메뉴 건너뛰기




Volumn 110, Issue 12, 2013, Pages 4604-4609

HDAC6 mutations rescue human tau-induced microtubule defects in Drosophila

Author keywords

Disease model; Genetic study

Indexed keywords

HISTONE DEACETYLASE 6; TAU PROTEIN; TUBULIN;

EID: 84875241051     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1207586110     Document Type: Article
Times cited : (84)

References (50)
  • 2
    • 0022550260 scopus 로고
    • Defective brain microtubule assembly in Alzheimer's disease
    • Iqbal K, et al. (1986) Defective brain microtubule assembly in Alzheimer's disease. Lancet 2(8504):421-426.
    • (1986) Lancet , vol.2 , Issue.8504 , pp. 421-426
    • Iqbal, K.1
  • 3
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • Bramblett GT, et al. (1993) Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron 10(6):1089-1099.
    • (1993) Neuron , vol.10 , Issue.6 , pp. 1089-1099
    • Bramblett, G.T.1
  • 4
    • 0032484089 scopus 로고    scopus 로고
    • Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17
    • Hong M, et al. (1998) Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17. Science 282(5395):1914-1917.
    • (1998) Science , vol.282 , Issue.5395 , pp. 1914-1917
    • Hong, M.1
  • 5
    • 7944236911 scopus 로고    scopus 로고
    • The cytoskeleton in neurodegenerative diseases
    • Cairns NJ, Lee VM, Trojanowski JQ (2004) The cytoskeleton in neurodegenerative diseases. J Pathol 204(4):438-449.
    • (2004) J Pathol , vol.204 , Issue.4 , pp. 438-449
    • Cairns, N.J.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 6
    • 0035882526 scopus 로고    scopus 로고
    • Attenuated neurodegenerative disease phenotype in tau transgenic mouse lacking neurofilaments
    • Ishihara T, et al. (2001) Attenuated neurodegenerative disease phenotype in tau transgenic mouse lacking neurofilaments. J Neurosci 21(16):6026-6035.
    • (2001) J Neurosci , vol.21 , Issue.16 , pp. 6026-6035
    • Ishihara, T.1
  • 7
    • 0036138044 scopus 로고    scopus 로고
    • Neurodegeneration with tau accumulation in a transgenic mouse expressing V337M human tau
    • Tanemura K, et al. (2002) Neurodegeneration with tau accumulation in a transgenic mouse expressing V337M human tau. J Neurosci 22(1):133-141.
    • (2002) J Neurosci , vol.22 , Issue.1 , pp. 133-141
    • Tanemura, K.1
  • 8
    • 19944429064 scopus 로고    scopus 로고
    • Microtubule-binding drugs offset tau sequestration by stabilizing microtubules and reversing fast axonal transport deficits in a tauopathy model
    • Zhang B, et al. (2005) Microtubule-binding drugs offset tau sequestration by stabilizing microtubules and reversing fast axonal transport deficits in a tauopathy model. Proc Natl Acad Sci USA 102(1):227-231.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.1 , pp. 227-231
    • Zhang, B.1
  • 9
    • 77958065504 scopus 로고    scopus 로고
    • Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy
    • Brunden KR, et al. (2010) Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy. J Neurosci 30(41): 13861-13866.
    • (2010) J Neurosci , vol.30 , Issue.41 , pp. 13861-13866
    • Brunden, K.R.1
  • 10
    • 84863230105 scopus 로고    scopus 로고
    • The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice
    • Zhang B, et al. (2012) The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice. J Neurosci 32(11):3601-3611.
    • (2012) J Neurosci , vol.32 , Issue.11 , pp. 3601-3611
    • Zhang, B.1
  • 11
    • 70350716183 scopus 로고    scopus 로고
    • Optically resolving individual microtubules in live axons
    • Mudrakola HV, Zhang K, Cui B (2009) Optically resolving individual microtubules in live axons. Structure 17(11):1433-1441.
    • (2009) Structure , vol.17 , Issue.11 , pp. 1433-1441
    • Mudrakola, H.V.1    Zhang, K.2    Cui, B.3
  • 12
    • 67649202108 scopus 로고    scopus 로고
    • Drosophila tubulin-specific chaperone e functions at neuromuscular synapses and is required for microtubule network formation
    • Jin S, et al. (2009) Drosophila tubulin-specific chaperone E functions at neuromuscular synapses and is required for microtubule network formation. Development 136(9): 1571-1581.
    • (2009) Development , vol.136 , Issue.9 , pp. 1571-1581
    • Jin, S.1
  • 13
    • 79951533987 scopus 로고    scopus 로고
    • Drosophila FMRP regulates microtubule network formation and axonal transport of mitochondria
    • Yao A, et al. (2011) Drosophila FMRP regulates microtubule network formation and axonal transport of mitochondria. Hum Mol Genet 20(1):51-63.
    • (2011) Hum Mol Genet , vol.20 , Issue.1 , pp. 51-63
    • Yao, A.1
  • 15
    • 78649660787 scopus 로고    scopus 로고
    • Aggregation of detergent-insoluble tau is involved in neuronal loss but not in synaptic loss
    • Kimura T, et al. (2010) Aggregation of detergent-insoluble tau is involved in neuronal loss but not in synaptic loss. J Biol Chem 285(49):38692-38699.
    • (2010) J Biol Chem , vol.285 , Issue.49 , pp. 38692-38699
    • Kimura, T.1
  • 16
    • 77954208049 scopus 로고    scopus 로고
    • Drosophila histone deacetylase 6 protects dopaminergic neurons against alpha-synuclein toxicity by promoting inclusion formation
    • Du GP, et al. (2010) Drosophila histone deacetylase 6 protects dopaminergic neurons against alpha-synuclein toxicity by promoting inclusion formation. Mol Biol Cell 21(13):2128-2137.
    • (2010) Mol Biol Cell , vol.21 , Issue.13 , pp. 2128-2137
    • Du, G.P.1
  • 17
    • 33947307791 scopus 로고    scopus 로고
    • Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1
    • Thies E, Mandelkow EM (2007) Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1. J Neurosci 27(11): 2896-2907.
    • (2007) J Neurosci , vol.27 , Issue.11 , pp. 2896-2907
    • Thies, E.1    Mandelkow, E.M.2
  • 18
    • 2442477424 scopus 로고    scopus 로고
    • New synaptic bouton formation is disrupted by misregulation of microtubule stability in aPKC mutants
    • Ruiz-Canada C, et al. (2004) New synaptic bouton formation is disrupted by misregulation of microtubule stability in aPKC mutants. Neuron 42(4):567-580.
    • (2004) Neuron , vol.42 , Issue.4 , pp. 567-580
    • Ruiz-Canada, C.1
  • 19
    • 13944280702 scopus 로고    scopus 로고
    • Drosophila spastin regulates synaptic microtubule networks and is required for normal motor function
    • Sherwood NT, Sun Q, Xue M, Zhang B, Zinn K (2004) Drosophila spastin regulates synaptic microtubule networks and is required for normal motor function. PLoS Biol 2(12):e429.
    • (2004) PLoS Biol , vol.2 , Issue.12
    • Sherwood, N.T.1    Sun, Q.2    Xue, M.3    Zhang, B.4    Zinn, K.5
  • 20
    • 34047106848 scopus 로고    scopus 로고
    • Cytoskeleton proteins are modulators of mutant tau-induced neurodegeneration in Drosophila
    • Blard O, et al. (2007) Cytoskeleton proteins are modulators of mutant tau-induced neurodegeneration in Drosophila. Hum Mol Genet 16(5):555-566.
    • (2007) Hum Mol Genet , vol.16 , Issue.5 , pp. 555-566
    • Blard, O.1
  • 21
    • 27744600579 scopus 로고    scopus 로고
    • Over-expression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions
    • Chee FC, et al. (2005) Over-expression of tau results in defective synaptic transmission in Drosophila neuromuscular junctions. Neurobiol Dis 20(3):918-928.
    • (2005) Neurobiol Dis , vol.20 , Issue.3 , pp. 918-928
    • Chee, F.C.1
  • 22
    • 0037161744 scopus 로고    scopus 로고
    • HDAC6 is a microtubule-associated deacetylase
    • Hubbert C, et al. (2002) HDAC6 is a microtubule-associated deacetylase. Nature 417(6887):455-458.
    • (2002) Nature , vol.417 , Issue.6887 , pp. 455-458
    • Hubbert, C.1
  • 23
    • 12244295468 scopus 로고    scopus 로고
    • In vivo destabilization of dynamic microtubules by HDAC6- mediated deacetylation
    • Matsuyama A, et al. (2002) In vivo destabilization of dynamic microtubules by HDAC6- mediated deacetylation. EMBO J 21(24):6820-6831.
    • (2002) EMBO J , vol.21 , Issue.24 , pp. 6820-6831
    • Matsuyama, A.1
  • 24
    • 0030240325 scopus 로고    scopus 로고
    • Reduction of acetylated alpha-tubulin immunoreactivity in neurofibrillary tangle-bearing neurons in Alzheimer's disease
    • Hempen B, Brion JP (1996) Reduction of acetylated alpha-tubulin immunoreactivity in neurofibrillary tangle-bearing neurons in Alzheimer's disease. J Neuropathol Exp Neurol 55(9):964-972.
    • (1996) J Neuropathol Exp Neurol , vol.55 , Issue.9 , pp. 964-972
    • Hempen, B.1    Brion, J.P.2
  • 25
    • 49549083278 scopus 로고    scopus 로고
    • Histone deacetylase 6 interacts with the microtubule- associated protein tau
    • Ding H, Dolan PJ, Johnson GV (2008) Histone deacetylase 6 interacts with the microtubule- associated protein tau. J Neurochem 106(5):2119-2130.
    • (2008) J Neurochem , vol.106 , Issue.5 , pp. 2119-2130
    • Ding, H.1    Dolan, P.J.2    Johnson, G.V.3
  • 26
    • 0344640906 scopus 로고    scopus 로고
    • Domainselective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • Haggarty SJ, Koeller KM, Wong JC, Grozinger CM, Schreiber SL (2003) Domainselective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc Natl Acad Sci USA 100(8):4389-4394.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.8 , pp. 4389-4394
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Grozinger, C.M.4    Schreiber, S.L.5
  • 27
    • 80054881600 scopus 로고    scopus 로고
    • Class IIb HDAC6 regulates endothelial cell migration and angiogenesis by deacetylation of cortactin
    • Kaluza D, et al. (2011) Class IIb HDAC6 regulates endothelial cell migration and angiogenesis by deacetylation of cortactin. EMBO J 30(20):4142-4156.
    • (2011) EMBO J , vol.30 , Issue.20 , pp. 4142-4156
    • Kaluza, D.1
  • 28
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • Dompierre JP, et al. (2007) Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J Neurosci 27(13):3571-3583.
    • (2007) J Neurosci , vol.27 , Issue.13 , pp. 3571-3583
    • Dompierre, J.P.1
  • 29
    • 0346361872 scopus 로고    scopus 로고
    • Genetic modifiers of tauopathy in Drosophila
    • Shulman JM, Feany MB (2003) Genetic modifiers of tauopathy in Drosophila. Genetics 165(3):1233-1242.
    • (2003) Genetics , vol.165 , Issue.3 , pp. 1233-1242
    • Shulman, J.M.1    Feany, M.B.2
  • 30
    • 1542358895 scopus 로고    scopus 로고
    • PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila
    • Nishimura I, Yang Y, Lu B (2004) PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila. Cell 116(5): 671-682.
    • (2004) Cell , vol.116 , Issue.5 , pp. 671-682
    • Nishimura, I.1    Yang, Y.2    Lu, B.3
  • 31
    • 0032786370 scopus 로고    scopus 로고
    • Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein
    • Spittaels K, et al. (1999) Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein. Am J Pathol 155(6): 2153-2165.
    • (1999) Am J Pathol , vol.155 , Issue.6 , pp. 2153-2165
    • Spittaels, K.1
  • 32
    • 20044385920 scopus 로고    scopus 로고
    • Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease
    • Stokin GB, et al. (2005) Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease. Science 307(5713):1282-1288.
    • (2005) Science , vol.307 , Issue.5713 , pp. 1282-1288
    • Stokin, G.B.1
  • 33
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore C, Lee VM, Trojanowski JQ (2007) Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat Rev Neurosci 8(9):663-672.
    • (2007) Nat Rev Neurosci , vol.8 , Issue.9 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 34
    • 0033230886 scopus 로고    scopus 로고
    • Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform
    • Ishihara T, et al. (1999) Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform. Neuron 24(3): 751-762.
    • (1999) Neuron , vol.24 , Issue.3 , pp. 751-762
    • Ishihara, T.1
  • 35
    • 0242600546 scopus 로고    scopus 로고
    • Microtubule reduction in Alzheimer's disease and aging is independent of tau filament formation
    • Cash AD, et al. (2003) Microtubule reduction in Alzheimer's disease and aging is independent of tau filament formation. Am J Pathol 162(5):1623-1627.
    • (2003) Am J Pathol , vol.162 , Issue.5 , pp. 1623-1627
    • Cash, A.D.1
  • 36
    • 16244366803 scopus 로고    scopus 로고
    • Class II histone deacetylases: From sequence to function, regulation, and clinical implication
    • Yang XJ, Grégoire S (2005) Class II histone deacetylases: From sequence to function, regulation, and clinical implication. Mol Cell Biol 25(8):2873-2884.
    • (2005) Mol Cell Biol , vol.25 , Issue.8 , pp. 2873-2884
    • Yang, X.J.1    Grégoire, S.2
  • 38
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Kawaguchi Y, et al. (2003) The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115(6):727-738.
    • (2003) Cell , vol.115 , Issue.6 , pp. 727-738
    • Kawaguchi, Y.1
  • 39
    • 77649337122 scopus 로고    scopus 로고
    • HDAC6 controls autophagosome maturation essential for ubiquitin- selective quality-control autophagy
    • Lee JY, et al. (2010) HDAC6 controls autophagosome maturation essential for ubiquitin- selective quality-control autophagy. EMBO J 29(5):969-980.
    • (2010) EMBO J , vol.29 , Issue.5 , pp. 969-980
    • Lee, J.Y.1
  • 40
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata A, Riley BE, Johnston JA, Kopito RR (2005) HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem 280(48): 40282-40292.
    • (2005) J Biol Chem , vol.280 , Issue.48 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 41
    • 34548851476 scopus 로고    scopus 로고
    • Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6
    • Olzmann JA, et al. (2007) Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6. J Cell Biol 178(6):1025-1038.
    • (2007) J Cell Biol , vol.178 , Issue.6 , pp. 1025-1038
    • Olzmann, J.A.1
  • 42
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • Pandey UB, et al. (2007) HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature 447(7146):859-863.
    • (2007) Nature , vol.447 , Issue.7146 , pp. 859-863
    • Pandey, U.B.1
  • 43
    • 21144444486 scopus 로고    scopus 로고
    • HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor
    • Kovacs JJ, et al. (2005) HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Mol Cell 18(5):601-607.
    • (2005) Mol Cell , vol.18 , Issue.5 , pp. 601-607
    • Kovacs, J.J.1
  • 44
    • 84863508369 scopus 로고    scopus 로고
    • Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation
    • Cook C, et al. (2012) Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation. Hum Mol Gene 21(13):2936-2945.
    • (2012) Hum Mol Gene , vol.21 , Issue.13 , pp. 2936-2945
    • Cook, C.1
  • 45
    • 77953046399 scopus 로고    scopus 로고
    • Acetylation of microtubules influences their sensitivity to severing by katanin in neurons and fibroblasts
    • Sudo H, Baas PW (2010) Acetylation of microtubules influences their sensitivity to severing by katanin in neurons and fibroblasts. J Neurosci 30(21):7215-7226.
    • (2010) J Neurosci , vol.30 , Issue.21 , pp. 7215-7226
    • Sudo, H.1    Baas, P.W.2
  • 46
    • 5444273804 scopus 로고    scopus 로고
    • MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons
    • Mandelkow EM, Thies E, Trinczek B, Biernat J, Mandelkow E (2004) MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons. J Cell Biol 167(1): 99-110.
    • (2004) J Cell Biol , vol.167 , Issue.1 , pp. 99-110
    • Mandelkow, E.M.1    Thies, E.2    Trinczek, B.3    Biernat, J.4    Mandelkow, E.5
  • 47
    • 33750618516 scopus 로고    scopus 로고
    • Microtubule acetylation promotes kinesin-1 binding and transport
    • Reed NA, et al. (2006) Microtubule acetylation promotes kinesin-1 binding and transport. Curr Biol 16(21):2166-2172.
    • (2006) Curr Biol , vol.16 , Issue.21 , pp. 2166-2172
    • Reed, N.A.1
  • 48
    • 70450239488 scopus 로고    scopus 로고
    • Kinesin-1 regulates microtubule dynamics via a c-Jun N-terminal kinase-dependent mechanism
    • Daire V, et al. (2009) Kinesin-1 regulates microtubule dynamics via a c-Jun N-terminal kinase-dependent mechanism. J Biol Chem 284(46):31992-32001.
    • (2009) J Biol Chem , vol.284 , Issue.46 , pp. 31992-32001
    • Daire, V.1
  • 49
    • 40749161986 scopus 로고    scopus 로고
    • Mice lacking histone deacetylase 6 have hyperacetylated tubulin but are viable and develop normally
    • Zhang Y, et al. (2008) Mice lacking histone deacetylase 6 have hyperacetylated tubulin but are viable and develop normally. Mol Cell Biol 28(5):1688-1701.
    • (2008) Mol Cell Biol , vol.28 , Issue.5 , pp. 1688-1701
    • Zhang, Y.1
  • 50
    • 77955355838 scopus 로고    scopus 로고
    • Rational design and simple chemistry yield a superior, neuroprotective HDAC6 inhibitor, tubastatin A
    • Butler KV, et al. (2010) Rational design and simple chemistry yield a superior, neuroprotective HDAC6 inhibitor, tubastatin A. J Am Chem Soc 132(31):10842-10846.
    • (2010) J Am Chem Soc , vol.132 , Issue.31 , pp. 10842-10846
    • Butler, K.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.