chao, E.D.2    Blackwell, H.E.3    Moazed, D.4    Schreiber, S.L.5
  • 13
    • 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
  • 14
    • 12244302878 scopus 로고    scopus 로고
    • Influence of age and caloric restriction on liver glycolytic enzyme activities and metabolite concentrations in mice
    • Hagopian K., Ramsey J.J., and Weindruch R. Influence of age and caloric restriction on liver glycolytic enzyme activities and metabolite concentrations in mice. Exp. Gerontol. 38 (2003) 253-266
    • (2003) Exp. Gerontol. , vol.38 , pp. 253-266
    • Hagopian, K.1    Ramsey, J.J.2    Weindruch, R.3
  • 15
    • 15544390626 scopus 로고    scopus 로고
    • Serine utilization in mouse liver: influence of caloric restriction and aging
    • Hagopian K., Ramsey J.J., and Weindruch R. Serine utilization in mouse liver: influence of caloric restriction and aging. FEBS Lett. 579 (2005) 2009-2013
    • (2005) FEBS Lett. , vol.579 , pp. 2009-2013
    • Hagopian, K.1    Ramsey, J.J.2    Weindruch, R.3
  • 17
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S., Armstrong C.M., Kaeberlein M., and Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403 (2000) 795-800
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 18
    • 0032524894 scopus 로고    scopus 로고
    • Enzymic, cysteine-specific ADP-ribosylation in bovine liver mitochondria
    • Jorcke D., Ziegler M., Herrero-Yraola A., and Schweiger M. Enzymic, cysteine-specific ADP-ribosylation in bovine liver mitochondria. Biochem. J. 332 (1998) 189-193
    • (1998) Biochem. J. , vol.332 , pp. 189-193
    • Jorcke, D.1    Ziegler, M.2    Herrero-Yraola, A.3    Schweiger, M.4
  • 19
    • 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
  • 21
    • 27744518040 scopus 로고    scopus 로고
    • FoxO1 protects against pancreatic beta cell failure through NeuroD and MafA induction
    • Kitamura Y.I., Kitamura T., Kruse J.P., Raum J.C., Stein R., Gu W., and Accili D. FoxO1 protects against pancreatic beta cell failure through NeuroD and MafA induction. Cell Metab. 2 (2005) 153-163
    • (2005) Cell Metab. , vol.2 , pp. 153-163
    • Kitamura, Y.I.1    Kitamura, T.2    Kruse, J.P.3    Raum, J.C.4    Stein, R.5    Gu, W.6    Accili, D.7
  • 25
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae
    • Lin S.J., Defossez P.A., and Guarente L. Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 289 (2000) 2126-2128
    • (2000) Science , vol.289 , pp. 2126-2128
    • Lin, S.J.1    Defossez, P.A.2    Guarente, L.3
  • 26
    • 0347128279 scopus 로고    scopus 로고
    • Calorie restriction extends yeast life span by lowering the level of NADH
    • Lin S.J., Ford E., Haigis M., Liszt G., and Guarente L. Calorie restriction extends yeast life span by lowering the level of NADH. Genes Dev. 18 (2004) 12-16
    • (2004) Genes Dev. , vol.18 , pp. 12-16
    • Lin, S.J.1    Ford, E.2    Haigis, M.3    Liszt, G.4    Guarente, L.5
  • 27
    • 20444409132 scopus 로고    scopus 로고
    • Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase
    • Liszt G., Ford E., Kurtev M., and Guarente L. Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J. Biol. Chem. 280 (2005) 21313-21320
    • (2005) J. Biol. Chem. , vol.280 , pp. 21313-21320
    • Liszt, G.1    Ford, E.2    Kurtev, M.3    Guarente, L.4
  • 28
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J., Nikolaev A.Y., Imai S., Chen D., Su F., Shiloh A., Guarente L., and Gu W. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 107 (2001) 137-148
    • (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    Guarente, L.7    Gu, W.8
  • 30
    • 0022483295 scopus 로고
    • Production of anti-(ADP-ribose) antibodies with the aid of a dinucleotide-pyrophosphatase-resistant hapten and their application for the detection of mono(ADP-ribosyl)ated polypeptides
    • Meyer T., and Hilz H. Production of anti-(ADP-ribose) antibodies with the aid of a dinucleotide-pyrophosphatase-resistant hapten and their application for the detection of mono(ADP-ribosyl)ated polypeptides. Eur. J. Biochem. 155 (1986) 157-165
    • (1986) Eur. J. Biochem. , vol.155 , pp. 157-165
    • Meyer, T.1    Hilz, H.2
  • 31
    • 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
  • 35
    • 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
  • 36
    • 0037108799 scopus 로고    scopus 로고
    • SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria
    • Onyango P., Celic I., McCaffery J.M., Boeke J.D., and Feinberg A.P. SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria. Proc. Natl. Acad. Sci. USA 99 (2002) 13653-13658
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13653-13658
    • Onyango, P.1    Celic, I.2    McCaffery, J.M.3    Boeke, J.D.4    Feinberg, A.P.5
  • 38
    • 0032879458 scopus 로고    scopus 로고
    • Controlling caloric consumption: protocols for rodents and rhesus monkeys
    • Pugh T.D., Klopp R.G., and Weindruch R. Controlling caloric consumption: protocols for rodents and rhesus monkeys. Neurobiol. Aging 20 (1999) 157-165
    • (1999) Neurobiol. Aging , vol.20 , pp. 157-165
    • Pugh, T.D.1    Klopp, R.G.2    Weindruch, R.3
  • 39
    • 0020659023 scopus 로고
    • Effect of age and diet on insulin secretion and insulin action in the rat
    • Reaven E., Wright D., Mondon C.E., Solomon R., Ho H., and Reaven G.M. Effect of age and diet on insulin secretion and insulin action in the rat. Diabetes 32 (1983) 175-180
    • (1983) Diabetes , vol.32 , pp. 175-180
    • Reaven, E.1    Wright, D.2    Mondon, C.E.3    Solomon, R.4    Ho, H.5    Reaven, G.M.6
  • 40
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers J.T., Lerin C., Haas W., Gygi S.P., Spiegelman B.M., and Puigserver P. Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434 (2005) 113-118
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5    Puigserver, P.6
  • 41
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • Rogina B., and Helfand S.L. Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl. Acad. Sci. USA 101 (2004) 15998-16003
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15998-16003
    • Rogina, B.1    Helfand, S.L.2
  • 42
    • 0035951072 scopus 로고    scopus 로고
    • Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions
    • Sauve A.A., Celic I., Avalos J., Deng H., Boeke J.D., and Schramm V.L. Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions. Biochemistry 40 (2001) 15456-15463
    • (2001) Biochemistry , vol.40 , pp. 15456-15463
    • Sauve, A.A.1    Celic, I.2    Avalos, J.3    Deng, H.4    Boeke, J.D.5    Schramm, V.L.6
  • 43
    • 0034113851 scopus 로고    scopus 로고
    • Evidence of endogenous mono-ADP-ribosylation of cardiac proteins via anti-ADP-ribosylarginine immunoreactivity
    • Schwab C.J., Colville M.J., Fullerton A.T., and McMahon K.K. Evidence of endogenous mono-ADP-ribosylation of cardiac proteins via anti-ADP-ribosylarginine immunoreactivity. Proc. Soc. Exp. Biol. Med. 223 (2000) 389-396
    • (2000) Proc. Soc. Exp. Biol. Med. , vol.223 , pp. 389-396
    • Schwab, C.J.1    Colville, M.J.2    Fullerton, A.T.3    McMahon, K.K.4
  • 44
    • 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
  • 45
    • 0019133275 scopus 로고
    • L-leucine and a nonmetabolized analogue activate pancreatic islet glutamate dehydrogenase
    • Sener A., and Malaisse W.J. L-leucine and a nonmetabolized analogue activate pancreatic islet glutamate dehydrogenase. Nature 288 (1980) 187-189
    • (1980) Nature , vol.288 , pp. 187-189
    • Sener, A.1    Malaisse, W.J.2
  • 46
    • 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
  • 47
    • 0031459980 scopus 로고    scopus 로고
    • Extrachromosomal rDNA circles--a cause of aging in yeast
    • Sinclair D.A., and Guarente L. Extrachromosomal rDNA circles--a cause of aging in yeast. Cell 91 (1997) 1033-1042
    • (1997) Cell , vol.91 , pp. 1033-1042
    • Sinclair, D.A.1    Guarente, L.2
  • 49
    • 0033598942 scopus 로고    scopus 로고
    • An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing
    • Tanny J.C., Dowd G.J., Huang J., Hilz H., and Moazed D. An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing. Cell 99 (1999) 735-745
    • (1999) Cell , vol.99 , pp. 735-745
    • Tanny, J.C.1    Dowd, G.J.2    Huang, J.3    Hilz, H.4    Moazed, D.5
  • 53
    • 27644585190 scopus 로고    scopus 로고
    • A role for SIR-2.1 regulation of ER stress response genes in determining C. elegans life span
    • Viswanathan M., Kim S.K., Berdichevsky A., and Guarente L. A role for SIR-2.1 regulation of ER stress response genes in determining C. elegans life span. Dev. Cell 9 (2005) 605-615
    • (2005) Dev. Cell , vol.9 , pp. 605-615
    • Viswanathan, M.1    Kim, S.K.2    Berdichevsky, A.3    Guarente, L.4
  • 54
    • 0023026817 scopus 로고
    • Regulation of acetyl-CoA carboxylase by ADP-ribosylation
    • Witters L.A., and McDermott J.M. Regulation of acetyl-CoA carboxylase by ADP-ribosylation. Biochemistry 25 (1986) 7216-7220
    • (1986) Biochemistry , vol.25 , pp. 7216-7220
    • Witters, L.A.1    McDermott, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.