메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

An acetylation switch controls TDP-43 function and aggregation propensity

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; HISTONE DEACETYLASE 6; LYSINE; TAR DNA BINDING PROTEIN; DNA BINDING PROTEIN; PRIMER DNA; RECOMBINANT PROTEIN; SMALL INTERFERING RNA; TDP-43 PROTEIN, HUMAN;

EID: 84941786176     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6845     Document Type: Article
Times cited : (221)

References (68)
  • 1
    • 80755153025 scopus 로고    scopus 로고
    • TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies
    • Cohen, T. J., Lee, V. M. &Trojanowski, J. Q. TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies. Trends Mol. Med. 17, 659-667 (2011).
    • (2011) Trends Mol. Med. , vol.17 , pp. 659-667
    • Cohen, T.J.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 2
    • 77649252528 scopus 로고    scopus 로고
    • Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
    • Pesiridis, G. S., Lee, V. M. & Trojanowski, J. Q. Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. Hum. Mol. Genet. 18, R156-R162 (2009).
    • (2009) Hum. Mol. Genet. , vol.18 , pp. R156-R162
    • Pesiridis, G.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 3
    • 77955784599 scopus 로고    scopus 로고
    • ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS
    • Ling, S. C. et al. ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS. Proc. Natl Acad. Sci. USA 107, 13318-13323 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 13318-13323
    • Ling, S.C.1
  • 4
    • 79953185674 scopus 로고    scopus 로고
    • Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
    • Polymenidou, M. et al. Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43. Nat. Neurosci. 14, 459-468 (2011).
    • (2011) Nat. Neurosci. , vol.14 , pp. 459-468
    • Polymenidou, M.1
  • 5
    • 79953180492 scopus 로고    scopus 로고
    • Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
    • Tollervey, J. R. et al. Characterizing the RNA targets and position-dependent splicing regulation by TDP-43. Nat. Neurosci. 14, 452-458 (2011).
    • (2011) Nat. Neurosci. , vol.14 , pp. 452-458
    • Tollervey, J.R.1
  • 6
    • 78651408754 scopus 로고    scopus 로고
    • Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexes
    • Sephton, C. F. et al. Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexes. J. Biol. Chem. 286, 1204-1215 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 1204-1215
    • Sephton, C.F.1
  • 7
    • 37549025044 scopus 로고    scopus 로고
    • A novel CpG-free vertebrate insulator silences the testis-specific SP-10 gene in somatic tissues: Role for TDP-43 in insulator function
    • Abhyankar, M. M., Urekar, C. & Reddi, P. P. A novel CpG-free vertebrate insulator silences the testis-specific SP-10 gene in somatic tissues: role for TDP-43 in insulator function. J. Biol. Chem. 282, 36143-36154 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 36143-36154
    • Abhyankar, M.M.1    Urekar, C.2    Reddi, P.P.3
  • 8
    • 33745277599 scopus 로고    scopus 로고
    • Cis-requirement for the maintenance of round spermatid-specific transcription
    • Acharya, K. K., Govind, C. K., Shore, A. N., Stoler, M. H. & Reddi, P. P. cis-requirement for the maintenance of round spermatid-specific transcription. Dev. Biol. 295, 781-790 (2006).
    • (2006) Dev. Biol. , vol.295 , pp. 781-790
    • Acharya, K.K.1    Govind, C.K.2    Shore, A.N.3    Stoler, M.H.4    Reddi, P.P.5
  • 9
    • 41649106307 scopus 로고    scopus 로고
    • TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression
    • Ayala, Y. M., Misteli, T. & Baralle, F. E. TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression. Proc. Natl Acad. Sci. USA 105, 3785-3789 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 3785-3789
    • Ayala, Y.M.1    Misteli, T.2    Baralle, F.E.3
  • 10
    • 42449163952 scopus 로고    scopus 로고
    • TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor
    • Wang, I. F., Wu, L. S., Chang, H. Y. & Shen, C. K. TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor. J. Neurochem. 105, 797-806 (2008).
    • (2008) J. Neurochem. , vol.105 , pp. 797-806
    • Wang, I.F.1    Wu, L.S.2    Chang, H.Y.3    Shen, C.K.4
  • 11
    • 84857997227 scopus 로고    scopus 로고
    • Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking
    • Cohen, T. J., Hwang, A. W., Unger, T., Trojanowski, J. Q. & Lee, V. M. Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking. EMBO J. 31, 1241-1252 (2012).
    • (2012) EMBO J. , vol.31 , pp. 1241-1252
    • Cohen, T.J.1    Hwang, A.W.2    Unger, T.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 12
    • 70350135049 scopus 로고    scopus 로고
    • TDP-43 is recruited to stress granules in conditions of oxidative insult
    • Colombrita, C. et al. TDP-43 is recruited to stress granules in conditions of oxidative insult. J. Neurochem. 111, 1051-1061 (2009).
    • (2009) J. Neurochem. , vol.111 , pp. 1051-1061
    • Colombrita, C.1
  • 13
    • 76149120427 scopus 로고    scopus 로고
    • Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery
    • Freibaum, B. D., Chitta, R. K., High, A. A. & Taylor, J. P. Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery. J. Proteome Res. 9, 1104-1120 (2010).
    • (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
  • 14
    • 84896298823 scopus 로고    scopus 로고
    • ALS-linked mutations enlarge TDP-43-enriched neuronal RNA granules in the dendritic arbor
    • Liu-Yesucevitz, L. et al. ALS-linked mutations enlarge TDP-43-enriched neuronal RNA granules in the dendritic arbor. J. Neurosci. 34, 4167-4174 (2014).
    • (2014) J. Neurosci. , vol.34 , pp. 4167-4174
    • Liu-Yesucevitz, L.1
  • 15
    • 37349039461 scopus 로고    scopus 로고
    • TDP-43 proteinopathies: Neurodegenerative protein misfolding diseases without amyloidosis
    • Kwong, L. K., Uryu, K., Trojanowski, J. Q. & Lee, V. M. TDP-43 proteinopathies: neurodegenerative protein misfolding diseases without amyloidosis. Neurosignals 16, 41-51 (2008).
    • (2008) Neurosignals , vol.16 , pp. 41-51
    • Kwong, L.K.1    Uryu, K.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 16
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann, M. et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314, 130-133 (2006).
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1
  • 17
    • 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, S. J. et al. 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).
    • (2010) J. Neurosci. , vol.30 , pp. 639-649
    • Barmada, S.J.1
  • 18
    • 77950360176 scopus 로고    scopus 로고
    • Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo
    • Kabashi, E. et al. Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo. Hum. Mol. Genet. 19, 671-683 (2009).
    • (2009) Hum. Mol. Genet. , vol.19 , pp. 671-683
    • Kabashi, E.1
  • 19
    • 79551523377 scopus 로고    scopus 로고
    • Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice
    • Igaz, L. M. et al. Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice. J. Clin. Invest. 121, 726-738 (2010).
    • (2010) J. Clin. Invest. , vol.121 , pp. 726-738
    • Igaz, L.M.1
  • 20
    • 77955395385 scopus 로고    scopus 로고
    • Elevated expression of TDP-43 in the forebrain of mice is sufficient to cause neurological and pathological phenotypes mimicking FTLD-U
    • Tsai, K. J. et al. Elevated expression of TDP-43 in the forebrain of mice is sufficient to cause neurological and pathological phenotypes mimicking FTLD-U. J. Exp. Med. 207, 1661-1673 (2010).
    • (2010) J. Exp. Med. , vol.207 , pp. 1661-1673
    • Tsai, K.J.1
  • 21
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska, I., Bell, S., Cairns, N. J., Miller, T. M. & Baloh, R. H. TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc. Natl Acad. Sci. USA 106, 18809-18814 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 22
    • 77649269011 scopus 로고    scopus 로고
    • TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration
    • Wils, H. et al. TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration. Proc. Natl Acad. Sci. USA 107, 3858-3863 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 3858-3863
    • Wils, H.1
  • 23
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton, M. J. et al. Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J. Biol. Chem. 283, 13302-13309 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 13302-13309
    • Winton, M.J.1
  • 24
    • 84893012138 scopus 로고    scopus 로고
    • TDP-43 Phosphorylation by casein kinase Iepsilon promotes oligomerization and enhances toxicity in vivo
    • Choksi, D. K. et al. TDP-43 Phosphorylation by casein kinase Iepsilon promotes oligomerization and enhances toxicity in vivo. Hum. Mol. Genet. 23, 1025-1035 (2014).
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 1025-1035
    • Choksi, D.K.1
  • 25
    • 47949086625 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Hasegawa, M. et al. Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann. Neurol. 64, 60-70 (2008).
    • (2008) Ann. Neurol. , vol.64 , pp. 60-70
    • Hasegawa, M.1
  • 26
    • 63349083295 scopus 로고    scopus 로고
    • Identification of casein kinase-1 phosphorylation sites on TDP-43
    • Kametani, F. et al. Identification of casein kinase-1 phosphorylation sites on TDP-43. Biochem. Biophys. Res. Commun. 382, 405-409 (2009).
    • (2009) Biochem. Biophys. Res. Commun. , vol.382 , pp. 405-409
    • Kametani, F.1
  • 27
    • 84883297079 scopus 로고    scopus 로고
    • CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration
    • Liachko, N. F. et al. CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration. Ann. Neurol. 74, 39-52 (2013).
    • (2013) Ann. Neurol. , vol.74 , pp. 39-52
    • Liachko, N.F.1
  • 28
    • 59249085091 scopus 로고    scopus 로고
    • Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies
    • Neumann, M. et al. Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies. Acta Neuropathol. 117, 137-149 (2009).
    • (2009) Acta Neuropathol. , vol.117 , pp. 137-149
    • Neumann, M.1
  • 29
    • 78650680776 scopus 로고    scopus 로고
    • Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1
    • Brady, O. A., Meng, P., Zheng, Y., Mao, Y. & Hu, F. Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1. J. Neurochem. 116, 248-259 (2011).
    • (2011) J. Neurochem. , vol.116 , pp. 248-259
    • Brady, O.A.1    Meng, P.2    Zheng, Y.3    Mao, Y.4    Hu, F.5
  • 30
    • 79961148135 scopus 로고    scopus 로고
    • Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
    • Li, H. Y., Yeh, P. A., Chiu, H. C., Tang, C. Y. & Tu, B. P. Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation. PLoS ONE 6, e23075 (2011).
    • (2011) PLoS ONE , vol.6
    • Li, H.Y.1    Yeh, P.A.2    Chiu, H.C.3    Tang, C.Y.4    Tu, B.P.5
  • 31
    • 79953087890 scopus 로고    scopus 로고
    • The acetylation of tau inhibits its function and promotes pathological tau aggregation
    • Cohen, T. J. et al. The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat. Commun. 2, 252 (2011).
    • (2011) Nat. Commun. , vol.2 , pp. 252
    • Cohen, T.J.1
  • 32
    • 84890357149 scopus 로고    scopus 로고
    • Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance
    • Cook, C. et al. Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance. Hum. Mol. Genet. 23, 104-116 (2014).
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 104-116
    • Cook, C.1
  • 33
    • 84880638106 scopus 로고    scopus 로고
    • Acetylated tau neuropathology in sporadic and hereditary tauopathies
    • Irwin, D. J. et al. Acetylated tau neuropathology in sporadic and hereditary tauopathies. Am. J. Pathol. 183, 344-351 (2013).
    • (2013) Am. J. Pathol. , vol.183 , pp. 344-351
    • Irwin, D.J.1
  • 34
    • 84857620173 scopus 로고    scopus 로고
    • Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies
    • Irwin, D. J. et al. Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies. Brain 135, 807-818 (2012).
    • (2012) Brain , vol.135 , pp. 807-818
    • Irwin, D.J.1
  • 35
    • 77957001697 scopus 로고    scopus 로고
    • Acetylation of tau inhibits its degradation and contributes to tauopathy
    • Min, S. W. et al. Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron 67, 953-966 (2010).
    • (2010) Neuron , vol.67 , pp. 953-966
    • Min, S.W.1
  • 36
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary, C. et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325, 834-840 (2009).
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1
  • 37
    • 84898987950 scopus 로고    scopus 로고
    • The crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids
    • Kuo, P. H., Chiang, C. H., Wang, Y. T., Doudeva, L. G. & Yuan, H. S. The crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids. Nucleic Acids Res. 42, 4712-4722 (2014).
    • (2014) Nucleic Acids Res. , vol.42 , pp. 4712-4722
    • Kuo, P.H.1    Chiang, C.H.2    Wang, Y.T.3    Doudeva, L.G.4    Yuan, H.S.5
  • 38
    • 64549100193 scopus 로고    scopus 로고
    • Structural insights into TDP-43 in nucleic-acid binding and domain interactions
    • Kuo, P. H., Doudeva, L. G., Wang, Y. T., Shen, C. K. & Yuan, H. S. Structural insights into TDP-43 in nucleic-acid binding and domain interactions. Nucleic Acids Res. 37, 1799-1808 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1799-1808
    • Kuo, P.H.1    Doudeva, L.G.2    Wang, Y.T.3    Shen, C.K.4    Yuan, H.S.5
  • 39
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • Buratti, E. & Baralle, F. E. Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J. Biol. Chem. 276, 36337-36343 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 40
    • 67649797399 scopus 로고    scopus 로고
    • Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 proteinopathies
    • Igaz, L. M. et al. Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 proteinopathies. J. Biol. Chem. 284, 8516-8524 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 8516-8524
    • Igaz, L.M.1
  • 41
    • 59549094064 scopus 로고    scopus 로고
    • Structural determinants of the cellular localization and shuttling of TDP-43
    • Ayala, Y. M. et al. Structural determinants of the cellular localization and shuttling of TDP-43. J. Cell Sci. 121, 3778-3785 (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 3778-3785
    • Ayala, Y.M.1
  • 42
    • 34249946466 scopus 로고    scopus 로고
    • Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations
    • Mackenzie, I. R. et al. Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Ann. Neurol. 61, 427-434 (2007).
    • (2007) Ann. Neurol. , vol.61 , pp. 427-434
    • Mackenzie, I.R.1
  • 43
    • 84883292041 scopus 로고    scopus 로고
    • Stages of pTDP-43 pathology in amyotrophic lateral sclerosis
    • Brettschneider, J. et al. Stages of pTDP-43 pathology in amyotrophic lateral sclerosis. Ann. Neurol. 74, 20-38 (2013).
    • (2013) Ann. Neurol. , vol.74 , pp. 20-38
    • Brettschneider, J.1
  • 44
    • 2442676753 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: A functional link with disease penetrance
    • Buratti, E., Brindisi, A., Pagani, F. & Baralle, F. E. Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: a functional link with disease penetrance. Am. J. Hum. Genet. 74, 1322-1325 (2004).
    • (2004) Am. J. Hum. Genet. , vol.74 , pp. 1322-1325
    • Buratti, E.1    Brindisi, A.2    Pagani, F.3    Baralle, F.E.4
  • 45
    • 0035794665 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
    • Buratti, E. et al. Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J. 20, 1774-1784 (2001).
    • (2001) EMBO J. , vol.20 , pp. 1774-1784
    • Buratti, E.1
  • 47
    • 84890134733 scopus 로고    scopus 로고
    • Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43
    • Lukavsky, P. J. et al. Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43. Nat. Struct. Mol. Biol. 20, 1443-1449 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1443-1449
    • Lukavsky, P.J.1
  • 48
    • 84863508369 scopus 로고    scopus 로고
    • Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation
    • Cook, C. et al. Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation. Hum. Mol. Genet. 21, 2936-2945 (2012).
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2936-2945
    • Cook, C.1
  • 49
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • Dompierre, J. P. et al. Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J. Neurosci. 27, 3571-3583 (2007).
    • (2007) J. Neurosci. , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1
  • 50
    • 84871946821 scopus 로고    scopus 로고
    • Reducing HDAC6 ameliorates cognitive deficits in a mouse model for Alzheimer's disease
    • Govindarajan, N. et al. Reducing HDAC6 ameliorates cognitive deficits in a mouse model for Alzheimer's disease. EMBO Mol. Med. 5, 52-63 (2013).
    • (2013) EMBO Mol. Med. , vol.5 , pp. 52-63
    • Govindarajan, N.1
  • 51
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Kawaguchi, Y. et al. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115, 727-738 (2003).
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1
  • 52
    • 77952326081 scopus 로고    scopus 로고
    • Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy
    • Lee, J. Y., Nagano, Y., Taylor, J. P., Lim, K. L. & Yao, T. P. Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy. J. Cell Biol. 189, 671-679 (2010).
    • (2010) J. Cell Biol. , vol.189 , pp. 671-679
    • Lee, J.Y.1    Nagano, Y.2    Taylor, J.P.3    Lim, K.L.4    Yao, T.P.5
  • 53
    • 79953311481 scopus 로고    scopus 로고
    • HDAC6 alpha-tubulin deacetylase: A potential therapeutic target in neurodegenerative diseases
    • Li, G., Jiang, H., Chang, M., Xie, H. & Hu, L. HDAC6 alpha-tubulin deacetylase: a potential therapeutic target in neurodegenerative diseases. J. Neurol. Sci. 304, 1-8 (2011).
    • (2011) J. Neurol. Sci. , vol.304 , pp. 1-8
    • Li, G.1    Jiang, H.2    Chang, M.3    Xie, H.4    Hu, L.5
  • 54
    • 82055164435 scopus 로고    scopus 로고
    • Accumulation of histone deacetylase 6, an aggresome-related protein, is specific to Lewy bodies and glial cytoplasmic inclusions
    • Miki, Y. et al. Accumulation of histone deacetylase 6, an aggresome-related protein, is specific to Lewy bodies and glial cytoplasmic inclusions. Neuropathology 31, 561-568 (2011).
    • (2011) Neuropathology , vol.31 , pp. 561-568
    • Miki, Y.1
  • 55
    • 84872410555 scopus 로고    scopus 로고
    • Brain expression level and activity of HDAC6 protein in neurodegenerative dementia
    • Odagiri, S. et al. Brain expression level and activity of HDAC6 protein in neurodegenerative dementia. Biochem. Biophys. Res. Commun. 430, 394-399 (2013).
    • (2013) Biochem. Biophys. Res. Commun. , vol.430 , pp. 394-399
    • Odagiri, S.1
  • 56
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • Pandey, U. B. et al. HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature 447, 859-863 (2007).
    • (2007) Nature , vol.447 , pp. 859-863
    • Pandey, U.B.1
  • 57
    • 84873376098 scopus 로고    scopus 로고
    • Evaluation of histone deacetylases as drug targets in Huntington's disease models. Study of HDACs in brain tissues from R6/2 and CAG140 knock-in HD mouse models and human patients and in a neuronal HD cell model
    • Quinti, L. et al. Evaluation of histone deacetylases as drug targets in Huntington's disease models. Study of HDACs in brain tissues from R6/2 and CAG140 knock-in HD mouse models and human patients and in a neuronal HD cell model. PLoS Curr. 2 (2010).
    • (2010) PLoS Curr. , vol.2
    • Quinti, L.1
  • 58
    • 84873615689 scopus 로고    scopus 로고
    • Parkin ubiquitinates Tar-DNA binding protein-43 (TDP-43) and promotes its cytosolic accumulation via interaction with histone deacetylase 6 (HDAC6)
    • Hebron, M. L. et al. Parkin ubiquitinates Tar-DNA binding protein-43 (TDP-43) and promotes its cytosolic accumulation via interaction with histone deacetylase 6 (HDAC6). J. Biol. Chem. 288, 4103-4115 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 4103-4115
    • Hebron, M.L.1
  • 59
    • 33847369469 scopus 로고    scopus 로고
    • The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins
    • Dickey, C. A. et al. The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. J. Clin. Invest. 117, 648-658 (2007).
    • (2007) J. Clin. Invest. , vol.117 , pp. 648-658
    • Dickey, C.A.1
  • 60
    • 11144356089 scopus 로고    scopus 로고
    • CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
    • Petrucelli, L. et al. CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. Hum. Mol. Genet. 13, 703-714 (2004).
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 703-714
    • Petrucelli, L.1
  • 61
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation targets mutant huntingtin to autophagosomes for degradation
    • Jeong, H. et al. Acetylation targets mutant huntingtin to autophagosomes for degradation. Cell 137, 60-72 (2009).
    • (2009) Cell , vol.137 , pp. 60-72
    • Jeong, H.1
  • 62
    • 84878476630 scopus 로고    scopus 로고
    • Inhibition of TDP-43 aggregation by nucleic acid binding
    • Huang, Y. C. et al. Inhibition of TDP-43 aggregation by nucleic acid binding. PLoS ONE 8, e64002 (2013).
    • (2013) PLoS ONE , vol.8
    • Huang, Y.C.1
  • 63
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Johnson, B. S. et al. TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J. Biol. Chem. 284, 20329-20339 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 20329-20339
    • Johnson, B.S.1
  • 64
    • 84884777626 scopus 로고    scopus 로고
    • Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders
    • Janssens, J. & Van Broeckhoven, C. Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders. Hum. Mol. Genet. 22, R77-R87 (2013).
    • (2013) Hum. Mol. Genet. , vol.22 , pp. R77-R87
    • Janssens, J.1    Van Broeckhoven, C.2
  • 65
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: Emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne, C., Polymenidou, M. & Cleveland, D. W. TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum. Mol. Genet. 19, R46-R64 (2010).
    • (2010) Hum. Mol. Genet. , vol.19 , pp. R46-R64
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 66
    • 84874531814 scopus 로고    scopus 로고
    • RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations
    • Daigle, J. G. et al. RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations. Hum. Mol. Genet. 22, 1193-1205 (2013).
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 1193-1205
    • Daigle, J.G.1
  • 67
    • 27944508215 scopus 로고    scopus 로고
    • CLIP: A method for identifying protein-RNA interaction sites in living cells
    • Ule, J., Jensen, K., Mele, A. & Darnell, R. B. CLIP: a method for identifying protein-RNA interaction sites in living cells. Methods 37, 376-386 (2005).
    • (2005) Methods , vol.37 , pp. 376-386
    • Ule, J.1    Jensen, K.2    Mele, A.3    Darnell, R.B.4
  • 68
    • 1642576077 scopus 로고    scopus 로고
    • Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity
    • Nikolay, R. et al. Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity. J. Biol. Chem. 279, 2673-2678 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 2673-2678
    • Nikolay, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.