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Volumn 7, Issue 314, 2014, Pages

MTORC1 promotes denervation-induced muscle atrophy through a mechanism involving the activation of FoxO and E3 ubiquitin ligases

Author keywords

[No Author keywords available]

Indexed keywords

ATROGIN 1; ISOPROTEIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MUSCLE RING FINGER 1 PROTEIN; PHOSPHATIDIC ACID; PHOSPHOLIPASE D; PROTEIN; PROTEIN KINASE B; RAPAMYCIN; TRANSCRIPTION FACTOR FKHR; TRANSCRIPTION FACTOR FOXO; TUBEROUS SCLEROSIS COMPLEX 1; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84895473275     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2004809     Document Type: Article
Times cited : (102)

References (64)
  • 1
    • 77949351725 scopus 로고    scopus 로고
    • Motor neuron disease: Systematic reviews of treatment for ALS and SMA
    • R. W. Orrell, Motor neuron disease: Systematic reviews of treatment for ALS and SMA. Br. Med. Bull. 93, 145-159 (2010).
    • (2010) Br. Med. Bull. , vol.93 , pp. 145-159
    • Orrell, R.W.1
  • 3
    • 84872094183 scopus 로고    scopus 로고
    • Cellular and molecularmechanisms ofmuscle atrophy
    • P. Bonaldo, M. Sandri, Cellular and molecularmechanisms ofmuscle atrophy. Dis. Model. Mech. 6, 25-39 (2013).
    • (2013) Dis. Model. Mech. , vol.6 , pp. 25-39
    • Bonaldo, P.1    Sandri, M.2
  • 4
    • 79952111161 scopus 로고    scopus 로고
    • PI3 kinase regulation of skeletal muscle hypertrophy and atrophy
    • D. J. Glass, PI3 kinase regulation of skeletal muscle hypertrophy and atrophy. Curr. Top. Microbiol. Immunol. 346, 267-278 (2010).
    • (2010) Curr. Top. Microbiol. Immunol. , vol.346 , pp. 267-278
    • Glass, D.J.1
  • 5
    • 80053272231 scopus 로고    scopus 로고
    • Recent progress toward understanding the molecular mechanisms that regulate skeletal muscle mass
    • C. A. Goodman, D. L. Mayhew, T. A. Hornberger, Recent progress toward understanding the molecular mechanisms that regulate skeletal muscle mass. Cell. Signal. 23, 1896-1906 (2011).
    • (2011) Cell. Signal. , vol.23 , pp. 1896-1906
    • Goodman, C.A.1    Mayhew, D.L.2    Hornberger, T.A.3
  • 7
    • 0030593939 scopus 로고    scopus 로고
    • Mechanisms of disease: Mechanisms of muscle wasting: The role of the ubiquitin-proteasome pathway
    • DOI 10.1056/NEJM199612193352507
    • W. E. Mitch, A. L. Goldberg, Mechanisms of muscle wasting-The role of the ubiquitin-proteasome pathway. N. Engl. J. Med. 335, 1897-1905 (1996). (Pubitemid 26419198)
    • (1996) New England Journal of Medicine , vol.335 , Issue.25 , pp. 1897-1905
    • Mitch, W.E.1    Goldberg, A.L.2
  • 12
    • 33644687189 scopus 로고    scopus 로고
    • Reduction of skeletal muscle atrophy by a proteasome inhibitor in a rat model of denervation
    • B. C. Beehler, P. G. Sleph, L. Benmassaoud, G. J. Grover, Reduction of skeletal muscle atrophy by a proteasome inhibitor in a rat model of denervation. Exp. Biol. Med. 231, 335-341 (2006). (Pubitemid 43334321)
    • (2006) Experimental Biology and Medicine , vol.231 , Issue.3 , pp. 335-341
    • Beehler, B.C.1    Sleph, P.G.2    Benmassaoud, L.3    Grover, G.J.4
  • 14
    • 33750947156 scopus 로고    scopus 로고
    • Activity-dependent gene regulation in skeletal muscle is mediated by a histone deacetylase (HDAC)-Dach2-myogenin signal transduction cascade
    • DOI 10.1073/pnas.0601565103
    • H. Tang, D. Goldman, Activity-dependent gene regulation in skeletal muscle is mediated by a histone deacetylase (HDAC)-Dach2-myogenin signal transduction cascade. Proc. Natl. Acad. Sci. U.S.A. 103, 16977-16982 (2006). (Pubitemid 44737363)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.45 , pp. 16977-16982
    • Tang, H.1    Goldman, D.2
  • 15
    • 64149118078 scopus 로고    scopus 로고
    • A histone deacetylase 4/myogenin positive feedback loop coordinates denervationdependent gene induction and suppression
    • H. Tang, P. Macpherson, M. Marvin, E. Meadows, W. H. Klein, X. J. Yang, D. Goldman, A histone deacetylase 4/myogenin positive feedback loop coordinates denervationdependent gene induction and suppression. Mol. Biol. Cell 20, 1120-1131 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1120-1131
    • Tang, H.1    Macpherson, P.2    Marvin, M.3    Meadows, E.4    Klein, W.H.5    Yang, X.J.6    Goldman, D.7
  • 17
    • 79957483811 scopus 로고    scopus 로고
    • Myogenin regulates denervation-dependent muscle atrophy in mouse soleus muscle
    • P. C. Macpherson, X. Wang, D. Goldman, Myogenin regulates denervation-dependent muscle atrophy in mouse soleus muscle. J. Cell. Biochem. 112, 2149-2159 (2011).
    • (2011) J. Cell. Biochem. , vol.112 , pp. 2149-2159
    • Macpherson, P.C.1    Wang, X.2    Goldman, D.3
  • 18
    • 11144356337 scopus 로고    scopus 로고
    • Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy
    • DOI 10.1016/S0092-8674(04)00400-3, PII S0092867404004003
    • M. Sandri, C. Sandri, A. Gilbert, C. Skurk, E. Calabria, A. Picard, K. Walsh, S. Schiaffino, S. H. Lecker, A. L. Goldberg, Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell 117, 399-412 (2004). (Pubitemid 38534545)
    • (2004) Cell , vol.117 , Issue.3 , pp. 399-412
    • Sandri, M.1    Sandri, C.2    Gilbert, A.3    Skurk, C.4    Calabria, E.5    Picard, A.6    Walsh, K.7    Schiaffino, S.8    Lecker, S.H.9    Goldberg, A.L.10
  • 19
    • 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
    • DOI 10.1074/jbc.M400674200
    • Y. Kamei, S. Miura, M. Suzuki, Y. Kai, J. Mizukami, T. Taniguchi, K. Mochida, T. Hata, J. Matsuda, H. Aburatani, I. Nishino, O. Ezaki, 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, 41114-41123 (2004). (Pubitemid 39287713)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , 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
  • 20
    • 73549116708 scopus 로고    scopus 로고
    • FOXO signaling is required for disuse muscle atrophy and is directly regulated by Hsp70
    • S. M. Senf, S. L. Dodd, A. R. Judge, FOXO signaling is required for disuse muscle atrophy and is directly regulated by Hsp70. Am. J. Physiol. Cell Physiol. 298, C38-C45 (2010).
    • (2010) Am. J. Physiol. Cell Physiol. , vol.298
    • Senf, S.M.1    Dodd, S.L.2    Judge, A.R.3
  • 21
    • 84857695549 scopus 로고    scopus 로고
    • Inhibition of FoxO transcriptional activity prevents muscle fiber atrophy during cachexia and induces hypertrophy
    • S. A. Reed, P. B. Sandesara, S. M. Senf, A. R. Judge, Inhibition of FoxO transcriptional activity prevents muscle fiber atrophy during cachexia and induces hypertrophy. FASEB J. 26, 987-1000 (2012).
    • (2012) FASEB J. , vol.26 , pp. 987-1000
    • Reed, S.A.1    Sandesara, P.B.2    Senf, S.M.3    Judge, A.R.4
  • 23
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • M. Laplante, D. M. Sabatini, mTOR signaling in growth control and disease. Cell 149, 274-293 (2012).
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 25
    • 34347220473 scopus 로고    scopus 로고
    • Defining the Role of mTOR in Cancer
    • DOI 10.1016/j.ccr.2007.05.008, PII S1535610807001511
    • D. A. Guertin, D. M. Sabatini, Defining the role of mTOR in cancer. Cancer Cell 12, 9-22 (2007). (Pubitemid 47001784)
    • (2007) Cancer Cell , vol.12 , Issue.1 , pp. 9-22
    • Guertin, D.A.1    Sabatini, D.M.2
  • 31
    • 33749366334 scopus 로고    scopus 로고
    • Muscle atrophy in transgenic mice expressing a human TSC1 transgene
    • DOI 10.1016/j.febslet.2006.09.008, PII S0014579306010866
    • M. Wan, X. Wu, K. L. Guan, M. Han, Y. Zhuang, T. Xu, Muscle atrophy in transgenic mice expressing a human TSC1 transgene. FEBS Lett. 580, 5621-5627 (2006). (Pubitemid 44498663)
    • (2006) FEBS Letters , vol.580 , Issue.24 , pp. 5621-5627
    • Wan, M.1    Wu, X.2    Guan, K.-L.3    Han, M.4    Zhuang, Y.5    Xu, T.6
  • 35
    • 79251576152 scopus 로고    scopus 로고
    • Intracellular signaling pathways regulating net protein balance following diaphragm muscle denervation
    • H. M. Argadine, C. B. Mantilla, W. Z. Zhan, G. C. Sieck, Intracellular signaling pathways regulating net protein balance following diaphragm muscle denervation. Am. J. Physiol. Cell Physiol. 300, C318-C327 (2011).
    • (2011) Am. J. Physiol. Cell Physiol. , vol.300
    • Argadine, H.M.1    Mantilla, C.B.2    Zhan, W.Z.3    Sieck, G.C.4
  • 36
    • 33747819801 scopus 로고    scopus 로고
    • MTOR and cancer: Insights into a complex relationship
    • DOI 10.1038/nrc1974, PII NRC1974
    • D. M. Sabatini, mTOR and cancer: Insights into a complex relationship. Nat. Rev. Cancer 6, 729-734 (2006). (Pubitemid 44286004)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.9 , pp. 729-734
    • Sabatini, D.M.1
  • 37
    • 58149094542 scopus 로고    scopus 로고
    • S6K directly phosphorylates IRS-1 on Ser-270 to promote insulin resistance in response to TNF-A signaling through IKK2
    • J. Zhang, Z. Gao, J. Yin, M. J. Quon, J. Ye, S6K directly phosphorylates IRS-1 on Ser-270 to promote insulin resistance in response to TNF-a signaling through IKK2. J. Biol. Chem. 283, 35375-35382 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 35375-35382
    • Zhang, J.1    Gao, Z.2    Yin, J.3    Quon, M.J.4    Ye, J.5
  • 38
    • 0034947869 scopus 로고    scopus 로고
    • Mammalian target of rapamycin pathway regulates insulin signaling via subcellular redistribution of insulin receptor substrate 1 and integrates nutritional signals and metabolic signals of insulin
    • DOI 10.1128/MCB.21.15.5050-5062.2001
    • A. Takano, I. Usui, T. Haruta, J. Kawahara, T. Uno, M. Iwata, M. Kobayashi, Mammalian target of rapamycin pathway regulates insulin signaling via subcellular redistribution of insulin receptor substrate 1 and integrates nutritional signals and metabolic signals of insulin. Mol. Cell. Biol. 21, 5050-5062 (2001). (Pubitemid 32656402)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.15 , pp. 5050-5062
    • Takano, A.1    Usui, I.2    Haruta, T.3    Kawahara, J.4    Uno, T.5    Iwata, M.6    Kobayashi, M.7
  • 39
    • 0035851205 scopus 로고    scopus 로고
    • Amino acid and insulin signaling via the mTOR/p70 S6 kinase pathway. A negative feedback mechanism leading to insulin resistance in skeletal muscle cells
    • F. Tremblay, A. Marette, Amino acid and insulin signaling via the mTOR/p70 S6 kinase pathway. A negative feedback mechanism leading to insulin resistance in skeletal muscle cells. J. Biol. Chem. 276, 38052-38060 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 38052-38060
    • Tremblay, F.1    Marette, A.2
  • 42
    • 28644439239 scopus 로고    scopus 로고
    • Inhibition of cap-dependent translation via phosphorylation of eIF4G by protein kinase Pak2
    • DOI 10.1038/sj.emboj.7600868
    • J. Ling, S. J. Morley, J. A. Traugh, Inhibition of cap-dependent translation via phosphorylation of eIF4G by protein kinase Pak2. EMBO J. 24, 4094-4105 (2005). (Pubitemid 41752878)
    • (2005) EMBO Journal , vol.24 , Issue.23 , pp. 4094-4105
    • Ling, J.1    Morley, S.J.2    Traugh, J.A.3
  • 43
    • 79960925868 scopus 로고    scopus 로고
    • Mechanotransduction and the regulation of mTORC1 signaling in skeletal muscle
    • T. A. Hornberger, Mechanotransduction and the regulation of mTORC1 signaling in skeletal muscle. Int. J. Biochem. Cell Biol. 43, 1267-1276 (2011).
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 1267-1276
    • Hornberger, T.A.1
  • 44
    • 33645241260 scopus 로고    scopus 로고
    • The role of phospholipase D and phosphatidic acid in the mechanical activation of mTOR signaling in skeletal muscle
    • T. A. Hornberger, W. K. Chu, Y. W. Mak, J. W. Hsiung, S. A. Huang, S. Chien, The role of phospholipase D and phosphatidic acid in the mechanical activation of mTOR signaling in skeletal muscle. Proc. Natl. Acad. Sci. U.S.A. 103, 4741-4746 (2006).
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 4741-4746
    • Hornberger, T.A.1    Chu, W.K.2    Mak, Y.W.3    Hsiung, J.W.4    Huang, S.A.5    Chien, S.6
  • 46
    • 84877577382 scopus 로고    scopus 로고
    • Sustained activation of mTORC1 in skeletal muscle inhibits constitutive and starvation-induced autophagy and causes a severe, late-onset myopathy
    • P. Castets, S. Lin, N. Rion, S. Di Fulvio, K. Romanino, M. Guridi, S. Frank, L. A. Tintignac, M. Sinnreich, M. A. Rüegg, Sustained activation of mTORC1 in skeletal muscle inhibits constitutive and starvation-induced autophagy and causes a severe, late-onset myopathy. Cell Metab. 17, 731-744 (2013).
    • (2013) Cell Metab. , vol.17 , pp. 731-744
    • Castets, P.1    Lin, S.2    Rion, N.3    Di Fulvio, S.4    Romanino, K.5    Guridi, M.6    Frank, S.7    Tintignac, L.A.8    Sinnreich, M.9    Rüegg, M.A.10
  • 48
    • 33749257102 scopus 로고    scopus 로고
    • Developmental regulation of the activation of signaling components leading to translation initiation in skeletal muscle of neonatal pigs
    • DOI 10.1152/ajpendo.00069.2006
    • A. Suryawan, J. Escobar, J. W. Frank, H. V. Nguyen, T. A. Davis, Developmental regulation of the activation of signaling components leading to translation initiation in skeletal muscle of neonatal pigs. Am. J. Physiol. Endocrinol. Metab. 291, E849-E859 (2006). (Pubitemid 44484929)
    • (2006) American Journal of Physiology - Endocrinology and Metabolism , vol.291 , Issue.4
    • Suryawan, A.1    Escobar, J.2    Frank, J.W.3    Nguyen, H.V.4    Davis, T.A.5
  • 51
    • 79953647105 scopus 로고    scopus 로고
    • Rapamycin treatment augments motor neuron degeneration in SOD1G93A mouse model of amyotrophic lateral sclerosis
    • X. Zhang, L. Li, S. Chen, D. Yang, Y. Wang, Z. Wang, W. Le, Rapamycin treatment augments motor neuron degeneration in SOD1G93A mouse model of amyotrophic lateral sclerosis. Autophagy 7, 412-425 (2011).
    • (2011) Autophagy , vol.7 , pp. 412-425
    • Zhang, X.1    Li, L.2    Chen, S.3    Yang, D.4    Wang, Y.5    Wang, Z.6    Le, W.7
  • 52
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors
    • DOI 10.1016/S1097-2765(04)00211-4, PII S1097276504002114
    • T. N. Stitt, D. Drujan, B. A. Clarke, F. Panaro, Y. Timofeyva, W. O. Kline, M. Gonzalez, G. D. Yancopoulos, D. J. Glass, The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol. Cell 14, 395-403 (2004). (Pubitemid 38591410)
    • (2004) Molecular Cell , vol.14 , Issue.3 , 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
  • 53
    • 83455215759 scopus 로고    scopus 로고
    • Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: Insights from genetic models
    • S. Schiaffino, C. Mammucari, Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: Insights from genetic models. Skelet. Muscle 1, 4 (2011).
    • (2011) Skelet. Muscle , vol.1 , pp. 4
    • Schiaffino, S.1    Mammucari, C.2
  • 54
    • 24744446252 scopus 로고    scopus 로고
    • Transgenic overexpression of locally acting insulin-like growth factor-1 inhibits ubiquitin-mediated muscle atrophy in chronic left-ventricular dysfunction
    • DOI 10.1161/01.RES.0000179580.72375.c2
    • P. C. Schulze, J. Fang, K. A. Kassik, J. Gannon, M. Cupesi, C. MacGillivray, R. T. Lee, N. Rosenthal, Transgenic overexpression of locally acting insulin-like growth factor-1 inhibits ubiquitin-mediated muscle atrophy in chronic left-ventricular dysfunction. Circ. Res. 97, 418-426 (2005). (Pubitemid 41298171)
    • (2005) Circulation Research , vol.97 , Issue.5 , pp. 418-426
    • Schulze, P.C.1    Fang, J.2    Kassik, K.A.3    Gannon, J.4    Cupesi, M.5    MacGillivray, C.6    Lee, R.T.7    Rosenthal, N.8
  • 55
    • 0035735902 scopus 로고    scopus 로고
    • Mediation of IGF-1-induced skeletal myotube hypertrophy by Pl(3)K/Alt/mTOR and Pl(3)K/Akt/GSK3 pathways
    • DOI 10.1038/ncb1101-1009
    • C.Rommel, S. C.Bodine, B. A. Clarke,R.Rossman, L. Nunez,T.N.Stitt, G.D.Yancopoulos, D. J. Glass, Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways. Nat. Cell Biol. 3, 1009-1013 (2001). (Pubitemid 34428746)
    • (2001) Nature Cell Biology , vol.3 , Issue.11 , pp. 1009-1013
    • Rommel, C.1    Bodine, S.C.2    Clarke, B.A.3    Rossman, R.4    Nunez, L.5    Stitt, T.N.6    Yancopoulos, G.D.7    Glass, D.J.8
  • 56
    • 0027297310 scopus 로고
    • Myogenin gene disruption results in perinatal lethality because of severe muscle defect
    • DOI 10.1038/364532a0
    • Y. Nabeshima, K. Hanaoka, M. Hayasaka, E. Esumi, S. Li, I. Nonaka, Myogenin gene disruption results in perinatal lethality because of severe muscle defect. Nature 364, 532-535 (1993). (Pubitemid 23273098)
    • (1993) Nature , vol.364 , Issue.6437 , pp. 532-535
    • Nabeshima, Y.1    Hanaoka, K.2    Hayasaka, M.3    Esumi, E.4    Li, S.5    Nonaka, I.6    Nabeshima -, Y.I.7
  • 57
    • 0027258162 scopus 로고
    • Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene
    • DOI 10.1038/364501a0
    • P. Hasty, A. Bradley, J. H.Morris, D. G. Edmondson, J. M. Venuti, E. N. Olson, W. H. Klein, Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene. Nature 364, 501-506 (1993). (Pubitemid 23273093)
    • (1993) Nature , vol.364 , Issue.6437 , pp. 501-506
    • Hasty, P.1    Bradley, A.2    Morris, J.H.3    Edmondson, D.G.4    Venuti, J.M.5    Olson, E.N.6    Klein, W.H.7
  • 58
    • 33645055656 scopus 로고    scopus 로고
    • Loss of myogenin in postnatal life leads to normal skeletal muscle but reduced body size
    • J. R. Knapp, J. K. Davie, A. Myer, E. Meadows, E. N. Olson, W. H. Klein, Loss of myogenin in postnatal life leads to normal skeletal muscle but reduced body size. Development 133, 601-610 (2006).
    • (2006) Development , vol.133 , pp. 601-610
    • Knapp, J.R.1    Davie, J.K.2    Myer, A.3    Meadows, E.4    Olson, E.N.5    Klein, W.H.6


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