메뉴 건너뛰기




Volumn 9, Issue 18, 2010, Pages 3704-3708

HDAC1 in axonal degeneration: A matter of subcellular localization

Author keywords

Demyelination; Histone deacetylase; Multiple sclerosis; Neurodegeneration; Nuclear export

Indexed keywords

ACETYL COENZYME A; ALPHA TUBULIN; AMYLOID PRECURSOR PROTEIN; ASPARTIC ACID; BRAIN DERIVED NEUROTROPHIC FACTOR; CYTOKINE; EXCITATORY AMINO ACID; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 6; HUNTINGTIN; KINESIN 1; LEPTOMYCIN B; MOLECULAR MOTOR; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; N ACETYLASPARTIC ACID; SIRTUIN 2; TAU PROTEIN;

EID: 77957013369     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.9.18.12716     Document Type: Review
Times cited : (18)

References (42)
  • 1
    • 33749059726 scopus 로고    scopus 로고
    • The neurobiology of multiple sclerosis: Genes, inflammation and neurodegeneration
    • Hauser SL, Oksenberg JR. The neurobiology of multiple sclerosis: genes, inflammation and neurodegeneration. Neuron 2006; 52:7-9.
    • (2006) Neuron , vol.52 , pp. 7-9
    • Hauser, S.L.1    Oksenberg, J.R.2
  • 4
    • 2942647959 scopus 로고    scopus 로고
    • Central nervous system atrophy and clinical status in multiple sclerosis
    • Zivadinov R, Bakshi R. Central nervous system atrophy and clinical status in multiple sclerosis. J Neuroimaging 2004; 14:27-35.
    • (2004) J Neuroimaging , vol.14 , pp. 27-35
    • Zivadinov, R.1    Bakshi, R.2
  • 5
    • 0033663894 scopus 로고    scopus 로고
    • Neurological disability correlates with spinal cord axonal loss and reduced N-acetyl aspartate in chronic multiple sclerosis patients
    • Bjartmar C, Kidd G, Mork S, Rudick R, Trapp BD. Neurological disability correlates with spinal cord axonal loss and reduced N-acetyl aspartate in chronic multiple sclerosis patients. Ann Neurol 2000; 48:893-901.
    • (2000) Ann Neurol , vol.48 , pp. 893-901
    • Bjartmar, C.1    Kidd, G.2    Mork, S.3    Rudick, R.4    Trapp, B.D.5
  • 6
    • 0031731910 scopus 로고    scopus 로고
    • N-acetyl aspartate: A marker for neuronal loss or mitochondrial dysfunction
    • Clark JB. N-acetyl aspartate: a marker for neuronal loss or mitochondrial dysfunction. Dev Neurosci 1998; 20:271-6.
    • (1998) Dev Neurosci , vol.20 , pp. 271-276
    • Clark, J.B.1
  • 7
    • 16844384074 scopus 로고    scopus 로고
    • Metabolite changes in normal-appearing gray and white matter are linked with disability in early primary progressive multiple sclerosis
    • DOI 10.1001/archneur.62.4.569
    • Sastre-Garriga J, Ingle GT, Chard DT, Ramio-Torrenta L, McLean MA, Miller DH, et al. Metabolite changes in normal-appearing gray and white matter are linked with disability in early primary progressive multiple sclerosis. Arch Neurol 2005; 62:569-73. (Pubitemid 40489887)
    • (2005) Archives of Neurology , vol.62 , Issue.4 , pp. 569-573
    • Sastre-Garriga, J.1    Ingle, G.T.2    Chard, D.T.3    Ramio-Torrenta, Li.4    McLean, M.A.5    Miller, D.H.6    Thompson, A.J.7
  • 8
    • 0001710321 scopus 로고    scopus 로고
    • MRI in multiple sclerosis: Correlation with expanded disability status scale (EDSS)
    • Barkhof F. MRI in multiple sclerosis: correlation with expanded disability status scale (EDSS). Mult Scler 1999; 5:283-6. (Pubitemid 29405626)
    • (1999) Multiple Sclerosis , vol.5 , Issue.4 , pp. 283-286
    • Barkhof, F.1
  • 10
    • 0031002545 scopus 로고    scopus 로고
    • Axonal damage in acute multiple sclerosis lesions
    • DOI 10.1093/brain/120.3.393
    • Ferguson B, Matyszak MK, Esiri MM, Perry VH. Axonal damage in acute multiple sclerosis lesions. Brain 1997; 120:393-9. (Pubitemid 27153632)
    • (1997) Brain , vol.120 , Issue.3 , pp. 393-399
    • Ferguson, B.1    Matyszak, M.K.2    Esiri, M.M.3    Perry, V.H.4
  • 11
    • 0034666282 scopus 로고    scopus 로고
    • Neurofilaments are transported rapidly but intermittently in axons: Implications for slow axonal transport
    • Roy S, Coffee P, Smith G, Liem RK, Brady ST, Black MM. Neurofilaments are transported rapidly but intermittently in axons: implications for slow axonal transport. J Neurosci 2000; 20:6849-61.
    • (2000) J Neurosci , vol.20 , pp. 6849-6861
    • Roy, S.1    Coffee, P.2    Smith, G.3    Liem, R.K.4    Brady, S.T.5    Black, M.M.6
  • 12
    • 0021131071 scopus 로고
    • Axonal transport of the cytoplasmic matrix
    • Lasek RJ, Garner JA, Brady ST. Axonal transport of the cytoplasmic matrix. J Cell Biol 1984; 99:212-21.
    • (1984) J Cell Biol , vol.99 , pp. 212-221
    • Lasek, R.J.1    Garner, J.A.2    Brady, S.T.3
  • 13
    • 33845993250 scopus 로고    scopus 로고
    • Kinesin-1 structural organization and conformational changes revealed by FRET stoichiometry in live cells
    • DOI 10.1083/jcb.200605097
    • Cai D, Hoppe AD, Swanson JA, Verhey KJ. Kinesin-1 structural organization and conformational changes revealed by FRET stoichiometry in live cells. J Cell Biol 2007; 176:51-63. (Pubitemid 46041680)
    • (2007) Journal of Cell Biology , vol.176 , Issue.1 , pp. 51-63
    • Cai, D.1    Hoppe, A.D.2    Swanson, J.A.3    Verhey, K.J.4
  • 14
    • 34547473554 scopus 로고    scopus 로고
    • Control of a Kinesin-Cargo Linkage Mechanism by JNK Pathway Kinases
    • DOI 10.1016/j.cub.2007.06.062, PII S0960982207016314
    • Horiuchi D, Collins CA, Bhat P, Barkus RV, Diantonio A, Saxton WM. Control of a kinesin-cargo linkage mechanism by JNK pathway kinases. Curr Biol 2007; 17:1313-7. (Pubitemid 47176890)
    • (2007) Current Biology , vol.17 , Issue.15 , pp. 1313-1317
    • Horiuchi, D.1    Collins, C.A.2    Bhat, P.3    Barkus, R.V.4    DiAntonio, A.5    Saxton, W.M.6
  • 15
    • 0036469290 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility
    • DOI 10.1093/emboj/21.3.281
    • Morfini G, Szebenyi G, Elluru R, Ratner N, Brady ST. Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesinbased motility. EMBO J 2002; 21:281-93. (Pubitemid 34137290)
    • (2002) EMBO Journal , vol.21 , Issue.3 , pp. 281-293
    • Morfini, G.1    Szebenyi, G.2    Elluru, R.3    Ratner, N.4    Brady, S.T.5
  • 16
    • 37749000849 scopus 로고    scopus 로고
    • Disruption of KIF17-Mint1 interaction by CaMKII-dependent phosphorylation: A molecular model of kinesin-cargo release
    • Guillaud L, Wong R, Hirokawa N. Disruption of KIF17-Mint1 interaction by CaMKII-dependent phosphorylation: a molecular model of kinesin-cargo release. Nat Cell Biol 2008; 10:19-29.
    • (2008) Nat Cell Biol , vol.10 , pp. 19-29
    • Guillaud, L.1    Wong, R.2    Hirokawa, N.3
  • 18
    • 0023389780 scopus 로고
    • Identification of an acetylation site of Chlamydomonas alpha-tubulin
    • LeDizet M, Piperno G. Identification of an acetylation site of Chlamydomonas alpha-tubulin. Proc Natl Acad Sci USA 1987; 84:5720-4.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5720-5724
    • LeDizet, M.1    Piperno, G.2
  • 21
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 2003; 11:437-44.
    • (2003) Mol Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 23
    • 0036479127 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel histone deacetylase HDAC10
    • Guardiola AR, Yao TP. Molecular cloning and characterization of a novel histone deacetylase HDAC10. J Biol Chem 2002; 277:3350-6.
    • (2002) J Biol Chem , vol.277 , pp. 3350-3356
    • Guardiola, A.R.1    Yao, T.P.2
  • 24
    • 0037067696 scopus 로고    scopus 로고
    • Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family
    • Gao L, Cueto MA, Asselbergs F, Atadja P. Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family. J Biol Chem 2002; 277:25748-55.
    • (2002) J Biol Chem , vol.277 , pp. 25748-25755
    • Gao, L.1    Cueto, M.A.2    Asselbergs, F.3    Atadja, P.4
  • 25
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • Dompierre JP, Godin JD, Charrin BC, Cordelieres FP, King SJ, Humbert S, Saudou F. Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J Neurosci 2007; 27:3571-83.
    • (2007) J Neurosci , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1    Godin, J.D.2    Charrin, B.C.3    Cordelieres, F.P.4    King, S.J.5    Humbert, S.6    Saudou, F.7
  • 26
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore C, Lee VM, Trojanowski JQ. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat Rev Neurosci 2007; 8:663-72.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 28
    • 33751243629 scopus 로고    scopus 로고
    • Neuronal intermediate filaments and ALS: A new look at an old question
    • Xiao S, McLean J, Robertson J. Neuronal intermediate filaments and ALS: a new look at an old question. Biochim Biophys Acta 2006; 1762:1001-12.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 1001-1012
    • Xiao, S.1    McLean, J.2    Robertson, J.3
  • 29
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in Huntington's disease
    • DOI 10.1016/S0140-6736(03)13304-1
    • Bates G. Huntingtin aggregation and toxicity in Huntington's disease. Lancet 2003; 361:1642-4. (Pubitemid 36579005)
    • (2003) Lancet , vol.361 , Issue.9369 , pp. 1642-1644
    • Bates, G.1
  • 30
    • 3242875557 scopus 로고    scopus 로고
    • Axonal mitochondrial transport and potential are correlated
    • Miller KE, Sheetz MP. Axonal mitochondrial transport and potential are correlated. J Cell Sci 2004; 117:2791-804.
    • (2004) J Cell Sci , vol.117 , pp. 2791-2804
    • Miller, K.E.1    Sheetz, M.P.2
  • 31
    • 75549089982 scopus 로고    scopus 로고
    • HDAC1 nuclear export induced by pathological conditions is essential for the onset of axonal damage
    • Kim JY, Shen S, Dietz K, He Y, Howell O, Reynolds R, Casaccia P. HDAC1 nuclear export induced by pathological conditions is essential for the onset of axonal damage. Nat Neurosci 13:180-9.
    • Nat Neurosci , vol.13 , pp. 180-189
    • Kim, J.Y.1    Shen, S.2    Dietz, K.3    He, Y.4    Howell, O.5    Reynolds, R.6    Casaccia, P.7
  • 32
    • 0035724044 scopus 로고    scopus 로고
    • Identification of a signal-responsive nuclear export sequence in class II histone deacetylases
    • McKinsey TA, Zhang CL, Olson EN. Identification of a signal-responsive nuclear export sequence in class II histone deacetylases. Mol Cell Biol 2001; 21:6312-21.
    • (2001) Mol Cell Biol , vol.21 , pp. 6312-6321
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 33
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen W, Meinkoth JL, Tsien RY, Taylor SS. Identification of a signal for rapid export of proteins from the nucleus. Cell 1995; 82:463-73.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 34
    • 61549116543 scopus 로고    scopus 로고
    • Histone deacetylases: Salesmen and customers in the post-translational modification market
    • Brandl A, Heinzel T, Kramer OH. Histone deacetylases: salesmen and customers in the post-translational modification market. Biol Cell 2009; 101:193-205.
    • (2009) Biol Cell , vol.101 , pp. 193-205
    • Brandl, A.1    Heinzel, T.2    Kramer, O.H.3
  • 35
    • 1542289920 scopus 로고    scopus 로고
    • Deactylase Inhibitors Disrupt Cellular Complexes Containing Protein Phosphatases and Deacetylases
    • DOI 10.1074/jbc.M310997200
    • Brush MH, Guardiola A, Connor JH, Yao TP, Shenolikar S. Deactylase inhibitors disrupt cellular complexes containing protein phosphatases and deacetylases. J Biol Chem 2004; 279:7685-91. (Pubitemid 38294650)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7685-7691
    • Brush, M.H.1    Guardiola, A.2    Connor, J.H.3    Yao, T.-P.4    Shenolikar, S.5
  • 36
    • 33744510851 scopus 로고    scopus 로고
    • HDAC1 acetylation is linked to progressive modulation of steroid receptor-induced gene transcription
    • Qiu Y, Zhao Y, Becker M, John S, Parekh BS, Huang S, et al. HDAC1 acetylation is linked to progressive modulation of steroid receptor-induced gene transcription. Mol Cell 2006; 22:669-79.
    • (2006) Mol Cell , vol.22 , pp. 669-679
    • Qiu, Y.1    Zhao, Y.2    Becker, M.3    John, S.4    Parekh, B.S.5    Huang, S.6
  • 37
    • 0037189568 scopus 로고    scopus 로고
    • SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
    • DOI 10.1074/jbc.M203690200
    • David G, Neptune MA, DePinho RA. SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities. J Biol Chem 2002; 277:23658-63. (Pubitemid 34952204)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23658-23663
    • David, G.1    Neptune, M.A.2    Depinho, R.A.3
  • 38
    • 0034523266 scopus 로고    scopus 로고
    • SUMO - Nonclassical ubiquitin
    • Melchior F. SUMO - nonclassical ubiquitin. Annu Rev Cell Dev Biol 2000; 16:591-626.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 591-626
    • Melchior, F.1
  • 39
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 2009; 325:834.
    • (2009) Science , vol.325 , pp. 834
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6
  • 40
    • 0033520325 scopus 로고    scopus 로고
    • Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase
    • DOI 10.1016/S0092-8674(00)80054-9
    • Chen H, Lin RJ, Xie W, Wilpitz D, Evans RM. Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell 1999; 98:675-86. (Pubitemid 29418958)
    • (1999) Cell , vol.98 , Issue.5 , pp. 675-686
    • Chen, H.1    Lin, R.J.2    Xie, W.3    Wilpitz, D.4    Evans, R.M.5
  • 41
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan R, Delphin C, Guan T, Gerace L, Melchior F. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 1997; 88:97-107. (Pubitemid 27180334)
    • (1997) Cell , vol.88 , Issue.1 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 42
    • 27644591304 scopus 로고    scopus 로고
    • Axon degeneration mechanisms: Commonality amid diversity
    • Coleman M. Axon degeneration mechanisms: commonality amid diversity. Nat Rev Neurosci 2005; 6:889-98.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 889-898
    • Coleman, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.