메뉴 건너뛰기




Volumn 33, Issue SUPPL. 1, 2013, Pages

Tau triage decisions mediated by the chaperone network

Author keywords

Alzheimer's disease; chaperone; CHIP; Hsp70; Hsp90; tau

Indexed keywords

AMYLOID BETA PROTEIN; CASPASE 3; CHAPERONE; CYCLIN DEPENDENT KINASE 5; GELDANAMYCIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 90; HEAT SHOCK TRANSCRIPTION FACTOR 1; HISTONE DEACETYLASE 6; MESSENGER RNA; POLYUBIQUITIN; TAU PROTEIN;

EID: 84872526813     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-2012-129008     Document Type: Review
Times cited : (9)

References (46)
  • 1
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H, Braak E (1991) Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 82, 239-259
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 7
    • 33746724745 scopus 로고    scopus 로고
    • Modulation of Hsp90 function in neurodegenerative disorders: Amolecular-Targeted therapy against disease-causing protein
    • Waza M, Adachi H, Katsuno M, Minamiyama M, Tanaka F, Doyu M, Sobue G (2006) Modulation of Hsp90 function in neurodegenerative disorders: Amolecular-Targeted therapy against disease-causing protein. J Mol Med (Berl) 84, 635-646
    • (2006) J Mol Med (Berl , vol.84 , pp. 635-646
    • Waza, M.1    Adachi, H.2    Katsuno, M.3    Minamiyama, M.4    Tanaka, F.5    Doyu, M.6    Sobue, G.7
  • 9
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura H, Schwartz D, Gygi SP, Kosik KS (2004) CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J Biol Chem 279, 4869-4876
    • (2004) J Biol Chem , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 13
    • 33744950091 scopus 로고    scopus 로고
    • Alzheimer disease-Specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation
    • Cripps D, Thomas SN, Jeng Y, Yang F, Davies P, Yang AJ (2006) Alzheimer disease-Specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation. J Biol Chem 281, 10825-10838
    • (2006) J Biol Chem , vol.281 , pp. 10825-10838
    • Cripps, D.1    Thomas, S.N.2    Jeng, Y.3    Yang, F.4    Davies, P.5    Yang, A.J.6
  • 14
    • 0027193036 scopus 로고
    • Ubiquitin is conjugated with aminoterminally processed tau in paired helical filaments
    • Morishima-KawashimaM, Hasegawa M, Takio K, Suzuki M, Titani K, Ihara Y (1993) Ubiquitin is conjugated with aminoterminally processed tau in paired helical filaments. Neuron 10, 1151-1160
    • (1993) Neuron , vol.10 , pp. 1151-1160
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 15
    • 0031013723 scopus 로고    scopus 로고
    • In vivo analysis of the Hsp90 cochaperone Sti1 (p60
    • Chang HC, Nathan DF, Lindquist S (1997) In vivo analysis of the Hsp90 cochaperone Sti1 (p60). Mol Cell Biol 17, 318-325
    • (1997) Mol Cell Biol , vol.17 , pp. 318-325
    • Chang, H.C.1    Nathan, D.F.2    Lindquist, S.3
  • 16
    • 0032567434 scopus 로고    scopus 로고
    • Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
    • Chen S, Smith DF (1998) Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery. J Biol Chem 273, 35194-35200
    • (1998) J Biol Chem , vol.273 , pp. 35194-35200
    • Chen, S.1    Smith, D.F.2
  • 17
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman J, Hohfeld J (1997) Chaperones get in touch: The Hip-Hop connection. Trends Biochem Sci 22, 87-92
    • (1997) Trends Biochem Sci , vol.22 , pp. 87-92
    • Frydman, J.1    Hohfeld, J.2
  • 18
    • 0032488906 scopus 로고    scopus 로고
    • Hop modulates Hsp70/Hsp90 interactions in protein folding
    • Johnson BD, Schumacher RJ, Ross ED, Toft DO (1998) Hop modulates Hsp70/Hsp90 interactions in protein folding. J Biol Chem 273, 3679-3686
    • (1998) J Biol Chem , vol.273 , pp. 3679-3686
    • Johnson, B.D.1    Schumacher, R.J.2    Ross, E.D.3    Toft, D.O.4
  • 22
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-Sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R (1998) Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-Sensitive complex with HSF1. Cell 94, 471-480
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 24
    • 0034282067 scopus 로고    scopus 로고
    • Conformational change as one of the earliest alterations of tau in Alzheimer's disease
    • Weaver CL, Espinoza M, Kress Y, Davies P (2000) Conformational change as one of the earliest alterations of tau in Alzheimer's disease. Neurobiol Aging 21, 719-727
    • (2000) Neurobiol Aging , vol.21 , pp. 719-727
    • Weaver, C.L.1    Espinoza, M.2    Kress, Y.3    Davies, P.4
  • 31
    • 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, 671-682
    • (2004) Cell , vol.116 , pp. 671-682
    • Nishimura, I.1    Yang, Y.2    Lu, B.3
  • 34
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali P, Pranpat M, Bradner J, Balasis M, Fiskus W, Guo F, Rocha K, Kumaraswamy S, Boyapalle S, Atadja P, Seto E, Bhalla K (2005) Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors. J Biol Chem 280, 26729-26734
    • (2005) J Biol Chem , vol.280 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3    Balasis, M.4    Fiskus, W.5    Guo, F.6    Rocha, K.7    Kumaraswamy, S.8    Boyapalle, S.9    Atadja, P.10    Seto, E.11    Bhalla, K.12
  • 36
    • 26644473193 scopus 로고    scopus 로고
    • Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone
    • Murphy PJ, MorishimaY,Kovacs JJ,Yao TP, PrattWB(2005) Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/ deacetylation of the chaperone. J Biol Chem 280, 33792-33799
    • (2005) J Biol Chem , vol.280 , pp. 33792-33799
    • Murphy, P.J.1    Morishima, Y.2    Kovacs, J.J.3    Yao, T.P.4    Pratt, W.B.5
  • 39
    • 49649108912 scopus 로고    scopus 로고
    • Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion
    • Yang Y, Rao R, Shen J, Tang Y, FiskusW, Nechtman J, Atadja P, Bhalla K (2008) Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion. Cancer Res 68, 4833-4842
    • (2008) Cancer Res , vol.68 , pp. 4833-4842
    • Yang, Y.1    Rao, R.2    Shen, J.3    Tang, Y.4    FiskusW Nechtman, J.5    Atadja, P.6    Bhalla, K.7
  • 40
    • 20844444898 scopus 로고    scopus 로고
    • Combination of the histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3
    • George P, Bali P, Annavarapu S, Scuto A, Fiskus W, Guo F, Sigua C, Sondarva G,Moscinski L, Atadja P, Bhalla K (2005) Combination of the histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3. Blood 105, 1768-1776
    • (2005) Blood , vol.105 , pp. 1768-1776
    • George, P.1    Bali, P.2    Annavarapu, S.3    Scuto, A.4    Fiskus, W.5    Guo, F.6    Sigua, C.7    Sondarva, G.8    Moscinski, L.9    Atadja, P.10    Bhalla, K.11
  • 44
    • 3242739968 scopus 로고    scopus 로고
    • O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
    • Liu F, Iqbal K, Grundke-Iqbal I, Hart GW, Gong CX (2004) O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease. Proc Natl Acad Sci U S A 101, 10804-10809
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10804-10809
    • Liu, F.1    Iqbal, K.2    Grundke-Iqbal, I.3    Hart, G.W.4    Gong, C.X.5
  • 46
    • 84857035370 scopus 로고    scopus 로고
    • Dual modification of Alzheimer's disease PHF-Tau protein by lysine methylation and ubiquitylation: A mass spectrometry approach
    • Thomas SN, Funk KE, Wan Y, Liao Z, Davies P, Kuret J, Yang AJ (2012) Dual modification of Alzheimer's disease PHF-Tau protein by lysine methylation and ubiquitylation: A mass spectrometry approach. Acta Neuropathol 123, 105-117
    • (2012) Acta Neuropathol , vol.123 , pp. 105-117
    • Thomas, S.N.1    Funk, K.E.2    Wan, Y.3    Liao, Z.4    Davies, P.5    Kuret, J.6    Yang, A.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.