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Volumn 441, Issue 7095, 2006, Pages 885-889

Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice

Author keywords

[No Author keywords available]

Indexed keywords

BIODIVERSITY; BIOMEDICAL ENGINEERING; CELLS; DEGRADATION; DISEASES; PROTEINS;

EID: 33745192802     PISSN: 00280836     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/nature04724     Document Type: Article
Times cited : (3317)

References (30)
  • 1
    • 0442323561 scopus 로고    scopus 로고
    • Autophagy: In sickness and in health
    • Cuervo, A. M. Autophagy: in sickness and in health. Trends Cell Biol. 14, 70-77 (2004).
    • (2004) Trends Cell Biol. , vol.14 , pp. 70-77
    • Cuervo, A.M.1
  • 2
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • Levine, B. & Klionsky, D. J. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev. Cell 6, 463-477 (2004).
    • (2004) Dev. Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 3
    • 14044277429 scopus 로고    scopus 로고
    • The molecular machinery of autophagy: Unanswered questions
    • Klionsky, D. J. The molecular machinery of autophagy: unanswered questions. J. Cell Sci. 118, 7-18 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 7-18
    • Klionsky, D.J.1
  • 4
    • 27644493346 scopus 로고    scopus 로고
    • The pleiotropic role of autophagy: From protein metabolism to bactericide
    • Mizushima, N. The pleiotropic role of autophagy: from protein metabolism to bactericide. Cell Death Differ. 12, 1535-1541 (2005).
    • (2005) Cell Death Differ. , vol.12 , pp. 1535-1541
    • Mizushima, N.1
  • 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. 11, 1107-1117 (2002).
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 6
    • 0344874551 scopus 로고    scopus 로고
    • Emerging role for autophagy in the removal of aggresomes in Schwann cells
    • Fortun, J., Dunn, W. A. Jr, Joy, S., Li, J. & Notterpek, L. Emerging role for autophagy in the removal of aggresomes in Schwann cells. J. Neurosci. 23, 10672-10680 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 10672-10680
    • Fortun, J.1    Dunn Jr., W.A.2    Joy, S.3    Li, J.4    Notterpek, L.5
  • 7
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • Ravikumar, B. et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nature Genet. 36, 585-595 (2004).
    • (2004) Nature Genet. , vol.36 , pp. 585-595
    • Ravikumar, B.1
  • 8
    • 24944482408 scopus 로고    scopus 로고
    • Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation
    • Iwata, A. et al. Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation. Proc. Natl Acad. Sci. USA 102, 13135-13140 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13135-13140
    • Iwata, A.1
  • 10
    • 11144245626 scopus 로고    scopus 로고
    • The role of autophagy during the early neonatal starvation period
    • Kuma, A. et al. The role of autophagy during the early neonatal starvation period. Nature 432, 1032-1036 (2004).
    • (2004) Nature , vol.432 , pp. 1032-1036
    • Kuma, A.1
  • 11
    • 21044455137 scopus 로고    scopus 로고
    • Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice
    • Komatsu, M. et al. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. J. Cell Biol. 169, 425-434 (2005).
    • (2005) J. Cell Biol. , vol.169 , pp. 425-434
    • Komatsu, M.1
  • 12
    • 0030267396 scopus 로고    scopus 로고
    • Bypass of lethality with mosaic mice generated by Cre-loxP-mediated recombination
    • Betz, U. A., Vosshenrich, C. A., Rajewsky, K. & Muller, W. Bypass of lethality with mosaic mice generated by Cre-loxP-mediated recombination. Curr. Biol. 6, 1307-1316 (1996).
    • (1996) Curr. Biol. , vol.6 , pp. 1307-1316
    • Betz, U.A.1    Vosshenrich, C.A.2    Rajewsky, K.3    Muller, W.4
  • 13
    • 0035911162 scopus 로고    scopus 로고
    • Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells
    • Mizushima, N. et al. Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. J. Cell Biol. 152, 657-667 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 657-667
    • Mizushima, N.1
  • 14
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya, Y. et al. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J. 19, 5720-5728 (2000).
    • (2000) EMBO J. , vol.19 , pp. 5720-5728
    • Kabeya, Y.1
  • 15
    • 0027465098 scopus 로고
    • Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: A mouse model of amyotrophic lateral sclerosis
    • Cote, F., Collard, J. F. & Julien, J. P. Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: a mouse model of amyotrophic lateral sclerosis. Cell 73, 35-46 (1993).
    • (1993) Cell , vol.73 , pp. 35-46
    • Cote, F.1    Collard, J.F.2    Julien, J.P.3
  • 16
    • 16044373842 scopus 로고    scopus 로고
    • Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
    • Mangiarini, L. et al. Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87, 493-506 (1996).
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1
  • 17
    • 0025290911 scopus 로고
    • Axonal degeneration of ascending sensory neurons in gracile axonal dystrophy mutant mouse
    • Kikuchi, T., Mukoyama, M., Yamazaki, K. & Moriya, H. Axonal degeneration of ascending sensory neurons in gracile axonal dystrophy mutant mouse. Acta Neuropathol. (Berl.) 80, 145-151 (1990).
    • (1990) Acta Neuropathol. (Berl.) , vol.80 , pp. 145-151
    • Kikuchi, T.1    Mukoyama, M.2    Yamazaki, K.3    Moriya, H.4
  • 18
    • 0025053468 scopus 로고
    • Axonal abnormalities in cerebellar Purkinje cells of the 'hyperspiny Purkinje cell' mutant mouse
    • Sotelo, C. Axonal abnormalities in cerebellar Purkinje cells of the 'hyperspiny Purkinje cell' mutant mouse. J. Neurocytol. 19, 737-755 (1990).
    • (1990) J. Neurocytol. , vol.19 , pp. 737-755
    • Sotelo, C.1
  • 19
    • 0037025034 scopus 로고    scopus 로고
    • Synapse-independent and synapse-dependent apoptosis of cerebellar granule cells in postnatal rabbits occur at two subsequent but partly overlapping developmental stages
    • Lossi, L., Mioletti, S. & Merighi, A. Synapse-independent and synapse-dependent apoptosis of cerebellar granule cells in postnatal rabbits occur at two subsequent but partly overlapping developmental stages. Neuroscience 112, 509-523 (2002).
    • (2002) Neuroscience , vol.112 , pp. 509-523
    • Lossi, L.1    Mioletti, S.2    Merighi, A.3
  • 20
    • 0031577470 scopus 로고    scopus 로고
    • A transgenic mouse line that retains Cre recombinase activity in mature oocytes irrespective of the cre transgene transmission
    • Sakai, K. & Miyazaki, J. A transgenic mouse line that retains Cre recombinase activity in mature oocytes irrespective of the cre transgene transmission. Biochem. Biophys. Res. Commun. 237, 318-324 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 318-324
    • Sakai, K.1    Miyazaki, J.2
  • 21
    • 0029155706 scopus 로고
    • Inducible gene targeting in mice
    • Kuhn, R., Schwenk, F., Aguet, M. & Rajewsky, K. Inducible gene targeting in mice. Science 269, 1427-1429 (1995).
    • (1995) Science , vol.269 , pp. 1427-1429
    • Kuhn, R.1    Schwenk, F.2    Aguet, M.3    Rajewsky, K.4
  • 22
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R. R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10, 524-530 (2000).
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 23
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou, F., Finkbeiner, S., Devys, D. & Greenberg, M. E. Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95, 55-66 (1998).
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 24
    • 0032590053 scopus 로고    scopus 로고
    • Huntington aggregates may not predict neuronal death in Huntington's disease
    • Kuemmerle, S. et al. Huntington aggregates may not predict neuronal death in Huntington's disease. Ann. Neurol. 46, 842-849 (1999).
    • (1999) Ann. Neurol. , vol.46 , pp. 842-849
    • Kuemmerle, S.1
  • 25
    • 0037388418 scopus 로고    scopus 로고
    • Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein
    • Taylor, J. P. et al. Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein. Hum. Mol. Genet. 12, 749-757 (2003).
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 749-757
    • Taylor, J.P.1
  • 26
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neurona death
    • Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R. & Finkbeiner, S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neurona death. Nature 431, 805-810 (2004).
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 27
    • 1042266326 scopus 로고    scopus 로고
    • Aggresomes formed by α-synuclein and synphilin-1 are cytoprotective
    • Tanaka, M. et al. Aggresomes formed by α-synuclein and synphilin-1 are cytoprotective. J. Biol. Chem. 279, 4625-4631 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 4625-4631
    • Tanaka, M.1
  • 28
    • 27944504351 scopus 로고    scopus 로고
    • P62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy, G. et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171, 603-614 (2005).
    • (2005) J. Cell Biol. , vol.171 , pp. 603-614
    • Bjorkoy, G.1
  • 29
    • 3142723983 scopus 로고    scopus 로고
    • Socs3 deficiency in the brain elevates leptin sensitivity and confers resistance to diet-induced obesity
    • Mori, H. et al. Socs3 deficiency in the brain elevates leptin sensitivity and confers resistance to diet-induced obesity. Nature Med. 10, 739-743 (2004).
    • (2004) Nature Med. , vol.10 , pp. 739-743
    • Mori, H.1
  • 30
    • 0025945812 scopus 로고
    • Stacks of flattened smooth endoplasmic reticulum highly enriched in inositol 1,4,5-trisphosphate (InsP3) receptor in mouse cerebellar Purkinje cells
    • Yamamoto, A. et al. Stacks of flattened smooth endoplasmic reticulum highly enriched in inositol 1,4,5-trisphosphate (InsP3) receptor in mouse cerebellar Purkinje cells. Cell Struct. Funct. 16, 419-432 (1991).
    • (1991) Cell Struct. Funct. , vol.16 , pp. 419-432
    • Yamamoto, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.