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Volumn 30, Issue 2, 2010, Pages 470-480

Regulation of the intracellular localization of Foxo3a by stress-activated protein kinase signaling pathways in skeletal muscle cells

Author keywords

[No Author keywords available]

Indexed keywords

ATROGIN 1; EXPORTIN 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE 4; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEASOME; PROTEIN KINASE B; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR FKHRL1;

EID: 73549122141     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00666-09     Document Type: Article
Times cited : (88)

References (51)
  • 1
    • 41849087003 scopus 로고    scopus 로고
    • FOXO animal models reveal a variety of diverse roles for FOXO transcription factors
    • Arden, K. C. 2008. FOXO animal models reveal a variety of diverse roles for FOXO transcription factors. Oncogene 27:2345-2350.
    • (2008) Oncogene , vol.27 , pp. 2345-2350
    • Arden, K.C.1
  • 6
    • 0035135841 scopus 로고    scopus 로고
    • Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)
    • Brunet, A., J. Park, H. Tran, L. S. Hu, B. A. Hemmings, and M. E. Greenberg. 2001. Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a). Mol. Cell. Biol. 21:952-965.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 952-965
    • Brunet, A.1    Park, J.2    Tran, H.3    Hu, L.S.4    Hemmings, B.A.5    Greenberg, M.E.6
  • 8
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering, B. M., and P. J. Coffer. 1995. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376:599-602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.1    Coffer, P.J.2
  • 9
    • 4644310423 scopus 로고    scopus 로고
    • The p38 pathway regulates Akt both at the protein and transcriptional activation levels during myogenesis
    • Cabane, C., A. S. Coldefy, K. Yeow, and B. Derijard. 2004. The p38 pathway regulates Akt both at the protein and transcriptional activation levels during myogenesis. Cell. Signal. 16:1405-1415.
    • (2004) Cell. Signal , vol.16 , pp. 1405-1415
    • Cabane, C.1    Coldefy, A.S.2    Yeow, K.3    Derijard, B.4
  • 12
    • 41849128523 scopus 로고    scopus 로고
    • The FoxO code
    • Calnan, D. R., and A. Brunet. 2008. The FoxO code. Oncogene 27:2276-2288.
    • (2008) Oncogene , vol.27 , pp. 2276-2288
    • Calnan, D.R.1    Brunet, A.2
  • 13
  • 14
    • 0043170836 scopus 로고    scopus 로고
    • Proteolytic regulation of Forkhead transcription factor FOXO3a by caspase-3-like proteases
    • Charvet, C., I. Alberti, F. Luciano, A. Jacquel, A. Bernard, P. Auberger, and M. Deckert. 2003. Proteolytic regulation of Forkhead transcription factor FOXO3a by caspase-3-like proteases. Oncogene 22:4557-4568.
    • (2003) Oncogene , vol.22 , pp. 4557-4568
    • Charvet, C.1    Alberti, I.2    Luciano, F.3    Jacquel, A.4    Bernard, A.5    Auberger, P.6    Deckert, M.7
  • 16
    • 33748526240 scopus 로고    scopus 로고
    • Atrophy-related ubiquitin ligases, atrogin-1 and MuRF1 are up-regulated in aged rat tibialis anterior muscle
    • Clavel, S., A. S. Coldefy, E. Kurkdjian, J. Salles, I. Margaritis, and B. Derijard. 2006. Atrophy-related ubiquitin ligases, atrogin-1 and MuRF1 are up-regulated in aged rat tibialis anterior muscle. Mech. Ageing Dev. 127:794-801.
    • (2006) Mech. Ageing Dev , vol.127 , pp. 794-801
    • Clavel, S.1    Coldefy, A.S.2    Kurkdjian, E.3    Salles, J.4    Margaritis, I.5    Derijard, B.6
  • 17
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., H. Reddy, M. Caivano, and P. Cohen. 2000. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351:95-105.
    • (2000) Biochem. J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 18
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • Dérijard, B., M. Hibi, I. H. Wu, T. Barrett, B. Su, T. Deng, M. Karin, and R. J. Davis. 1994. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76:1025-1037.
    • (1994) Cell , vol.76 , pp. 1025-1037
    • Dérijard, B.1    Hibi, M.2    Wu, I.H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 19
    • 0028935974 scopus 로고
    • Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms
    • Dérijard, B., J. Raingeaud, T. Barrett, I. H. Wu, J. Han, R. J. Ulevitch, and R. J. Davis. 1995. Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms. Science 267:682-685.
    • (1995) Science , vol.267 , pp. 682-685
    • Dérijard, B.1    Raingeaud, J.2    Barrett, T.3    Wu, I.H.4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 21
    • 34848861463 scopus 로고    scopus 로고
    • The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor
    • Greer, E. L., P. R. Oskoui, M. R. Banko, J. M. Maniar, M. P. Gygi, S. P. Gygi, and A. Brunet. 2007. The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor. J. Biol. Chem. 282:30107-30119.
    • (2007) J. Biol. Chem , vol.282 , pp. 30107-30119
    • Greer, E.L.1    Oskoui, P.R.2    Banko, M.R.3    Maniar, J.M.4    Gygi, M.P.5    Gygi, S.P.6    Brunet, A.7
  • 22
    • 41849093037 scopus 로고    scopus 로고
    • The role of FoxO in the regulation of metabolism
    • Gross, D. N., A. P. van den Heuvel, and M. J. Birnbaum. 2008. The role of FoxO in the regulation of metabolism. Oncogene 27:2320-2336.
    • (2008) Oncogene , vol.27 , pp. 2320-2336
    • Gross, D.N.1    van den Heuvel, A.P.2    Birnbaum, M.J.3
  • 23
    • 63649159307 scopus 로고    scopus 로고
    • p66Shc links alpha1-adrenergic receptors to a reactive oxygen species-dependent AKT-FOXO3A phosphorylation pathway in cardiomyocytes
    • Guo, J., Z. Gertsberg, N. Ozgen, and S. F. Steinberg. 2009. p66Shc links alpha1-adrenergic receptors to a reactive oxygen species-dependent AKT-FOXO3A phosphorylation pathway in cardiomyocytes. Circ. Res. 104:660-669.
    • (2009) Circ. Res , vol.104 , pp. 660-669
    • Guo, J.1    Gertsberg, Z.2    Ozgen, N.3    Steinberg, S.F.4
  • 24
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han, J., J. D. Lee, L. Bibbs, and R. J. Ulevitch. 1994. A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265:808-811.
    • (1994) Science , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 25
    • 0031896910 scopus 로고    scopus 로고
    • Anisomycin selectively desensitizes signalling components involved in stress kinase activation and fos and jun induction
    • Hazzalin, C. A., R. Le Panse, E. Cano, and L. C. Mahadevan. 1998. Anisomycin selectively desensitizes signalling components involved in stress kinase activation and fos and jun induction. Mol. Cell. Biol. 18:1844-1854.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 1844-1854
    • Hazzalin, C.A.1    Le Panse, R.2    Cano, E.3    Mahadevan, L.C.4
  • 27
    • 0035350530 scopus 로고    scopus 로고
    • What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
    • Jagoe, R. T., and A. L. Goldberg. 2001. What do we really know about the ubiquitin-proteasome pathway in muscle atrophy? Curr. Opin. Clin. Nutr. Metab. Care 4:183-190.
    • (2001) Curr. Opin. Clin. Nutr. Metab. Care , vol.4 , pp. 183-190
    • Jagoe, R.T.1    Goldberg, A.L.2
  • 28
    • 33745183356 scopus 로고    scopus 로고
    • The p38 MAPK signaling pathway: A major regulator of skeletal muscle development
    • Keren, A., Y. Tamir, and E. Bengal. 2006. The p38 MAPK signaling pathway: a major regulator of skeletal muscle development. Mol. Cell. Endocrinol. 252:224-230.
    • (2006) Mol. Cell. Endocrinol , vol.252 , pp. 224-230
    • Keren, A.1    Tamir, Y.2    Bengal, E.3
  • 31
    • 0037458622 scopus 로고    scopus 로고
    • Expression of the serum- and glucocorticoid-inducible protein kinase, Sgk, is a cell survival response to multiple types of environmental stress stimuli in mammary epithelial cells
    • Leong, M. L., A. C. Maiyar, B. Kim, B. A. O'Keeffe, and G. L. Firestone. 2003. Expression of the serum- and glucocorticoid-inducible protein kinase, Sgk, is a cell survival response to multiple types of environmental stress stimuli in mammary epithelial cells. J. Biol. Chem. 278:5871-5882.
    • (2003) J. Biol. Chem , vol.278 , pp. 5871-5882
    • Leong, M.L.1    Maiyar, A.C.2    Kim, B.3    O'Keeffe, B.A.4    Firestone, G.L.5
  • 32
    • 14644400387 scopus 로고    scopus 로고
    • TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle
    • Li, Y. P., Y. Chen, J. John, J. Moylan, B. Jin, D. L. Mann, and M. B. Reid. 2005. TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle. FASEB J. 19:362-370.
    • (2005) FASEB J , vol.19 , pp. 362-370
    • Li, Y.P.1    Chen, Y.2    John, J.3    Moylan, J.4    Jin, B.5    Mann, D.L.6    Reid, M.B.7
  • 34
    • 43949109275 scopus 로고    scopus 로고
    • Downstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle
    • Mammucari, C., S. Schiaffino, and M. Sandri. 2008. Downstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle. Autophagy 4:524-526.
    • (2008) Autophagy , vol.4 , pp. 524-526
    • Mammucari, C.1    Schiaffino, S.2    Sandri, M.3
  • 35
    • 33144454419 scopus 로고    scopus 로고
    • Development of a new bicistronic retroviral vector with strong IRES activity
    • Martin, P., O. Albagli, M. C. Poggi, K. E. Boulukos, and P. Pognonec. 2006. Development of a new bicistronic retroviral vector with strong IRES activity. BMC Biotechnol. 6:4.
    • (2006) BMC Biotechnol , vol.6 , pp. 4
    • Martin, P.1    Albagli, O.2    Poggi, M.C.3    Boulukos, K.E.4    Pognonec, P.5
  • 37
    • 0035977073 scopus 로고    scopus 로고
    • Glial cell line-derived neurotrophic factor-stimulated phosphatidylinositol 3-kinase and Akt activities exert opposing effects on the ERK pathway: Importance for the rescue of neuroectodermic cells
    • Mograbi, B., R. Bocciardi, I. Bourget, R. Busca, N. Rochet, D. Farahi-Far, T. Juhel, and B. Rossi. 2001. Glial cell line-derived neurotrophic factor-stimulated phosphatidylinositol 3-kinase and Akt activities exert opposing effects on the ERK pathway: importance for the rescue of neuroectodermic cells. J. Biol. Chem. 276:45307-45319.
    • (2001) J. Biol. Chem , vol.276 , pp. 45307-45319
    • Mograbi, B.1    Bocciardi, R.2    Bourget, I.3    Busca, R.4    Rochet, N.5    Farahi-Far, D.6    Juhel, T.7    Rossi, B.8
  • 38
    • 34047213532 scopus 로고    scopus 로고
    • Oxidative stress, chronic disease, and muscle wasting
    • Moylan, J. S., and M. B. Reid. 2007. Oxidative stress, chronic disease, and muscle wasting. Muscle Nerve 35:411-429.
    • (2007) Muscle Nerve , vol.35 , pp. 411-429
    • Moylan, J.S.1    Reid, M.B.2
  • 39
    • 0037192473 scopus 로고    scopus 로고
    • Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway
    • Nemoto, S., and T. Finkel. 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
  • 40
    • 38449101649 scopus 로고    scopus 로고
    • Roles and potential therapeutic targets of the ubiquitin proteasome system in muscle wasting
    • Nury, D., C. Doucet, and O. Coux. 2007. Roles and potential therapeutic targets of the ubiquitin proteasome system in muscle wasting. BMC Biochem. 8(Suppl. 1):S7.
    • (2007) BMC Biochem , vol.8 , Issue.SUPPL. 1
    • Nury, D.1    Doucet, C.2    Coux, O.3
  • 41
    • 15444371989 scopus 로고    scopus 로고
    • JNK regulates lifespan in Caenorhabditis elegans by modulating nuclear translocation of forkhead transcription factor/DAF-16
    • Oh, S. W., A. Mukhopadhyay, N. Svrzikapa, F. Jiang, R. J. Davis, and H. A. Tissenbaum. 2005. JNK regulates lifespan in Caenorhabditis elegans by modulating nuclear translocation of forkhead transcription factor/DAF-16. Proc. Natl. Acad. Sci. U. S. A. 102:4494-4499.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , 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
  • 42
    • 34248597065 scopus 로고    scopus 로고
    • Differential regulation and properties of MAPKs
    • Raman, M., W. Chen, and M. H. Cobb. 2007. Differential regulation and properties of MAPKs. Oncogene 26:3100-3112.
    • (2007) Oncogene , vol.26 , pp. 3100-3112
    • Raman, M.1    Chen, W.2    Cobb, M.H.3
  • 43
    • 41549135942 scopus 로고    scopus 로고
    • FoxO transcription factors in the maintenance of cellular homeostasis during aging
    • Salih, D. A., and A. Brunet. 2008. FoxO transcription factors in the maintenance of cellular homeostasis during aging. Curr. Opin. Cell Biol. 20:126-136.
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 126-136
    • Salih, D.A.1    Brunet, A.2
  • 45
    • 0029670584 scopus 로고    scopus 로고
    • Efficient control of gene expression by single step integration of the tetracycline system in transgenic mice
    • Schultze, N., Y. Burki, Y. Lang, U. Certa, and H. Bluethmann. 1996. Efficient control of gene expression by single step integration of the tetracycline system in transgenic mice. Nat. Biotechnol. 14:499-503.
    • (1996) Nat. Biotechnol , vol.14 , pp. 499-503
    • Schultze, N.1    Burki, Y.2    Lang, Y.3    Certa, U.4    Bluethmann, H.5
  • 46
    • 0028061674 scopus 로고
    • Signal transduction by tumor necrosis factor mediated by JNK protein kinases
    • Sluss, H. K., T. Barrett, B. Derijard, and R. J. Davis. 1994. Signal transduction by tumor necrosis factor mediated by JNK protein kinases. Mol. Cell. Biol. 14:8376-8384.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 8376-8384
    • Sluss, H.K.1    Barrett, T.2    Derijard, B.3    Davis, R.J.4
  • 47
    • 22944479314 scopus 로고    scopus 로고
    • JNK antagonizes Akt-mediated survival signals by phosphorylating 14-3-3
    • Sunayama, J., F. Tsuruta, N. Masuyama, and Y. Gotoh. 2005. JNK antagonizes Akt-mediated survival signals by phosphorylating 14-3-3. J. Cell Biol. 170:295-304.
    • (2005) J. Cell Biol , vol.170 , pp. 295-304
    • Sunayama, J.1    Tsuruta, F.2    Masuyama, N.3    Gotoh, Y.4
  • 48
    • 34249281690 scopus 로고    scopus 로고
    • Stressing the role of FoxO proteins in lifespan and disease
    • van der Horst, A., and B. M. Burgering. 2007. Stressing the role of FoxO proteins in lifespan and disease. Nat. Rev. Mol. Cell Biol. 8:440-450.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 440-450
    • van der Horst, A.1    Burgering, B.M.2
  • 49
    • 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., D. Bohmann, and H. Jasper. 2005. JNK extends life span and limits growth by antagonizing cellular and organism-wide responses to insulin signaling. Cell 121:115-125.
    • (2005) Cell , vol.121 , pp. 115-125
    • Wang, M.C.1    Bohmann, D.2    Jasper, H.3
  • 50
    • 0242362732 scopus 로고    scopus 로고
    • JNK signaling confers tolerance to oxidative stress and extends lifespan in Drosophila
    • Wang, M. C., D. Bohmann, and H. Jasper. 2003. JNK signaling confers tolerance to oxidative stress and extends lifespan in Drosophila. Dev. Cell 5:811-816.
    • (2003) Dev. Cell , vol.5 , pp. 811-816
    • Wang, M.C.1    Bohmann, D.2    Jasper, H.3
  • 51
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • Zhao, J., J. J. Brault, A. Schild, P. Cao, M. Sandri, S. Schiaffino, S. H. Lecker, and A. L. Goldberg. 2007. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab. 6:472-483.
    • (2007) Cell Metab , vol.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3    Cao, P.4    Sandri, M.5    Schiaffino, S.6    Lecker, S.H.7    Goldberg, A.L.8


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