메뉴 건너뛰기




Volumn 32, Issue 27, 2012, Pages 9133-9142

ALS-associated ataxin 2 polyQ expansions enhance stress-induced caspase 3 activation and increase TDP-43 pathological modifications

Author keywords

[No Author keywords available]

Indexed keywords

ATAXIN 2; CASPASE 3; NUCLEIC ACID BINDING PROTEIN; POLYGLUTAMINE; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84863431578     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.0996-12.2012     Document Type: Article
Times cited : (78)

References (62)
  • 2
    • 74949135753 scopus 로고    scopus 로고
    • Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis
    • Barmada SJ, Skibinski G, Korb E, Rao EJ, Wu JY, Finkbeiner S (2010) Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis. J Neurosci 30:639-649.
    • (2010) J Neurosci , vol.30 , pp. 639-649
    • Barmada, S.J.1    Skibinski, G.2    Korb, E.3    Rao, E.J.4    Wu, J.Y.5    Finkbeiner, S.6
  • 3
    • 78650680776 scopus 로고    scopus 로고
    • Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1
    • Brady OA, Meng P, Zheng Y, Mao Y, Hu F (2011) Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1. J Neurochem 116:248-259.
    • (2011) J Neurochem , vol.116 , pp. 248-259
    • Brady, O.A.1    Meng, P.2    Zheng, Y.3    Mao, Y.4    Hu, F.5
  • 4
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: The ins and outs of translation
    • Buchan JR, Parker R (2009) Eukaryotic stress granules: the ins and outs of translation. Mol Cell 36:932-941.
    • (2009) Mol Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 5
    • 80051566617 scopus 로고    scopus 로고
    • Ataxin-2 intermediate-length polyglutamine: A possible risk factor for Chinese patients with amyotrophic lateral sclerosis
    • Chen Y, Huang R, Yang Y, Chen K, Song W, Pan P, Li J, Shang HF (2011) Ataxin-2 intermediate-length polyglutamine: a possible risk factor for Chinese patients with amyotrophic lateral sclerosis. Neurobiol Aging 32:1925.e1-e5.
    • (2011) Neurobiol Aging , vol.32
    • Chen, Y.1    Huang, R.2    Yang, Y.3    Chen, K.4    Song, W.5    Pan, P.6    Li, J.7    Shang, H.F.8
  • 6
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: Deciphering selective motor neuron death in ALS
    • Cleveland DW, Rothstein JD (2001) From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat Rev Neurosci 2:806-819.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 7
    • 84155171976 scopus 로고    scopus 로고
    • Understanding the role of TDP-43 and FUS/TLS in ALS and beyond
    • Da Cruz S, Cleveland DW (2011) Understanding the role of TDP-43 and FUS/TLS in ALS and beyond. Curr Opin Neurobiol 21:904-919.
    • (2011) Curr Opin Neurobiol , vol.21 , pp. 904-919
    • da Cruz, S.1    Cleveland, D.W.2
  • 12
    • 79959636879 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis and spinocerebellar ataxia 2
    • Fischbeck KH, Pulst SM (2011) Amyotrophic lateral sclerosis and spinocerebellar ataxia 2. Neurology 76:2050-2051.
    • (2011) Neurology , vol.76 , pp. 2050-2051
    • Fischbeck, K.H.1    Pulst, S.M.2
  • 13
    • 76149120427 scopus 로고    scopus 로고
    • Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery
    • Freibaum BD, Chitta RK, High AA, Taylor JP (2010) Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery. J Proteome Res 9:1104-1120.
    • (2010) J Proteome Res , vol.9 , pp. 1104-1120
    • Freibaum, B.D.1    Chitta, R.K.2    High, A.A.3    Taylor, J.P.4
  • 18
    • 0033811788 scopus 로고    scopus 로고
    • Nuclear localization or inclusion body formation of ataxin-2 are not necessary for SCA2 pathogenesis in mouse or human
    • Huynh DP, Figueroa K, Hoang N, Pulst SM (2000) Nuclear localization or inclusion body formation of ataxin-2 are not necessary for SCA2 pathogenesis in mouse or human. Nat Genet 26:44-50.
    • (2000) Nat Genet , vol.26 , pp. 44-50
    • Huynh, D.P.1    Figueroa, K.2    Hoang, N.3    Pulst, S.M.4
  • 19
    • 0037767510 scopus 로고    scopus 로고
    • Expansion of the polyQ repeat in ataxin-2 alters its Golgi localization, disrupts the Golgi complex and causes cell death
    • Huynh DP, Yang HT, Vakharia H, Nguyen D, Pulst SM (2003) Expansion of the polyQ repeat in ataxin-2 alters its Golgi localization, disrupts the Golgi complex and causes cell death. Hum Mol Genet 12:1485-1496.
    • (2003) Hum Mol Genet , vol.12 , pp. 1485-1496
    • Huynh, D.P.1    Yang, H.T.2    Vakharia, H.3    Nguyen, D.4    Pulst, S.M.5
  • 23
    • 4344676312 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type 2 with Levodopa-responsive parkinsonism culminating in motor neuron disease
    • Infante J, Berciano J, Volpini V, Corral J, Polo JM, Pascual J, Combarros O (2004) Spinocerebellar ataxia type 2 with Levodopa-responsive parkinsonism culminating in motor neuron disease. Mov Disord 19:848-852.
    • (2004) Mov Disord , vol.19 , pp. 848-852
    • Infante, J.1    Berciano, J.2    Volpini, V.3    Corral, J.4    Polo, J.M.5    Pascual, J.6    Combarros, O.7
  • 25
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Johnson BS, Snead D, Lee JJ, McCaffery JM, Shorter J, Gitler AD (2009) TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J Biol Chem 284:20329-20339.
    • (2009) J Biol Chem , vol.284 , pp. 20329-20339
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3    McCaffery, J.M.4    Shorter, J.5    Gitler, A.D.6
  • 26
    • 70450191208 scopus 로고    scopus 로고
    • Preventing Ataxin-3 protein cleavage mitigates degeneration in a Drosophila model of SCA3
    • Jung J, Xu K, Lessing D, Bonini NM (2009) Preventing Ataxin-3 protein cleavage mitigates degeneration in a Drosophila model of SCA3. Hum Mol Genet 18:4843-4852.
    • (2009) Hum Mol Genet , vol.18 , pp. 4843-4852
    • Jung, J.1    Xu, K.2    Lessing, D.3    Bonini, N.M.4
  • 27
    • 78951492184 scopus 로고    scopus 로고
    • Modulation of stress granules and P bodies during dicistrovirus infection
    • Khong A, Jan E (2011) Modulation of stress granules and P bodies during dicistrovirus infection. J Virol 85:1439-1451.
    • (2011) J Virol , vol.85 , pp. 1439-1451
    • Khong, A.1    Jan, E.2
  • 29
    • 37449030154 scopus 로고    scopus 로고
    • The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response
    • Kwon S, Zhang Y, Matthias P (2007) The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response. Genes Dev 21:3381-3394.
    • (2007) Genes Dev , vol.21 , pp. 3381-3394
    • Kwon, S.1    Zhang, Y.2    Matthias, P.3
  • 30
    • 77956147372 scopus 로고    scopus 로고
    • Neurodegeneration: An expansion in ALS genetics
    • Lagier-Tourenne C, Cleveland DW (2010) Neurodegeneration: an expansion in ALS genetics. Nature 466:1052-1053.
    • (2010) Nature , vol.466 , pp. 1052-1053
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 33
    • 78649750391 scopus 로고    scopus 로고
    • Phosphorylation promotes neurotoxicity in a Caenorhabditis elegans model of TDP-43 proteinopathy
    • Liachko NF, Guthrie CR, Kraemer BC (2010) Phosphorylation promotes neurotoxicity in a Caenorhabditis elegans model of TDP-43 proteinopathy. J Neurosci 30:16208-16219.
    • (2010) J Neurosci , vol.30 , pp. 16208-16219
    • Liachko, N.F.1    Guthrie, C.R.2    Kraemer, B.C.3
  • 36
    • 0030668895 scopus 로고    scopus 로고
    • The expansion of the CAG repeat in ataxin-2 is a frequent cause of autosomal dominant spinocerebellar ataxia
    • Lorenzetti D, Bohlega S, Zoghbi HY (1997) The expansion of the CAG repeat in ataxin-2 is a frequent cause of autosomal dominant spinocerebellar ataxia. Neurology 49:1009-1013.
    • (1997) Neurology , vol.49 , pp. 1009-1013
    • Lorenzetti, D.1    Bohlega, S.2    Zoghbi, H.Y.3
  • 38
    • 78650607406 scopus 로고    scopus 로고
    • Both cytoplasmic and nuclear accumulations of the protein are neurotoxic in Drosophila models of TDP-43 proteinopathies
    • Miguel L, Frébourg T, Campion D, Lecourtois M (2011) Both cytoplasmic and nuclear accumulations of the protein are neurotoxic in Drosophila models of TDP-43 proteinopathies. Neurobiol Dis 41:398-406.
    • (2011) Neurobiol Dis , vol.41 , pp. 398-406
    • Miguel, L.1    Frébourg, T.2    Campion, D.3    Lecourtois, M.4
  • 39
    • 73449090497 scopus 로고    scopus 로고
    • Rare association of motor neuron disease and spinocerebellar ataxia type 2 (SCA2): A new case and review of the literature
    • Nanetti L, Fancellu R, Tomasello C, Gellera C, Pareyson D, Mariotti C (2009) Rare association of motor neuron disease and spinocerebellar ataxia type 2 (SCA2): a new case and review of the literature. J Neurol 256:1926-1928.
    • (2009) J Neurol , vol.256 , pp. 1926-1928
    • Nanetti, L.1    Fancellu, R.2    Tomasello, C.3    Gellera, C.4    Pareyson, D.5    Mariotti, C.6
  • 42
    • 36049003085 scopus 로고    scopus 로고
    • Ataxin-2 mediated cell death is dependent on domains downstream of the polyQ repeat
    • Ng H, Pulst SM, Huynh DP (2007) Ataxin-2 mediated cell death is dependent on domains downstream of the polyQ repeat. Exp Neurol 208:207-215.
    • (2007) Exp Neurol , vol.208 , pp. 207-215
    • Ng, H.1    Pulst, S.M.2    Huynh, D.P.3
  • 43
    • 73649148708 scopus 로고    scopus 로고
    • Characterization of alternative isoforms and inclusion body of the TAR DNA-binding protein-43
    • Nishimoto Y, Ito D, Yagi T, Nihei Y, Tsunoda Y, Suzuki N (2010) Characterization of alternative isoforms and inclusion body of the TAR DNA-binding protein-43. J Biol Chem 285:608-619.
    • (2010) J Biol Chem , vol.285 , pp. 608-619
    • Nishimoto, Y.1    Ito, D.2    Yagi, T.3    Nihei, Y.4    Tsunoda, Y.5    Suzuki, N.6
  • 44
    • 58149498300 scopus 로고    scopus 로고
    • Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells
    • Nonaka T, Arai T, Buratti E, Baralle FE, Akiyama H, Hasegawa M (2009) Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells. FEBS Lett 583:394-400.
    • (2009) FEBS Lett , vol.583 , pp. 394-400
    • Nonaka, T.1    Arai, T.2    Buratti, E.3    Baralle, F.E.4    Akiyama, H.5    Hasegawa, M.6
  • 46
    • 53349165578 scopus 로고    scopus 로고
    • A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly
    • Ohn T, Kedersha N, Hickman T, Tisdale S, Anderson P (2008) A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly. Nat Cell Biol 10:1224-1231.
    • (2008) Nat Cell Biol , vol.10 , pp. 1224-1231
    • Ohn, T.1    Kedersha, N.2    Hickman, T.3    Tisdale, S.4    Anderson, P.5
  • 47
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • Orr HT, Zoghbi HY (2007) Trinucleotide repeat disorders. Annu Rev Neurosci 30:575-621.
    • (2007) Annu Rev Neurosci , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 48
    • 79956304001 scopus 로고    scopus 로고
    • A "twohit" hypothesis for inclusion formation by C-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubuledependent transport
    • Pesiridis GS, Tripathy K, Tanik S, Trojanowski JQ, Lee VM (2011) A "twohit" hypothesis for inclusion formation by C-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubuledependent transport. J Biol Chem 286:18845-18855.
    • (2011) J Biol Chem , vol.286 , pp. 18845-18855
    • Pesiridis, G.S.1    Tripathy, K.2    Tanik, S.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 50
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington's disease and related disorders
    • Ross CA (2002) Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders. Neuron 35:819-822.
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.A.1
  • 54
    • 77955099645 scopus 로고    scopus 로고
    • Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae
    • Swisher KD, Parker R (2010) Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae. PLoS One 5:e10006.
    • (2010) PLoS One , vol.5
    • Swisher, K.D.1    Parker, R.2
  • 56
    • 40949135034 scopus 로고    scopus 로고
    • Regulation of stress granule dynamics by Grb7 and FAK signalling pathway
    • Tsai NP, Ho PC, Wei LN (2008) Regulation of stress granule dynamics by Grb7 and FAK signalling pathway. EMBO J 27:715-726.
    • (2008) EMBO J , vol.27 , pp. 715-726
    • Tsai, N.P.1    Ho, P.C.2    Wei, L.N.3
  • 59
    • 35848929915 scopus 로고    scopus 로고
    • Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase
    • White JP, Cardenas AM, Marissen WE, Lloyd RE (2007) Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase. Cell Host Microbe 2:295-305.
    • (2007) Cell Host Microbe , vol.2 , pp. 295-305
    • White, J.P.1    Cardenas, A.M.2    Marissen, W.E.3    Lloyd, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.