메뉴 건너뛰기




Volumn 318, Issue 1, 2012, Pages 33-42

GADD34 mediates cytoprotective autophagy in mutant huntingtin expressing cells via the mTOR pathway

Author keywords

Autophagy; Cell death; GADD34; HD; MTOR; TSC

Indexed keywords

CELL PROTEIN; ELONGATION FACTOR 2; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 34; HUNTINGTIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; MAMMALIAN TARGET OF RAPAMYCIN; TUBERIN; UNCLASSIFIED DRUG;

EID: 81355150598     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2011.08.020     Document Type: Article
Times cited : (39)

References (38)
  • 1
    • 23644455243 scopus 로고    scopus 로고
    • Gene-environment interactions, neuronal dysfunction and pathological plasticity in Huntington's disease
    • van Dellen A., Grote H.E., Hannan A.J. Gene-environment interactions, neuronal dysfunction and pathological plasticity in Huntington's disease. Clin. Exp. Pharmacol. Physiol. 2005, 32:1007-1019.
    • (2005) Clin. Exp. Pharmacol. Physiol. , vol.32 , pp. 1007-1019
    • van Dellen, A.1    Grote, H.E.2    Hannan, A.J.3
  • 2
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 1993, 72:971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 5
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B., Duden R., Rubinsztein D.C. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum. Mol. Genet. 2002, 11:1107-1117.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 7
    • 43949145273 scopus 로고    scopus 로고
    • Amelioration of protein misfolding disease by rapamycin: translation or autophagy?
    • Wyttenbach A., Hands S., King M.A., Lipkow K., Tolkovsky A.M. Amelioration of protein misfolding disease by rapamycin: translation or autophagy?. Autophagy 2008, 4:542-545.
    • (2008) Autophagy , vol.4 , pp. 542-545
    • Wyttenbach, A.1    Hands, S.2    King, M.A.3    Lipkow, K.4    Tolkovsky, A.M.5
  • 11
    • 33646548305 scopus 로고    scopus 로고
    • The amino acid sensitive TOR pathway from yeast to mammals
    • Dann S.G., Thomas G. The amino acid sensitive TOR pathway from yeast to mammals. FEBS Lett. 2006, 580:2821-2829.
    • (2006) FEBS Lett. , vol.580 , pp. 2821-2829
    • Dann, S.G.1    Thomas, G.2
  • 13
    • 0034672332 scopus 로고    scopus 로고
    • Interaction between DNA-damage protein GADD34 and a new member of the Hsp40 family of heat shock proteins that is induced by a DNA-damaging reagent
    • Hasegawa T., Xiao H., Hamajima F., Isobe K. Interaction between DNA-damage protein GADD34 and a new member of the Hsp40 family of heat shock proteins that is induced by a DNA-damaging reagent. Biochem. J. 2000, 352:795-800.
    • (2000) Biochem. J. , vol.352 , pp. 795-800
    • Hasegawa, T.1    Xiao, H.2    Hamajima, F.3    Isobe, K.4
  • 14
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha
    • Novoa I., Zeng H., Harding H.P., Ron D. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J. Cell Biol. 2001, 153:1011-1022.
    • (2001) J. Cell Biol. , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 15
    • 0037416211 scopus 로고    scopus 로고
    • Stress-induced gene expression requires programmed recovery from translational repression
    • Novoa I., Zhang Y., Zeng H., Jungreis R., Harding H.P., Ron D. Stress-induced gene expression requires programmed recovery from translational repression. EMBO J. 2003, 22:1180-1187.
    • (2003) EMBO J. , vol.22 , pp. 1180-1187
    • Novoa, I.1    Zhang, Y.2    Zeng, H.3    Jungreis, R.4    Harding, H.P.5    Ron, D.6
  • 16
    • 13744253138 scopus 로고    scopus 로고
    • Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2alpha dephosphorylation by the gamma(1)34.5 protein
    • Cheng G., Feng Z., He B. Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2alpha dephosphorylation by the gamma(1)34.5 protein. J. Virol. 2005, 79:1379-1388.
    • (2005) J. Virol. , vol.79 , pp. 1379-1388
    • Cheng, G.1    Feng, Z.2    He, B.3
  • 17
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress induced gene expression in mammalian cells
    • Harding H.P., Novoa I., Zhang Y., Zeng H., Wek R., Schapira M., Ron D. Regulated translation initiation controls stress induced gene expression in mammalian cells. Mol. Cell 2000, 6:1099-1108.
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 18
    • 0034968330 scopus 로고    scopus 로고
    • Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival
    • Harding H.P., Zeng H., Zhang Y., Jungries R., Chung P., Plesken H., Sabatini D.D., Ron D. Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival. Mol. Cell 2001, 7:1153-1163.
    • (2001) Mol. Cell , vol.7 , pp. 1153-1163
    • Harding, H.P.1    Zeng, H.2    Zhang, Y.3    Jungries, R.4    Chung, P.5    Plesken, H.6    Sabatini, D.D.7    Ron, D.8
  • 19
    • 0041703031 scopus 로고    scopus 로고
    • The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: elucidation by GADD34-deficient mice
    • Kojima E., Takeuchi A., Haneda M., Yagi A., Hasegawa T., Yamaki K., Takeda K., Akira S., Shimokata K., Isobe K. The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: elucidation by GADD34-deficient mice. FASEB J. 2003, 17:1573-1575.
    • (2003) FASEB J. , vol.17 , pp. 1573-1575
    • Kojima, E.1    Takeuchi, A.2    Haneda, M.3    Yagi, A.4    Hasegawa, T.5    Yamaki, K.6    Takeda, K.7    Akira, S.8    Shimokata, K.9    Isobe, K.10
  • 20
    • 39649114320 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins
    • Reijonen S., Putkonen N., Nørremølle A., Lindholm D., Korhonen L. Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins. Exp. Cell Res. 2008, 314:950-960.
    • (2008) Exp. Cell Res. , vol.314 , pp. 950-960
    • Reijonen, S.1    Putkonen, N.2    Nørremølle, A.3    Lindholm, D.4    Korhonen, L.5
  • 22
    • 33947538578 scopus 로고    scopus 로고
    • GADD34 inhibits mammalian target of rapamycin signaling via tuberous sclerosis complex and controls cell survival under bioenergetic stress
    • Watanabe R., Tambe Y., Inoue H., Isono T., Haneda M., Isobe K., Kobayashi T., Hino O., Okabe H., Chano T. GADD34 inhibits mammalian target of rapamycin signaling via tuberous sclerosis complex and controls cell survival under bioenergetic stress. Int. J. Mol. Med. 2007, 19:475-483.
    • (2007) Int. J. Mol. Med. , vol.19 , pp. 475-483
    • Watanabe, R.1    Tambe, Y.2    Inoue, H.3    Isono, T.4    Haneda, M.5    Isobe, K.6    Kobayashi, T.7    Hino, O.8    Okabe, H.9    Chano, T.10
  • 24
    • 10344253840 scopus 로고    scopus 로고
    • Critical role of endogenous Akt/IAPs and MEK1/ERK pathways in counteracting endoplasmic reticulum stress-induced cell death
    • Hu P., Han Z., Couvillon A.D., Exton J.H. Critical role of endogenous Akt/IAPs and MEK1/ERK pathways in counteracting endoplasmic reticulum stress-induced cell death. J. Biol. Chem. 2004, 279:49420-49429.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49420-49429
    • Hu, P.1    Han, Z.2    Couvillon, A.D.3    Exton, J.H.4
  • 25
    • 34249016897 scopus 로고    scopus 로고
    • Akt up- and down-regulation in response to endoplasmic reticulum stress
    • Hosoi T., Hyoda K., Okuma Y., Nomura Y., Ozawa K. Akt up- and down-regulation in response to endoplasmic reticulum stress. Brain Res. 2007, 1152:27-31.
    • (2007) Brain Res. , vol.1152 , pp. 27-31
    • Hosoi, T.1    Hyoda, K.2    Okuma, Y.3    Nomura, Y.4    Ozawa, K.5
  • 26
    • 44449161481 scopus 로고    scopus 로고
    • The TSC1-TSC2 complex: a molecular switchboard controlling cell growth
    • Huang J., Manning B.D. The TSC1-TSC2 complex: a molecular switchboard controlling cell growth. Biochem. J. 2008, 412:179-190.
    • (2008) Biochem. J. , vol.412 , pp. 179-190
    • Huang, J.1    Manning, B.D.2
  • 27
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
    • Inoki K., Li Y., Zhu T., Wu J., Guan K.L. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat. Cell Biol. 2002, 4:648-657.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.L.5
  • 28
    • 34548037901 scopus 로고    scopus 로고
    • Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium
    • Høyer-Hansen M., Jäättelä M. Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium. Cell Death Differ. 2007, 14:1576-1582.
    • (2007) Cell Death Differ. , vol.14 , pp. 1576-1582
    • Høyer-Hansen, M.1    Jäättelä, M.2
  • 29
    • 0005677775 scopus 로고
    • 3-Methyladenine: specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes
    • Seglen P.O., Gordon P.B. 3-Methyladenine: specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes. Proc. Natl. Acad. Sci. U.S.A. 1982, 79:1889-1892.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 1889-1892
    • Seglen, P.O.1    Gordon, P.B.2
  • 30
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald M.L., Lindquist S. Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev. 2008, 22:3308-3319.
    • (2008) Genes Dev. , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 31
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B., Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008, 132:27-42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 32
    • 77956268597 scopus 로고    scopus 로고
    • The evolutionarily conserved interaction between LC3 and p62 selectively mediates autophagy-dependent degradation of mutant huntingtin
    • Tung Y.T., Hsu W.M., Lee H., Huang W.P., Liao Y.F. The evolutionarily conserved interaction between LC3 and p62 selectively mediates autophagy-dependent degradation of mutant huntingtin. Cell. Mol. Neurobiol. 2010, 30:795-806.
    • (2010) Cell. Mol. Neurobiol. , vol.30 , pp. 795-806
    • Tung, Y.T.1    Hsu, W.M.2    Lee, H.3    Huang, W.P.4    Liao, Y.F.5
  • 33
    • 0347363611 scopus 로고    scopus 로고
    • Ischaemic preconditioning in the rat brain: effect on the activity of several initiation factors, Akt and extracellular signal-regulated protein kinase phosphorylation, and GRP78 and GADD34 expression
    • García L., Burda J., Hrehorovská M., Burda R., Martín M.E., Salinas M. Ischaemic preconditioning in the rat brain: effect on the activity of several initiation factors, Akt and extracellular signal-regulated protein kinase phosphorylation, and GRP78 and GADD34 expression. J. Neurochem. 2004, 88:136-147.
    • (2004) J. Neurochem. , vol.88 , pp. 136-147
    • García, L.1    Burda, J.2    Hrehorovská, M.3    Burda, R.4    Martín, M.E.5    Salinas, M.6
  • 34
    • 3343020683 scopus 로고    scopus 로고
    • GADD34 protein levels increase after transient ischemia in the cortex but not in the CA1 subfield: implications for post-ischemic recovery of protein synthesis in ischemia-resistant cells
    • Paschen W., Hayashi T., Saito A., Chan P.H. GADD34 protein levels increase after transient ischemia in the cortex but not in the CA1 subfield: implications for post-ischemic recovery of protein synthesis in ischemia-resistant cells. J. Neurochem. 2004, 90:694-700.
    • (2004) J. Neurochem. , vol.90 , pp. 694-700
    • Paschen, W.1    Hayashi, T.2    Saito, A.3    Chan, P.H.4
  • 35
    • 65949106140 scopus 로고    scopus 로고
    • Tuberous sclerosis complex activity is required to control neuronal stress responses in an mTOR-dependent manner
    • Di Nardo A., Kramvis I., Cho N., Sadowski A., Meikle L., Kwiatkowsk D.J., Sahin M. Tuberous sclerosis complex activity is required to control neuronal stress responses in an mTOR-dependent manner. J. Neurosci. 2009, 29:5926-5937.
    • (2009) J. Neurosci. , vol.29 , pp. 5926-5937
    • Di Nardo, A.1    Kramvis, I.2    Cho, N.3    Sadowski, A.4    Meikle, L.5    Kwiatkowsk, D.J.6    Sahin, M.7
  • 36
    • 40649104735 scopus 로고    scopus 로고
    • Loss of the tuberous sclerosis complex tumor suppressors triggers the unfolded protein response to regulate insulin signaling and apoptosis
    • Ozcan U., Ozcan L., Yilmaz E., Düvel K., Sahin M., Manning B.D., Hotamisligil G.S. Loss of the tuberous sclerosis complex tumor suppressors triggers the unfolded protein response to regulate insulin signaling and apoptosis. Mol. Cell 2008, 29:541-551.
    • (2008) Mol. Cell , vol.29 , pp. 541-551
    • Ozcan, U.1    Ozcan, L.2    Yilmaz, E.3    Düvel, K.4    Sahin, M.5    Manning, B.D.6    Hotamisligil, G.S.7
  • 38
    • 70349973869 scopus 로고    scopus 로고
    • Expandind roles for AMP-activated protein kinase in neuronal survival and autophagy
    • Poels J., Spasić M.R., Callaerts P., Norga K.K. Expandind roles for AMP-activated protein kinase in neuronal survival and autophagy. Bioessays 2009, 31:944-952.
    • (2009) Bioessays , vol.31 , pp. 944-952
    • Poels, J.1    Spasić, M.R.2    Callaerts, P.3    Norga, K.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.