메뉴 건너뛰기




Volumn 582, Issue 1, 2008, Pages 54-67

The FoxO transcription factors and metabolic regulation

Author keywords

FoxO; Insulin resistance; Metabolism; Phosphorylation; Transcription; Type 2 diabetes

Indexed keywords

FOXO4 PROTEIN; HISTONE ACETYLTRANSFERASE PCAF; INSULIN; NUCLEIC ACID BINDING PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; S6 KINASE; SIRTUIN 1; TRANSCRIPTION FACTOR FKHR; TRANSCRIPTION FACTOR FKHRL1; TRANSCRIPTION FACTOR FOXO; UNCLASSIFIED DRUG;

EID: 37349100520     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.11.025     Document Type: Short Survey
Times cited : (160)

References (133)
  • 1
    • 0017301265 scopus 로고
    • Non-ageing developmental variant of Caenorhabditis elegans
    • Klass M., and Hirsh D. Non-ageing developmental variant of Caenorhabditis elegans. Nature 260 (1976) 523-525
    • (1976) Nature , vol.260 , pp. 523-525
    • Klass, M.1    Hirsh, D.2
  • 2
    • 0019496482 scopus 로고
    • Interacting genes in nematode dauer larva formation
    • Riddle D.L., Swanson M.M., and Albert P.S. Interacting genes in nematode dauer larva formation. Nature 290 (1981) 668-671
    • (1981) Nature , vol.290 , pp. 668-671
    • Riddle, D.L.1    Swanson, M.M.2    Albert, P.S.3
  • 3
    • 0030659557 scopus 로고    scopus 로고
    • The Fork head transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. elegans
    • Ogg S., Paradis S., Gottlieb S., Patterson G.I., Lee L., Tissenbaum H.A., and Ruvkun G. The Fork head transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. elegans. Nature 389 (1997) 994-999
    • (1997) Nature , vol.389 , pp. 994-999
    • Ogg, S.1    Paradis, S.2    Gottlieb, S.3    Patterson, G.I.4    Lee, L.5    Tissenbaum, H.A.6    Ruvkun, G.7
  • 4
    • 0030657540 scopus 로고    scopus 로고
    • daf-16: An HNF-3/forkhead family member that can function to double the life-span of Caenorhabditis elegans
    • Lin K., Dorman J.B., Rodan A., and Kenyon C. daf-16: An HNF-3/forkhead family member that can function to double the life-span of Caenorhabditis elegans. Science 278 (1997) 1319-1322
    • (1997) Science , vol.278 , pp. 1319-1322
    • Lin, K.1    Dorman, J.B.2    Rodan, A.3    Kenyon, C.4
  • 5
    • 2342496712 scopus 로고    scopus 로고
    • FoxOs at the crossroads of cellular metabolism, differentiation, and transformation
    • Accili D., and Arden K.C. FoxOs at the crossroads of cellular metabolism, differentiation, and transformation. Cell 117 (2004) 421-426
    • (2004) Cell , vol.117 , pp. 421-426
    • Accili, D.1    Arden, K.C.2
  • 6
    • 27844497945 scopus 로고    scopus 로고
    • FOXO transcription factors at the interface between longevity and tumor suppression
    • Greer E.L., and Brunet A. FOXO transcription factors at the interface between longevity and tumor suppression. Oncogene 24 (2005) 7410-7425
    • (2005) Oncogene , vol.24 , pp. 7410-7425
    • Greer, E.L.1    Brunet, A.2
  • 7
    • 0027270989 scopus 로고
    • Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
    • Clark K.L., Halay E.D., Lai E., and Burley S.K. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature 364 (1993) 412-420
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 8
    • 0342614209 scopus 로고    scopus 로고
    • Unified nomenclature for the winged helix/forkhead transcription factors
    • Kaestner K.H., Knochel W., and Martinez D.E. Unified nomenclature for the winged helix/forkhead transcription factors. Genes Dev. 14 (2000) 142-146
    • (2000) Genes Dev. , vol.14 , pp. 142-146
    • Kaestner, K.H.1    Knochel, W.2    Martinez, D.E.3
  • 9
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley L.C. The phosphoinositide 3-kinase pathway. Science 296 (2002) 1655-1657
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 11
    • 0032759047 scopus 로고    scopus 로고
    • Forkhead transcription factors: new insights into protein kinase B (c-akt) signaling
    • Kops G.J., and Burgering B.M. Forkhead transcription factors: new insights into protein kinase B (c-akt) signaling. J. Mol. Med. 77 (1999) 656-665
    • (1999) J. Mol. Med. , vol.77 , pp. 656-665
    • Kops, G.J.1    Burgering, B.M.2
  • 12
    • 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., and Accili D. Insulin stimulates phosphorylation of the forkhead transcription factor FKHR on serine 253 through a Wortmannin-sensitive pathway. J. Biol. Chem. 274 (1999) 15982-15985
    • (1999) J. Biol. Chem. , vol.274 , pp. 15982-15985
    • Nakae, J.1    Park, B.C.2    Accili, D.3
  • 13
    • 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., and Cohen P. Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B. J. Biol. Chem. 274 (1999) 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
  • 14
    • 0039425278 scopus 로고    scopus 로고
    • Negative regulation of the forkhead transcription factor FKHR by Akt
    • Tang E.D., Nunez G., Barr F.G., and Guan K.L. Negative regulation of the forkhead transcription factor FKHR by Akt. J. Biol. Chem. 274 (1999) 16741-16746
    • (1999) J. Biol. Chem. , vol.274 , pp. 16741-16746
    • Tang, E.D.1    Nunez, G.2    Barr, F.G.3    Guan, K.L.4
  • 15
    • 0033595011 scopus 로고    scopus 로고
    • Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1
    • Biggs III W.H., Meisenhelder J., Hunter T., Cavenee W.K., and Arden K.C. Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1. Proc. Natl. Acad. Sci. USA 96 (1999) 7421-7426
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7421-7426
    • Biggs III, W.H.1    Meisenhelder, J.2    Hunter, T.3    Cavenee, W.K.4    Arden, K.C.5
  • 17
    • 0035918148 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase signaling inhibits DAF-16 DNA binding and function via 14-3-3-dependent and 14-3-3-independent pathways
    • Cahill C.M., Tzivion G., Nasrin N., Ogg S., Dore J., Ruvkun G., and Alexander-Bridges M. Phosphatidylinositol 3-kinase signaling inhibits DAF-16 DNA binding and function via 14-3-3-dependent and 14-3-3-independent pathways. J. Biol. Chem. 276 (2001) 13402-13410
    • (2001) J. Biol. Chem. , vol.276 , pp. 13402-13410
    • Cahill, C.M.1    Tzivion, G.2    Nasrin, N.3    Ogg, S.4    Dore, J.5    Ruvkun, G.6    Alexander-Bridges, M.7
  • 18
    • 0035034038 scopus 로고    scopus 로고
    • Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX
    • Brownawell A.M., Kops G.J., Macara I.G., and Burgering B.M. Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX. Mol. Cell Biol. 21 (2001) 3534-3546
    • (2001) Mol. Cell Biol. , vol.21 , pp. 3534-3546
    • Brownawell, A.M.1    Kops, G.J.2    Macara, I.G.3    Burgering, B.M.4
  • 19
    • 0035868368 scopus 로고    scopus 로고
    • Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation sites in regulating 14-3-3 binding, transactivation and nuclear targeting
    • Rena G., Prescott A.R., Guo S., Cohen P., and Unterman T.G. Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation sites in regulating 14-3-3 binding, transactivation and nuclear targeting. Biochem. J. 354 (2001) 605-612
    • (2001) Biochem. J. , vol.354 , pp. 605-612
    • Rena, G.1    Prescott, A.R.2    Guo, S.3    Cohen, P.4    Unterman, T.G.5
  • 21
    • 0034967720 scopus 로고    scopus 로고
    • Regulation of the Caenorhabditis elegans longevity protein DAF-16 by insulin/IGF-1 and germline signaling
    • Lin K., Hsin H., Libina N., and Kenyon C. Regulation of the Caenorhabditis elegans longevity protein DAF-16 by insulin/IGF-1 and germline signaling. Nat. Genet. 28 (2001) 139-145
    • (2001) Nat. Genet. , vol.28 , pp. 139-145
    • Lin, K.1    Hsin, H.2    Libina, N.3    Kenyon, C.4
  • 22
    • 1242276189 scopus 로고    scopus 로고
    • D4476, a cell-permeant inhibitor of CK1, suppresses the site-specific phosphorylation and nuclear exclusion of FOXO1a
    • Rena G., Bain J., Elliott M., and Cohen P. D4476, a cell-permeant inhibitor of CK1, suppresses the site-specific phosphorylation and nuclear exclusion of FOXO1a. EMBO Rep. 5 (2004) 60-65
    • (2004) EMBO Rep. , vol.5 , pp. 60-65
    • Rena, G.1    Bain, J.2    Elliott, M.3    Cohen, P.4
  • 23
    • 0035340356 scopus 로고    scopus 로고
    • The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site
    • Woods Y.L., Rena G., Morrice N., Barthel A., Becker W., Guo S., Unterman T.G., and Cohen P. The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site. Biochem. J. 355 (2001) 597-607
    • (2001) Biochem. J. , vol.355 , pp. 597-607
    • Woods, Y.L.1    Rena, G.2    Morrice, N.3    Barthel, A.4    Becker, W.5    Guo, S.6    Unterman, T.G.7    Cohen, P.8
  • 24
    • 15444371989 scopus 로고    scopus 로고
    • JNK regulates lifespan in Caenorhabditis elegans by modulating nuclear translocation of forkhead transcription factor/DAF-16
    • Oh S.W., Mukhopadhyay A., Svrzikapa N., Jiang F., Davis R.J., and Tissenbaum H.A. JNK regulates lifespan in Caenorhabditis elegans by modulating nuclear translocation of forkhead transcription factor/DAF-16. Proc. Natl. Acad. Sci. USA 102 (2005) 4494-4499
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4494-4499
    • Oh, S.W.1    Mukhopadhyay, A.2    Svrzikapa, N.3    Jiang, F.4    Davis, R.J.5    Tissenbaum, H.A.6
  • 25
    • 17044408768 scopus 로고    scopus 로고
    • JNK extends life span and limits growth by antagonizing cellular and organism-wide responses to insulin signaling
    • Wang M.C., Bohmann D., and Jasper H. JNK extends life span and limits growth by antagonizing cellular and organism-wide responses to insulin signaling. Cell 121 (2005) 115-125
    • (2005) Cell , vol.121 , pp. 115-125
    • Wang, M.C.1    Bohmann, D.2    Jasper, H.3
  • 27
    • 0031685774 scopus 로고    scopus 로고
    • The beta-catenin homolog BAR-1 and LET-60 Ras coordinately regulate the Hox gene lin-39 during Caenorhabditis elegans vulval development
    • Eisenmann D.M., Maloof J.N., Simske J.S., Kenyon C., and Kim S.K. The beta-catenin homolog BAR-1 and LET-60 Ras coordinately regulate the Hox gene lin-39 during Caenorhabditis elegans vulval development. Development 125 (1998) 3667-3680
    • (1998) Development , vol.125 , pp. 3667-3680
    • Eisenmann, D.M.1    Maloof, J.N.2    Simske, J.S.3    Kenyon, C.4    Kim, S.K.5
  • 28
    • 8444251784 scopus 로고    scopus 로고
    • The Wnt signaling pathway in development and disease
    • Logan C.Y., and Nusse R. The Wnt signaling pathway in development and disease. Annu. Rev. Cell Dev. Biol. 20 (2004) 781-810
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 781-810
    • Logan, C.Y.1    Nusse, R.2
  • 29
    • 17244376814 scopus 로고    scopus 로고
    • Wnt signalling in stem cells and cancer
    • Reya T., and Clevers H. Wnt signalling in stem cells and cancer. Nature 434 (2005) 843-850
    • (2005) Nature , vol.434 , pp. 843-850
    • Reya, T.1    Clevers, H.2
  • 34
    • 0037312020 scopus 로고    scopus 로고
    • How does calorie restriction work?
    • Koubova J., and Guarente L. How does calorie restriction work?. Genes Dev. 17 (2003) 313-321
    • (2003) Genes Dev. , vol.17 , pp. 313-321
    • Koubova, J.1    Guarente, L.2
  • 35
    • 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
  • 37
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum H.A., and Guarente L. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410 (2001) 227-230
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 41
    • 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
  • 42
    • 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
  • 43
    • 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., and Accili D. Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes. J. Biol. Chem. 280 (2005) 20589-20595
    • (2005) J. Biol. Chem. , vol.280 , pp. 20589-20595
    • Frescas, D.1    Valenti, L.2    Accili, D.3
  • 45
    • 2342445654 scopus 로고    scopus 로고
    • Negative regulation of forkhead transcription factor AFX (Foxo4) by CBP-induced acetylation
    • Fukuoka M., Daitoku H., Hatta M., Matsuzaki H., Umemura S., and Fukamizu A. Negative regulation of forkhead transcription factor AFX (Foxo4) by CBP-induced acetylation. Int. J. Mol. Med. 12 (2003) 503-508
    • (2003) Int. J. Mol. Med. , vol.12 , pp. 503-508
    • Fukuoka, M.1    Daitoku, H.2    Hatta, M.3    Matsuzaki, H.4    Umemura, S.5    Fukamizu, A.6
  • 51
    • 33748335578 scopus 로고    scopus 로고
    • The LXXLL motif of murine forkhead transcription factor FoxO1 mediates Sirt1-dependent transcriptional activity
    • Nakae J., Cao Y., Daitoku H., Fukamizu A., Ogawa W., Yano Y., and Hayashi Y. The LXXLL motif of murine forkhead transcription factor FoxO1 mediates Sirt1-dependent transcriptional activity. J. Clin. Invest. 116 (2006) 2473-2483
    • (2006) J. Clin. Invest. , vol.116 , pp. 2473-2483
    • Nakae, J.1    Cao, Y.2    Daitoku, H.3    Fukamizu, A.4    Ogawa, W.5    Yano, Y.6    Hayashi, Y.7
  • 52
    • 0141706357 scopus 로고    scopus 로고
    • Insulin-induced phosphorylation of FKHR (Foxo1) targets to proteasomal degradation
    • Matsuzaki H., Daitoku H., Hatta M., Tanaka K., and Fukamizu A. Insulin-induced phosphorylation of FKHR (Foxo1) targets to proteasomal degradation. Proc. Natl. Acad. Sci. USA 100 (2003) 11285-11290
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11285-11290
    • Matsuzaki, H.1    Daitoku, H.2    Hatta, M.3    Tanaka, K.4    Fukamizu, A.5
  • 53
    • 4544312844 scopus 로고    scopus 로고
    • Proteasomal degradation of the FoxO1 transcriptional regulator in cells transformed by the P3k and Akt oncoproteins
    • Aoki M., Jiang H., and Vogt P.K. Proteasomal degradation of the FoxO1 transcriptional regulator in cells transformed by the P3k and Akt oncoproteins. Proc. Natl. Acad. Sci. USA 101 (2004) 13613-13617
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13613-13617
    • Aoki, M.1    Jiang, H.2    Vogt, P.K.3
  • 54
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • Carrano A.C., Eytan E., Hershko A., and Pagano M. SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat. Cell Biol. 1 (1999) 193-199
    • (1999) Nat. Cell Biol. , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 55
    • 0037112174 scopus 로고    scopus 로고
    • The pRb-related protein p130 is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2)
    • Tedesco D., Lukas J., and Reed S.I. The pRb-related protein p130 is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2). Genes Dev. 16 (2002) 2946-2957
    • (2002) Genes Dev. , vol.16 , pp. 2946-2957
    • Tedesco, D.1    Lukas, J.2    Reed, S.I.3
  • 57
    • 0030602813 scopus 로고    scopus 로고
    • SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box
    • Bai C., Sen P., Hofmann K., Ma L., Goebl M., Harper J.W., and Elledge S.J. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86 (1996) 263-274
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1    Sen, P.2    Hofmann, K.3    Ma, L.4    Goebl, M.5    Harper, J.W.6    Elledge, S.J.7
  • 60
  • 62
    • 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., and DePinho R.A. Suppression of ovarian follicle activation in mice by the transcription factor Foxo3a. Science 301 (2003) 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
  • 65
    • 0029859045 scopus 로고    scopus 로고
    • Regulation of gene expression by insulin
    • O'Brien R.M., and Granner D.K. Regulation of gene expression by insulin. Physiol. Rev. 76 (1996) 1109-1161
    • (1996) Physiol. Rev. , vol.76 , pp. 1109-1161
    • O'Brien, R.M.1    Granner, D.K.2
  • 67
    • 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., Biggs W.H., Kitamura T., Cavenee W.K., Wright C.V., Arden K.C., and Accili D. Regulation of insulin action and pancreatic beta-cell function by mutated alleles of the gene encoding forkhead transcription factor Foxo1. Nat. Genet. 32 (2002) 245-253
    • (2002) Nat. Genet. , vol.32 , pp. 245-253
    • Nakae, J.1    Biggs, W.H.2    Kitamura, T.3    Cavenee, W.K.4    Wright, C.V.5    Arden, K.C.6    Accili, D.7
  • 68
    • 28444483953 scopus 로고    scopus 로고
    • Insulin regulation of PEPCK gene expression: a model for rapid and reversible modulation
    • Quinn P.G., and Yeagley D. Insulin regulation of PEPCK gene expression: a model for rapid and reversible modulation. Curr. Drug Targets Immune Endocr. Metabol. Disord. 5 (2005) 423-437
    • (2005) Curr. Drug Targets Immune Endocr. Metabol. Disord. , vol.5 , pp. 423-437
    • Quinn, P.G.1    Yeagley, D.2
  • 69
    • 0035185021 scopus 로고    scopus 로고
    • The forkhead transcription factor Foxo1 (Fkhr) confers insulin sensitivity onto glucose-6-phosphatase expression
    • Nakae J., Kitamura T., Silver D.L., and Accili D. The forkhead transcription factor Foxo1 (Fkhr) confers insulin sensitivity onto glucose-6-phosphatase expression. J. Clin. Invest. 108 (2001) 1359-1367
    • (2001) J. Clin. Invest. , vol.108 , pp. 1359-1367
    • Nakae, J.1    Kitamura, T.2    Silver, D.L.3    Accili, D.4
  • 72
    • 34548349302 scopus 로고    scopus 로고
    • Impaired regulation of hepatic glucose production in mice lacking the forkhead transcription factor foxo1 in liver
    • Matsumoto M., Pocai A., Rossetti L., Depinho R.A., and Accili D. Impaired regulation of hepatic glucose production in mice lacking the forkhead transcription factor foxo1 in liver. Cell Metab. 6 (2007) 208-216
    • (2007) Cell Metab. , vol.6 , pp. 208-216
    • Matsumoto, M.1    Pocai, A.2    Rossetti, L.3    Depinho, R.A.4    Accili, D.5
  • 78
    • 33748312093 scopus 로고    scopus 로고
    • Dual role of transcription factor FoxO1 in controlling hepatic insulin sensitivity and lipid metabolism
    • Matsumoto M., Han S., Kitamura T., and Accili D. Dual role of transcription factor FoxO1 in controlling hepatic insulin sensitivity and lipid metabolism. J. Clin. Invest. 116 (2006) 2464-2472
    • (2006) J. Clin. Invest. , vol.116 , pp. 2464-2472
    • Matsumoto, M.1    Han, S.2    Kitamura, T.3    Accili, D.4
  • 81
    • 0033524937 scopus 로고    scopus 로고
    • Tissue-specific knockout of the insulin receptor in pancreatic beta cells creates an insulin secretory defect similar to that in type 2 diabetes
    • Kulkarni R.N., Bruning J.C., Winnay J.N., Postic C., Magnuson M.A., and Kahn C.R. Tissue-specific knockout of the insulin receptor in pancreatic beta cells creates an insulin secretory defect similar to that in type 2 diabetes. Cell 96 (1999) 329-339
    • (1999) Cell , vol.96 , pp. 329-339
    • Kulkarni, R.N.1    Bruning, J.C.2    Winnay, J.N.3    Postic, C.4    Magnuson, M.A.5    Kahn, C.R.6
  • 82
    • 0036578921 scopus 로고    scopus 로고
    • Beta-cell-specific deletion of the Igf1 receptor leads to hyperinsulinemia and glucose intolerance but does not alter beta-cell mass
    • Kulkarni R.N., Holzenberger M., Shih D.Q., Ozcan U., Stoffel M., Magnuson M.A., and Kahn C.R. Beta-cell-specific deletion of the Igf1 receptor leads to hyperinsulinemia and glucose intolerance but does not alter beta-cell mass. Nat. Genet. 31 (2002) 111-115
    • (2002) Nat. Genet. , vol.31 , pp. 111-115
    • Kulkarni, R.N.1    Holzenberger, M.2    Shih, D.Q.3    Ozcan, U.4    Stoffel, M.5    Magnuson, M.A.6    Kahn, C.R.7
  • 85
    • 33644660954 scopus 로고    scopus 로고
    • Role of the forkhead protein FoxO1 in beta cell compensation to insulin resistance
    • Okamoto H., Hribal M.L., Lin H.V., Bennett W.R., Ward A., and Accili D. Role of the forkhead protein FoxO1 in beta cell compensation to insulin resistance. J. Clin. Invest. 116 (2006) 775-782
    • (2006) J. Clin. Invest. , vol.116 , pp. 775-782
    • Okamoto, H.1    Hribal, M.L.2    Lin, H.V.3    Bennett, W.R.4    Ward, A.5    Accili, D.6
  • 87
    • 0035936764 scopus 로고    scopus 로고
    • Obesity and the regulation of energy balance
    • Spiegelman B.M., and Flier J.S. Obesity and the regulation of energy balance. Cell 104 (2001) 531-543
    • (2001) Cell , vol.104 , pp. 531-543
    • Spiegelman, B.M.1    Flier, J.S.2
  • 88
    • 33845886915 scopus 로고    scopus 로고
    • Abdominal obesity and metabolic syndrome
    • Despres J.P., and Lemieux I. Abdominal obesity and metabolic syndrome. Nature 444 (2006) 881-887
    • (2006) Nature , vol.444 , pp. 881-887
    • Despres, J.P.1    Lemieux, I.2
  • 89
    • 0017713248 scopus 로고
    • Acquisition of increased hormone sensitivity during in vitro adipocyte development
    • Rubin C.S., Lai E., and Rosen O.M. Acquisition of increased hormone sensitivity during in vitro adipocyte development. J. Biol. Chem. 252 (1977) 3554-3557
    • (1977) J. Biol. Chem. , vol.252 , pp. 3554-3557
    • Rubin, C.S.1    Lai, E.2    Rosen, O.M.3
  • 90
    • 0025853329 scopus 로고
    • Targeted inactivation of the insulin receptor gene in mouse 3T3-L1 fibroblasts via homologous recombination
    • Accili D., and Taylor S.I. Targeted inactivation of the insulin receptor gene in mouse 3T3-L1 fibroblasts via homologous recombination. Proc. Natl. Acad. Sci. USA 88 (1991) 4708-4712
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4708-4712
    • Accili, D.1    Taylor, S.I.2
  • 91
    • 0031888649 scopus 로고    scopus 로고
    • Lack of insulin receptors affects the formation of white adipose tissue in mice. A morphometric and ultrastructural analysis
    • Cinti S., Eberbach S., Castellucci M., and Accili D. Lack of insulin receptors affects the formation of white adipose tissue in mice. A morphometric and ultrastructural analysis. Diabetologia 41 (1998) 171-177
    • (1998) Diabetologia , vol.41 , pp. 171-177
    • Cinti, S.1    Eberbach, S.2    Castellucci, M.3    Accili, D.4
  • 93
    • 0242580872 scopus 로고    scopus 로고
    • Convergence of peroxisome proliferator-activated receptor gamma and Foxo1 signaling pathways
    • Dowell P., Otto T.C., Adi S., and Lane M.D. Convergence of peroxisome proliferator-activated receptor gamma and Foxo1 signaling pathways. J. Biol. Chem. 278 (2003) 45485-45491
    • (2003) J. Biol. Chem. , vol.278 , pp. 45485-45491
    • Dowell, P.1    Otto, T.C.2    Adi, S.3    Lane, M.D.4
  • 94
    • 33746017379 scopus 로고    scopus 로고
    • FOXO1 represses peroxisome proliferator-activated receptor-gamma1 and -gamma2 gene promoters in primary adipocytes. A novel paradigm to increase insulin sensitivity
    • Armoni M., Harel C., Karni S., Chen H., Bar-Yoseph F., Ver M.R., Quon M.J., and Karnieli E. FOXO1 represses peroxisome proliferator-activated receptor-gamma1 and -gamma2 gene promoters in primary adipocytes. A novel paradigm to increase insulin sensitivity. J. Biol. Chem. 281 (2006) 19881-19891
    • (2006) J. Biol. Chem. , vol.281 , pp. 19881-19891
    • Armoni, M.1    Harel, C.2    Karni, S.3    Chen, H.4    Bar-Yoseph, F.5    Ver, M.R.6    Quon, M.J.7    Karnieli, E.8
  • 95
    • 0036068133 scopus 로고    scopus 로고
    • Adipose tissue selective insulin receptor knockout protects against obesity and obesity-related glucose intolerance
    • Bluher M., Michael M.D., Peroni O.D., Ueki K., Carter N., Kahn B.B., and Kahn C.R. Adipose tissue selective insulin receptor knockout protects against obesity and obesity-related glucose intolerance. Dev. Cell 3 (2002) 25-38
    • (2002) Dev. Cell , vol.3 , pp. 25-38
    • Bluher, M.1    Michael, M.D.2    Peroni, O.D.3    Ueki, K.4    Carter, N.5    Kahn, B.B.6    Kahn, C.R.7
  • 97
    • 0036267472 scopus 로고    scopus 로고
    • Decreasing hypothalamic insulin receptors causes hyperphagia and insulin resistance in rats
    • Obici S., Feng Z., Karkanias G., Baskin D.G., and Rossetti L. Decreasing hypothalamic insulin receptors causes hyperphagia and insulin resistance in rats. Nat. Neurosci. 5 (2002) 566-572
    • (2002) Nat. Neurosci. , vol.5 , pp. 566-572
    • Obici, S.1    Feng, Z.2    Karkanias, G.3    Baskin, D.G.4    Rossetti, L.5
  • 99
    • 18244384200 scopus 로고    scopus 로고
    • Restoration of liver insulin signaling in Insr knockout mice fails to normalize hepatic insulin action
    • Okamoto H., Obici S., Accili D., and Rossetti L. Restoration of liver insulin signaling in Insr knockout mice fails to normalize hepatic insulin action. J. Clin. Invest. 115 (2005) 1314-1322
    • (2005) J. Clin. Invest. , vol.115 , pp. 1314-1322
    • Okamoto, H.1    Obici, S.2    Accili, D.3    Rossetti, L.4
  • 102
    • 9644260563 scopus 로고    scopus 로고
    • Dysregulation of insulin receptor substrate 2 in beta cells and brain causes obesity and diabetes
    • Lin X., Taguchi A., Park S., Kushner J.A., Li F., Li Y., and White M.F. Dysregulation of insulin receptor substrate 2 in beta cells and brain causes obesity and diabetes. J. Clin. Invest. 114 (2004) 908-916
    • (2004) J. Clin. Invest. , vol.114 , pp. 908-916
    • Lin, X.1    Taguchi, A.2    Park, S.3    Kushner, J.A.4    Li, F.5    Li, Y.6    White, M.F.7
  • 108
    • 0142200472 scopus 로고    scopus 로고
    • Forkhead transcription factor FOXO1 (FKHR)-dependent induction of PDK4 gene expression in skeletal muscle during energy deprivation
    • Furuyama T., Kitayama K., Yamashita H., and Mori N. Forkhead transcription factor FOXO1 (FKHR)-dependent induction of PDK4 gene expression in skeletal muscle during energy deprivation. Biochem. J. 375 (2003) 365-371
    • (2003) Biochem. J. , vol.375 , pp. 365-371
    • Furuyama, T.1    Kitayama, K.2    Yamashita, H.3    Mori, N.4
  • 109
    • 0035914338 scopus 로고    scopus 로고
    • Insulin-like growth factor-mediated muscle differentiation: collaboration between phosphatidylinositol 3-kinase-Akt-signaling pathways and myogenin
    • Tureckova J., Wilson E.M., Cappalonga J.L., and Rotwein P. Insulin-like growth factor-mediated muscle differentiation: collaboration between phosphatidylinositol 3-kinase-Akt-signaling pathways and myogenin. J. Biol. Chem. 276 (2001) 39264-39270
    • (2001) J. Biol. Chem. , vol.276 , pp. 39264-39270
    • Tureckova, J.1    Wilson, E.M.2    Cappalonga, J.L.3    Rotwein, P.4
  • 110
    • 0027496895 scopus 로고
    • Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r)
    • Liu J.P., Baker J., Perkins A.S., Robertson E.J., and Efstratiadis A. Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r). Cell 75 (1993) 59-72
    • (1993) Cell , vol.75 , pp. 59-72
    • Liu, J.P.1    Baker, J.2    Perkins, A.S.3    Robertson, E.J.4    Efstratiadis, A.5
  • 111
    • 0029040848 scopus 로고
    • Myogenic vector expression of insulin-like growth factor I stimulates muscle cell differentiation and myofiber hypertrophy in transgenic mice
    • Coleman M.E., DeMayo F., Yin K.C., Lee H.M., Geske R., Montgomery C., and Schwartz R.J. Myogenic vector expression of insulin-like growth factor I stimulates muscle cell differentiation and myofiber hypertrophy in transgenic mice. J. Biol. Chem. 270 (1995) 12109-12116
    • (1995) J. Biol. Chem. , vol.270 , pp. 12109-12116
    • Coleman, M.E.1    DeMayo, F.2    Yin, K.C.3    Lee, H.M.4    Geske, R.5    Montgomery, C.6    Schwartz, R.J.7
  • 112
    • 0042477748 scopus 로고    scopus 로고
    • Regulation of insulin-like growth factor-dependent myoblast differentiation by Foxo forkhead transcription factors
    • Hribal M.L., Nakae J., Kitamura T., Shutter J.R., and Accili D. Regulation of insulin-like growth factor-dependent myoblast differentiation by Foxo forkhead transcription factors. J. Cell Biol. 162 (2003) 535-541
    • (2003) J. Cell Biol. , vol.162 , pp. 535-541
    • Hribal, M.L.1    Nakae, J.2    Kitamura, T.3    Shutter, J.R.4    Accili, D.5
  • 113
    • 0037318822 scopus 로고    scopus 로고
    • Signalling pathways that mediate skeletal muscle hypertrophy and atrophy
    • Glass D.J. Signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Nat. Cell Biol. 5 (2003) 87-90
    • (2003) Nat. Cell Biol. , vol.5 , pp. 87-90
    • Glass, D.J.1
  • 117
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors
    • Stitt T.N., Drujan D., Clarke B.A., Panaro F., Timofeyva Y., Kline W.O., Gonzalez M., Yancopoulos G.D., and Glass D.J. The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol. Cell 14 (2004) 395-403
    • (2004) Mol. Cell , vol.14 , pp. 395-403
    • Stitt, T.N.1    Drujan, D.2    Clarke, B.A.3    Panaro, F.4    Timofeyva, Y.5    Kline, W.O.6    Gonzalez, M.7    Yancopoulos, G.D.8    Glass, D.J.9
  • 118
    • 4544358547 scopus 로고    scopus 로고
    • Skeletal muscle FOXO1 (FKHR) transgenic mice have less skeletal muscle mass, down-regulated Type I (slow twitch/red muscle) fiber genes, and impaired glycemic control
    • Kamei Y., Miura S., Suzuki M., Kai Y., Mizukami J., Taniguchi T., Mochida K., Hata T., Matsuda J., Aburatani H., Nishino I., and Ezaki O. Skeletal muscle FOXO1 (FKHR) transgenic mice have less skeletal muscle mass, down-regulated Type I (slow twitch/red muscle) fiber genes, and impaired glycemic control. J. Biol. Chem. 279 (2004) 41114-41123
    • (2004) J. Biol. Chem. , vol.279 , pp. 41114-41123
    • Kamei, Y.1    Miura, S.2    Suzuki, M.3    Kai, Y.4    Mizukami, J.5    Taniguchi, T.6    Mochida, K.7    Hata, T.8    Matsuda, J.9    Aburatani, H.10    Nishino, I.11    Ezaki, O.12
  • 119
    • 0021814480 scopus 로고
    • Characterization of the receptors for insulin and the insulin-like growth factors on micro- and macrovascular tissues
    • Jialal I., Crettaz M., Hachiya H.L., Kahn C.R., Moses A.C., Buzney S.M., and King G.L. Characterization of the receptors for insulin and the insulin-like growth factors on micro- and macrovascular tissues. Endocrinology 117 (1985) 1222-1229
    • (1985) Endocrinology , vol.117 , pp. 1222-1229
    • Jialal, I.1    Crettaz, M.2    Hachiya, H.L.3    Kahn, C.R.4    Moses, A.C.5    Buzney, S.M.6    King, G.L.7
  • 122
    • 0027241856 scopus 로고
    • The pathogenesis of atherosclerosis: a perspective for the 1990s
    • Ross R. The pathogenesis of atherosclerosis: a perspective for the 1990s. Nature 362 (1993) 801-809
    • (1993) Nature , vol.362 , pp. 801-809
    • Ross, R.1
  • 123
    • 3042588831 scopus 로고    scopus 로고
    • Molecular regulation of vascular smooth muscle cell differentiation in development and disease
    • Owens G.K., Kumar M.S., and Wamhoff B.R. Molecular regulation of vascular smooth muscle cell differentiation in development and disease. Physiol. Rev. 84 (2004) 767-801
    • (2004) Physiol. Rev. , vol.84 , pp. 767-801
    • Owens, G.K.1    Kumar, M.S.2    Wamhoff, B.R.3
  • 124
    • 0037870478 scopus 로고    scopus 로고
    • Serum response factor: toggling between disparate programs of gene expression
    • Miano J.M. Serum response factor: toggling between disparate programs of gene expression. J. Mol. Cell Cardiol. 35 (2003) 577-593
    • (2003) J. Mol. Cell Cardiol. , vol.35 , pp. 577-593
    • Miano, J.M.1
  • 125
    • 5444235587 scopus 로고    scopus 로고
    • Control of smooth muscle development by the myocardin family of transcriptional coactivators
    • Wang D.Z., and Olson E.N. Control of smooth muscle development by the myocardin family of transcriptional coactivators. Curr. Opin. Genet. Dev. 14 (2004) 558-566
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 558-566
    • Wang, D.Z.1    Olson, E.N.2
  • 126
    • 22944451474 scopus 로고    scopus 로고
    • Phenotypic modulation of smooth muscle cells through interaction of Foxo4 and myocardin
    • Liu Z.P., Wang Z., Yanagisawa H., and Olson E.N. Phenotypic modulation of smooth muscle cells through interaction of Foxo4 and myocardin. Dev. Cell 9 (2005) 261-270
    • (2005) Dev. Cell , vol.9 , pp. 261-270
    • Liu, Z.P.1    Wang, Z.2    Yanagisawa, H.3    Olson, E.N.4
  • 127
    • 33751534932 scopus 로고    scopus 로고
    • Myocardin is a direct transcriptional target of Mef2, Tead and Foxo proteins during cardiovascular development
    • Creemers E.E., Sutherland L.B., McAnally J., Richardson J.A., and Olson E.N. Myocardin is a direct transcriptional target of Mef2, Tead and Foxo proteins during cardiovascular development. Development 133 (2006) 4245-4256
    • (2006) Development , vol.133 , pp. 4245-4256
    • Creemers, E.E.1    Sutherland, L.B.2    McAnally, J.3    Richardson, J.A.4    Olson, E.N.5
  • 128
    • 0042161896 scopus 로고    scopus 로고
    • Control of cell number by Drosophila FOXO: downstream and feedback regulation of the insulin receptor pathway
    • Puig O., Marr M.T., Ruhf M.L., and Tjian R. Control of cell number by Drosophila FOXO: downstream and feedback regulation of the insulin receptor pathway. Genes Dev. 17 (2003) 2006-2020
    • (2003) Genes Dev. , vol.17 , pp. 2006-2020
    • Puig, O.1    Marr, M.T.2    Ruhf, M.L.3    Tjian, R.4
  • 132
    • 22944488274 scopus 로고    scopus 로고
    • Drosophila melted modulates FOXO and TOR activity
    • Teleman A.A., Chen Y.W., and Cohen S.M. Drosophila melted modulates FOXO and TOR activity. Dev. Cell 9 (2005) 271-281
    • (2005) Dev. Cell , vol.9 , pp. 271-281
    • Teleman, A.A.1    Chen, Y.W.2    Cohen, S.M.3
  • 133
    • 33846015072 scopus 로고    scopus 로고
    • Interaction of FoxO1 and TSC2 induces insulin resistance through activation of the mammalian target of rapamycin/p70 S6K pathway
    • Cao Y., Kamioka Y., Yokoi N., Kobayashi T., Hino O., Onodera M., Mochizuki N., and Nakae J. Interaction of FoxO1 and TSC2 induces insulin resistance through activation of the mammalian target of rapamycin/p70 S6K pathway. J. Biol. Chem. 281 (2006) 40242-40251
    • (2006) J. Biol. Chem. , vol.281 , pp. 40242-40251
    • Cao, Y.1    Kamioka, Y.2    Yokoi, N.3    Kobayashi, T.4    Hino, O.5    Onodera, M.6    Mochizuki, N.7    Nakae, J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.