메뉴 건너뛰기




Volumn 116, Issue 9, 2006, Pages 2473-2483

The LXXLL motif of murine forkhead transcription factor FoxO1 mediates Sirt1-dependent transcriptional activity

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; GLUCOSE 6 PHOSPHATASE; LEUCINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PROTEIN KINASE B; RESVERATROL; SIRTUIN; SIRTUIN 1; SOMATOMEDIN BINDING PROTEIN 1; TRANSCRIPTION FACTOR FKHR; UNCLASSIFIED DRUG;

EID: 33748335578     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI25518     Document Type: Article
Times cited : (109)

References (52)
  • 2
    • 2342496712 scopus 로고    scopus 로고
    • FoxOs at the crossroads of cellular metabolism, differentiation, and transformation
    • Accili D. and Arden K.C. 2004. FoxOs at the crossroads of cellular metabolism, differentiation, and transformation. Cell. 117:421-426.
    • (2004) Cell , vol.117 , pp. 421-426
    • Accili, D.1    Arden, K.C.2
  • 3
    • 0033560896 scopus 로고    scopus 로고
    • Direct control of the Forkhead transcription factor AFX by protein kinase B
    • Kops G.J., et al. 1999. Direct control of the Forkhead transcription factor AFX by protein kinase B. Nature. 398:630-634.
    • (1999) Nature , vol.398 , pp. 630-634
    • Kops, G.J.1
  • 4
    • 0034459180 scopus 로고    scopus 로고
    • Forkhead transcription factor FKHR-L1 modulates cytokine-dependent transcriptional regulation of p27(KIP1)
    • Dijkers P.F., et al. 2000. Forkhead transcription factor FKHR-L1 modulates cytokine-dependent transcriptional regulation of p27(KIP1). Mol. Cell. Biol. 20:9138-9148.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 9138-9148
    • Dijkers, P.F.1
  • 5
    • 0036120725 scopus 로고    scopus 로고
    • Control of cell cycle exit and entry by protein kinase B-regulated forkhead transcription factors
    • Kops G.J., et al. 2002. Control of cell cycle exit and entry by protein kinase B-regulated forkhead transcription factors. Mol. Cell. Biol. 22:2025-2036.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2025-2036
    • Kops, G.J.1
  • 6
    • 0034643331 scopus 로고    scopus 로고
    • AFX-like forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1
    • Medema R.H., Kops G.J., Bos J.L., Burgering B.M. 2000. AFX-like forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1 Nature. 404:782-787.
    • (2000) Nature , vol.404 , pp. 782-787
    • Medema, R.H.1    Kops, G.J.2    Bos, J.L.3    Burgering, B.M.4
  • 7
    • 0037237279 scopus 로고    scopus 로고
    • The forkhead transcription factor Foxo1 regulates adipocyte differentiation
    • Nakae J., et al. 2003. The forkhead transcription factor Foxo1 regulates adipocyte differentiation. Dev. Cell. 4:119-129.
    • (2003) Dev. Cell. , vol.4 , pp. 119-129
    • Nakae, J.1
  • 8
    • 2342653278 scopus 로고    scopus 로고
    • Control of cyclin G2 mRNA expression by forkhead transcription factors: Novel mechanism for cell cycle control by phosphoinositide 3-kinase and forkhead
    • Martinez-Gac L., Marques M., Garcia Z., Campanero M.R., Carrera A.C. 2004. Control of cyclin G2 mRNA expression by forkhead transcription factors: novel mechanism for cell cycle control by phosphoinositide 3-kinase and forkhead. Mol. Cell. Biol. 24:2181-2189.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2181-2189
    • Martinez-Gac, L.1    Marques, M.2    Garcia, Z.3    Campanero, M.R.4    Carrera, A.C.5
  • 9
    • 0033582929 scopus 로고    scopus 로고
    • Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor
    • Brunet A., et al. 1999. Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell. 96:857-868.
    • (1999) Cell , vol.96 , pp. 857-868
    • Brunet, A.1
  • 10
    • 0034609737 scopus 로고    scopus 로고
    • Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1
    • Dijkers P.F., Medema R.H., Lammers J.W., Koenderman L., Coffer P.J. 2000. Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1. Curr. Biol. 10:1201-1204.
    • (2000) Curr. Biol. , vol.10 , pp. 1201-1204
    • Dijkers, P.F.1    Medema, R.H.2    Lammers, J.W.3    Koenderman, L.4    Coffer, P.J.5
  • 11
    • 0037134040 scopus 로고    scopus 로고
    • DNA repair pathway stimulated by the forkhead transcription factor FOXO3a through the Gadd45 protein
    • Tran H., et al. 2002. DNA repair pathway stimulated by the forkhead transcription factor FOXO3a through the Gadd45 protein. Science. 296:530-534.
    • (2002) Science , vol.296 , pp. 530-534
    • Tran, H.1
  • 12
    • 0037178789 scopus 로고    scopus 로고
    • FOXO fork-head transcription factors induce G(2)-M checkpoint in response to oxidative stress
    • Furukawa-Hibi Y., Yoshida-Araki K., Ohta T., Ikeda K., Motoyama N. 2002. FOXO fork-head transcription factors induce G(2)-M checkpoint in response to oxidative stress. J. Biol. Chem. 277:26729-26732.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26729-26732
    • Furukawa-Hibi, Y.1    Yoshida-Araki, K.2    Ohta, T.3    Ikeda, K.4    Motoyama, N.5
  • 13
    • 0042092531 scopus 로고    scopus 로고
    • Genes that act downstream of DAF-16 to influence the lifespan of Caenorhabditis elegans
    • Murphy C.T., et al. 2003. Genes that act downstream of DAF-16 to influence the lifespan of Caenorhabditis elegans. Nature. 424:277-283.
    • (2003) Nature , vol.424 , pp. 277-283
    • Murphy, C.T.1
  • 14
    • 0037136563 scopus 로고    scopus 로고
    • Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress
    • Kops G.J., et al. 2002. Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress. Nature. 419:316-321.
    • (2002) Nature , vol.419 , pp. 316-321
    • Kops, G.J.1
  • 15
    • 0037192473 scopus 로고    scopus 로고
    • Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway
    • Nemoto S. and Finkel T. 2002. Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway. Science. 295:2450-2452.
    • (2002) Science , vol.295 , pp. 2450-2452
    • Nemoto, S.1    Finkel, T.2
  • 16
    • 0035185021 scopus 로고    scopus 로고
    • The forkhead transcription factor Foxo1 (Fkhr) confers insulin sensitivity onto glucose-6-phosphatase expression
    • doi: 10.1172/JCI200112876.
    • Nakae J., Kitamura T., Silver D.L., Accili D. 2001. The forkhead transcription factor Foxo1 (Fkhr) confers insulin sensitivity onto glucose-6-phosphatase expression. J. Clin. Invest. 108:1359-1367 doi: 10.1172/JCI200112876.
    • (2001) J. Clin. Invest. , vol.108 , pp. 1359-1367
    • Nakae, J.1    Kitamura, T.2    Silver, D.L.3    Accili, D.4
  • 17
    • 0036787607 scopus 로고    scopus 로고
    • Regulation of insulin action and pancreatic beta-cell function by mutated alleles of the gene encoding forkhead transcription factor Foxo1
    • Nakae J., et al. 2002. Regulation of insulin action and pancreatic beta-cell function by mutated alleles of the gene encoding forkhead transcription factor Foxo1. Nat. Genet. 32:245-253.
    • (2002) Nat. Genet. , vol.32 , pp. 245-253
    • Nakae, J.1
  • 18
    • 15244339047 scopus 로고    scopus 로고
    • Foxo1 mediates insulin action on apoC-III and triglyceride metabolism
    • doi: 10.1172/JCI200419992.
    • Altomonte J., et al. 2004. Foxo1 mediates insulin action on apoC-III and triglyceride metabolism. J. Clin. Invest. 114:1493-1503 doi: 10.1172/JCI200419992.
    • (2004) J. Clin. Invest. , vol.114 , pp. 1493-1503
    • Altomonte, J.1
  • 19
    • 1542267804 scopus 로고    scopus 로고
    • Disruption of forkhead transcription factor (FOXO) family members in mice reveals their functional diversification
    • Hosaka T., et al. 2004. Disruption of forkhead transcription factor (FOXO) family members in mice reveals their functional diversification. Proc. Natl. Acad. Sci. U. S. A. 101:2975-2980.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2975-2980
    • Hosaka, T.1
  • 20
    • 0038152845 scopus 로고    scopus 로고
    • Suppression of ovarian follicle activation in mice by the transcription factor Foxo3a
    • Castrillon D.H., Miao L., Kollipara R., Horner J.W., DePinho R.A. 2003. Suppression of ovarian follicle activation in mice by the transcription factor Foxo3a. Science. 301:215-218.
    • (2003) Science , vol.301 , pp. 215-218
    • Castrillon, D.H.1    Miao, L.2    Kollipara, R.3    Horner, J.W.4    DePinho, R.A.5
  • 21
    • 0033118984 scopus 로고    scopus 로고
    • RNA polymerase II as a control panel for multiple coactivator complexes
    • Hampsey M. and Reinberg D. 1999. RNA polymerase II as a control panel for multiple coactivator complexes. Curr. Opin. Genet. Dev. 9:132-139.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 132-139
    • Hampsey, M.1    Reinberg, D.2
  • 23
    • 0032213938 scopus 로고    scopus 로고
    • Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation
    • McInerney E.M., et al. 1998. Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation. Genes Dev. 12:3357-3368.
    • (1998) Genes Dev. , vol.12 , pp. 3357-3368
    • McInerney, E.M.1
  • 24
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional coactivators mediates binding to nuclear receptors
    • Heery D.M., Kalkhoven E., Hoare S., Parker M.G. 1997. A signature motif in transcriptional coactivators mediates binding to nuclear receptors. Nature. 387:733-736.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 25
    • 0033522897 scopus 로고    scopus 로고
    • Insulin stimulates phosphorylation of the forkhead transcription factor FKHR on serine 253 through a Wortmannin-sensitive pathway
    • Nakae J., Park B.C., Accili D. 1999. Insulin stimulates phosphorylation of the forkhead transcription factor FKHR on serine 253 through a Wortmannin-sensitive pathway J. Biol. Chem. 274:15982-15985.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15982-15985
    • Nakae, J.1    Park, B.C.2    Accili, D.3
  • 26
    • 0033546439 scopus 로고    scopus 로고
    • Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B
    • Rena G., Guo S., Cichy S.C., Unterman T.G., Cohen P. 1999. Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B. J. Biol. Chem. 274:17179-17183.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17179-17183
    • Rena, G.1    Guo, S.2    Cichy, S.C.3    Unterman, T.G.4    Cohen, P.5
  • 27
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet A., et al. 2004. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science. 303:2011-2015.
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1
  • 28
    • 3042750643 scopus 로고    scopus 로고
    • Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity
    • Daitoku H., et al. 2004. Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity. Proc. Natl. Acad. Sci. U. S. A. 101:10042-10047.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10042-10047
    • Daitoku, H.1
  • 29
    • 1342264308 scopus 로고    scopus 로고
    • Mammalian SIRT1 represses forkhead transcription factors
    • Motta M.C., et al. 2004. Mammalian SIRT1 represses forkhead transcription factors. Cell. 116:551-563.
    • (2004) Cell , vol.116 , pp. 551-563
    • Motta, M.C.1
  • 30
    • 3142742707 scopus 로고    scopus 로고
    • FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1)
    • van der Horst A., et al. 2004. FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1). J. Biol. Chem. 279:28873-28879.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28873-28879
    • Van Der Horst, A.1
  • 31
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • Howitz K.T., et al. 2003. Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature. 425:191-196.
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1
  • 32
    • 20144365700 scopus 로고    scopus 로고
    • Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes
    • Frescas D., Valenti L., Accili D. 2005. Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes. J. Biol. Chem. 280:20589-20595.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20589-20595
    • Frescas, D.1    Valenti, L.2    Accili, D.3
  • 33
    • 0141727772 scopus 로고    scopus 로고
    • Inhibition of Foxo1 function is associated with improved fasting glycemia in diabetic mice
    • Altomonte J., et al. 2003. Inhibition of Foxo1 function is associated with improved fasting glycemia in diabetic mice. Am. J. Physiol. Endocrinol. Metab. 285:E718-E728.
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.285
    • Altomonte, J.1
  • 34
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S., Armstrong C.M., Kaeberlein M., Guarente L. 2000. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature. 403:795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 35
    • 12944283150 scopus 로고    scopus 로고
    • A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family
    • Smith J.S., et al. 2000. A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proc. Natl. Acad. Sci. U. S. A. 97:6658-6663.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6658-6663
    • Smith, J.S.1
  • 36
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum H.A. and Guarente L. 2001. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature. 410:227-230.
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 37
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J., et al. 2001. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell. 107:137-148.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1
  • 38
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri H., et al. 2001. hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell. 107:149-159.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1
  • 39
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • Langley E., et al. 2002. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J. 21:2383-2396.
    • (2002) EMBO J. , vol.21 , pp. 2383-2396
    • Langley, E.1
  • 40
    • 0141814680 scopus 로고    scopus 로고
    • Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
    • Cheng H.L., et al. 2003. Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice. Proc. Natl. Acad. Sci. U. S. A. 100:10794-10799.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10794-10799
    • Cheng, H.L.1
  • 41
    • 0043244921 scopus 로고    scopus 로고
    • Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state
    • Fulco M., et al. 2003. Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol. Cell. 12:51-62.
    • (2003) Mol. Cell. , vol.12 , pp. 51-62
    • Fulco, M.1
  • 42
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye R.A. 2000. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273:793-798.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 43
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC1alpha and SIRT1
    • Rodgers J.T., et al. 2005. Nutrient control of glucose homeostasis through a complex of PGC1alpha and SIRT1. Nature. 434:113-118.
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1
  • 44
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • Borra M.T., Smith B.C., Denu J.M. 2005. Mechanism of human SIRT1 activation by resveratrol. J. Biol. Chem. 280:17187-17195.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 45
    • 20444431507 scopus 로고    scopus 로고
    • Substrate-specific activation of sirtuins by resveratrol
    • Kaeberlein M., et al. 2005. Substrate-specific activation of sirtuins by resveratrol. J. Biol. Chem. 280:17038-17045.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17038-17045
    • Kaeberlein, M.1
  • 46
    • 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., Guarente L. 2005. A role for SIR-2.1 regulation of ER stress response genes in determining C. elegans life span. Dev. Cell. 9:605-615.
    • (2005) Dev. Cell. , vol.9 , pp. 605-615
    • Viswanathan, M.1    Kim, S.K.2    Berdichevsky, A.3    Guarente, L.4
  • 47
    • 27144468317 scopus 로고    scopus 로고
    • FoxO-dependent and -independent mechanisms mediate SirT1 effects on IGFBP-1 gene expression
    • Gan L., et al. 2005. FoxO-dependent and -independent mechanisms mediate SirT1 effects on IGFBP-1 gene expression. Biochem. Biophys. Res. Commun. 337:1092-1096.
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 1092-1096
    • Gan, L.1
  • 48
    • 0038187621 scopus 로고    scopus 로고
    • Insulin-regulated hepatic gluconeogenesis through FOXO1-PGC-1alpha interaction
    • Puigserver P., et al. 2003. Insulin-regulated hepatic gluconeogenesis through FOXO1-PGC-1alpha interaction. Nature. 423:550-555.
    • (2003) Nature , vol.423 , pp. 550-555
    • Puigserver, P.1
  • 49
    • 13244287966 scopus 로고    scopus 로고
    • Regulation of FoxO activity by CBP/p300-mediated acetylation
    • van der Heide L.P. and Smidt M.P. 2005. Regulation of FoxO activity by CBP/p300-mediated acetylation. Trends Biochem. Sci. 30:81-86.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 81-86
    • Van Der Heide, L.P.1    Smidt, M.P.2
  • 50
    • 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 H.R., Guarente L. 2006. C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span. Cell. 125:1165-1177.
    • (2006) Cell , vol.125 , pp. 1165-1177
    • Berdichevsky, A.1    Viswanathan, M.2    Horvitz, H.R.3    Guarente, L.4
  • 51
    • 2542435874 scopus 로고    scopus 로고
    • Bile acids regulate gluconeogenic gene expression via small heterodimer partner-mediated repression of hepatocyte nuclear factor 4 and Foxo1
    • Yamagata K., et al. 2004. Bile acids regulate gluconeogenic gene expression via small heterodimer partner-mediated repression of hepatocyte nuclear factor 4 and Foxo1. J. Biol. Chem. 279:23158-23165.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23158-23165
    • Yamagata, K.1
  • 52
    • 0034161544 scopus 로고    scopus 로고
    • Differential regulation of gene expression by insulin and IGF-1 receptors correlates with phosphorylation of a single amino acid residue in the forkhead transcription factor FKHR
    • Nakae J., Barr V., Accili D. 2000. Differential regulation of gene expression by insulin and IGF-1 receptors correlates with phosphorylation of a single amino acid residue in the forkhead transcription factor FKHR. EMBO J. 19:989-996.
    • (2000) EMBO J. , vol.19 , pp. 989-996
    • Nakae, J.1    Barr, V.2    Accili, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.