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Volumn 21, Issue 24, 2012, Pages 5254-5267

NUB1 modulation of GSK3β reduces tau aggregation

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOGEN SYNTHASE KINASE 3BETA; NEDD8 ULTIMATE BUSTER 1; PROTEASOME; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 84870320500     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/dds376     Document Type: Article
Times cited : (28)

References (46)
  • 1
    • 19744382953 scopus 로고    scopus 로고
    • The MAP2/Tau family of microtubule-associated proteins
    • Dehmelt, L. and Halpain, S. (2005) The MAP2/Tau family of microtubule-associated proteins. Genome. Biol., 6, 204.
    • (2005) Genome. Biol. , vol.6 , pp. 204
    • Dehmelt, L.1    Halpain, S.2
  • 4
    • 79952105548 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein: implications for Alzheimer's disease
    • Martin, L., Latypova, X. and Terro, F. (2011) Post-translational modifications of tau protein: implications for Alzheimer's disease. Neurochem. Int., 58, 458-471.
    • (2011) Neurochem. Int. , vol.58 , pp. 458-471
    • Martin, L.1    Latypova, X.2    Terro, F.3
  • 5
    • 0142139311 scopus 로고    scopus 로고
    • Tau protein in familial and sporadic diseases
    • Yancopoulou, D. and Spillantini, M.G. (2003) Tau protein in familial and sporadic diseases. Neuromolecular Med., 4, 37-48.
    • (2003) Neuromolecular Med , vol.4 , pp. 37-48
    • Yancopoulou, D.1    Spillantini, M.G.2
  • 7
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
    • Hanger, D.P., Anderton, B.H. and Noble, W. (2009) Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol. Med., 15, 112-119.
    • (2009) Trends Mol. Med. , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 8
    • 39849110726 scopus 로고    scopus 로고
    • The GSK3 hypothesis of Alzheimer's disease
    • Hooper, C., Killick, R. and Lovestone, S. (2008) The GSK3 hypothesis of Alzheimer's disease. J. Neurochem., 104, 1433-1439.
    • (2008) J. Neurochem. , vol.104 , pp. 1433-1439
    • Hooper, C.1    Killick, R.2    Lovestone, S.3
  • 11
    • 36348935683 scopus 로고    scopus 로고
    • Soluble Abeta inhibits specific signal transduction cascades common to the insulin receptor pathway
    • Townsend, M., Mehta, T. and Selkoe, D.J. (2007) Soluble Abeta inhibits specific signal transduction cascades common to the insulin receptor pathway. J. Biol. Chem., 282, 33305-33312.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33305-33312
    • Townsend, M.1    Mehta, T.2    Selkoe, D.J.3
  • 13
    • 0030044463 scopus 로고    scopus 로고
    • Exposure of rat hippocampal neurons to amyloid beta peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3 beta
    • Takashima, A., Noguchi, K., Michel, G., Mercken, M., Hoshi, M., Ishiguro, K. and Imahori, K. (1996) Exposure of rat hippocampal neurons to amyloid beta peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3 beta. Neurosci. Lett., 203, 33-36.
    • (1996) Neurosci. Lett. , vol.203 , pp. 33-36
    • Takashima, A.1    Noguchi, K.2    Michel, G.3    Mercken, M.4    Hoshi, M.5    Ishiguro, K.6    Imahori, K.7
  • 15
    • 84857429142 scopus 로고    scopus 로고
    • GSK-3 inhibitors: preclinical and clinical focus on CNS
    • Eldar-Finkelman, H. and Martinez, A. (2011) GSK-3 inhibitors: preclinical and clinical focus on CNS. Front Mol. Neurosci., 4, 32.
    • (2011) Front Mol. Neurosci. , vol.4 , pp. 32
    • Eldar-Finkelman, H.1    Martinez, A.2
  • 16
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice
    • Lucas, J.J., Hernandez, F., Gomez-Ramos, P., Moran, M.A., Hen, R. and Avila, J. (2001) Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. EMBO J., 20, 27-39.
    • (2001) EMBO J , vol.20 , pp. 27-39
    • Lucas, J.J.1    Hernandez, F.2    Gomez-Ramos, P.3    Moran, M.A.4    Hen, R.5    Avila, J.6
  • 17
    • 12344323961 scopus 로고    scopus 로고
    • Tau phosphorylation in neuronal cell function and dysfunction
    • Johnson, G.V. and Stoothoff, W.H. (2004) Tau phosphorylation in neuronal cell function and dysfunction. J. Cell Sci., 117, 5721-5729.
    • (2004) J. Cell Sci. , vol.117 , pp. 5721-5729
    • Johnson, G.V.1    Stoothoff, W.H.2
  • 18
    • 49349110485 scopus 로고    scopus 로고
    • Pre-assembled tau filaments phosphorylated by GSK-3b form large tangle-like structures
    • Rankin, C.A., Sun, Q. and Gamblin, T.C. (2008) Pre-assembled tau filaments phosphorylated by GSK-3b form large tangle-like structures. Neurobiol. Dis., 31, 368-377.
    • (2008) Neurobiol. Dis. , vol.31 , pp. 368-377
    • Rankin, C.A.1    Sun, Q.2    Gamblin, T.C.3
  • 20
    • 34250818767 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation but not A beta or working memory deficits in a transgenic model with both plaques and tangles
    • Caccamo, A., Oddo, S., Tran, L.X. and LaFerla, F.M. (2007) Lithium reduces tau phosphorylation but not A beta or working memory deficits in a transgenic model with both plaques and tangles. Am. J. Pathol., 170, 1669-1675.
    • (2007) Am. J. Pathol. , vol.170 , pp. 1669-1675
    • Caccamo, A.1    Oddo, S.2    Tran, L.X.3    LaFerla, F.M.4
  • 21
    • 42349089604 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in Alzheimer's disease
    • Oddo, S. (2008) The ubiquitin-proteasome system in Alzheimer's disease. J. Cell Mol. Med., 12, 363-373.
    • (2008) J. Cell Mol. Med. , vol.12 , pp. 363-373
    • Oddo, S.1
  • 22
    • 0037312293 scopus 로고    scopus 로고
    • NEDD8 protein is involved in ubiquitinated inclusion bodies
    • Dil Kuazi, A., Kito, K., Abe, Y., Shin, R.W., Kamitani, T. and Ueda, N. (2003) NEDD8 protein is involved in ubiquitinated inclusion bodies. J. Pathol., 199, 259-266.
    • (2003) J. Pathol. , vol.199 , pp. 259-266
    • Dil Kuazi, A.1    Kito, K.2    Abe, Y.3    Shin, R.W.4    Kamitani, T.5    Ueda, N.6
  • 23
    • 70349339322 scopus 로고    scopus 로고
    • Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization
    • Merlet, J., Burger, J., Gomes, J.E. and Pintard, L. (2009) Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization. Cell. Mol. Life Sci., 66, 1924-1938.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1924-1938
    • Merlet, J.1    Burger, J.2    Gomes, J.E.3    Pintard, L.4
  • 24
    • 0035824559 scopus 로고    scopus 로고
    • Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1
    • Kamitani, T., Kito, K., Fukuda-Kamitani, T. and Yeh, E.T. (2001) Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1. J. Biol. Chem., 276, 46655-46660.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46655-46660
    • Kamitani, T.1    Kito, K.2    Fukuda-Kamitani, T.3    Yeh, E.T.4
  • 25
    • 1342300578 scopus 로고    scopus 로고
    • Integral UBL domain proteins: a family of proteasome interacting proteins
    • Hartmann-Petersen, R. and Gordon, C. (2004) Integral UBL domain proteins: a family of proteasome interacting proteins. Semin. Cell Dev. Biol., 15, 247-259.
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 247-259
    • Hartmann-Petersen, R.1    Gordon, C.2
  • 26
    • 84859175458 scopus 로고    scopus 로고
    • FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis
    • Rani, N., Aichem, A., Schmidtke, G., Kreft, S.G. and Groettrup, M. (2012) FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis. Nat. Commun., 3, 749.
    • (2012) Nat. Commun. , vol.3 , pp. 749
    • Rani, N.1    Aichem, A.2    Schmidtke, G.3    Kreft, S.G.4    Groettrup, M.5
  • 27
    • 0041856380 scopus 로고    scopus 로고
    • Regulation of the NEDD8 conjugation system by a splicing variant
    • Tanaka, T., Kawashima, H., Yeh, E.T. and Kamitani, T. (2003) Regulation of the NEDD8 conjugation system by a splicing variant, NUB1L. J. Biol. Chem., 278, 32905-32913.
    • (2003) NUB1L. J. Biol. Chem. , vol.278 , pp. 32905-32913
    • Tanaka, T.1    Kawashima, H.2    Yeh, E.T.3    Kamitani, T.4
  • 28
    • 33746023341 scopus 로고    scopus 로고
    • The UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10
    • Schmidtke, G., Kalveram, B., Weber, E., Bochtler, P., Lukasiak, S., Hipp, M.S. and Groettrup, M. (2006) The UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10. J. Biol. Chem., 281, 20045-20054.
    • (2006) J. Biol. Chem. , vol.281 , pp. 20045-20054
    • Schmidtke, G.1    Kalveram, B.2    Weber, E.3    Bochtler, P.4    Lukasiak, S.5    Hipp, M.S.6    Groettrup, M.7
  • 30
    • 33746644725 scopus 로고    scopus 로고
    • NUB1 suppresses the formation of Lewy body-like inclusions by proteasomal degradation of synphilin-1
    • Tanji, K., Tanaka, T., Mori, F., Kito, K., Takahashi, H., Wakabayashi, K. and Kamitani, T. (2006) NUB1 suppresses the formation of Lewy body-like inclusions by proteasomal degradation of synphilin-1. Am. J. Pathol., 169, 553-565.
    • (2006) Am. J. Pathol. , vol.169 , pp. 553-565
    • Tanji, K.1    Tanaka, T.2    Mori, F.3    Kito, K.4    Takahashi, H.5    Wakabayashi, K.6    Kamitani, T.7
  • 31
    • 80053343424 scopus 로고    scopus 로고
    • Synphilin-1-binding protein NUB1 is colocalized with nonfibrillar, proteinase K-resistant a-synuclein in presynapses in Lewy body disease
    • Tanji, K., Mori, F., Kito, K., Kakita, A., Mimura, J., Itoh, K., Takahashi, H., Kamitani, T. and Wakabayashi, K.J. (2011) Synphilin-1-binding protein NUB1 is colocalized with nonfibrillar, proteinase K-resistant a-synuclein in presynapses in Lewy body disease. J Neuropathol. Exp. Neurol., 70, 879-889.
    • (2011) J Neuropathol. Exp. Neurol. , vol.70 , pp. 879-889
    • Tanji, K.1    Mori, F.2    Kito, K.3    Kakita, A.4    Mimura, J.5    Itoh, K.6    Takahashi, H.7    Kamitani, T.8    Wakabayashi, K.J.9
  • 32
    • 77951073143 scopus 로고    scopus 로고
    • NUB1 promotes cytoplasmic localization of p53 through cooperation of the NEDD8 and ubiquitin pathways
    • Liu, G. and Xirodimas, D.P. (2010) NUB1 promotes cytoplasmic localization of p53 through cooperation of the NEDD8 and ubiquitin pathways. Oncogene, 29, 2252-2261.
    • (2010) Oncogene , vol.29 , pp. 2252-2261
    • Liu, G.1    Xirodimas, D.P.2
  • 33
    • 27844470590 scopus 로고    scopus 로고
    • Molecular motors implicated in the axonal transport of tau and alpha-synuclein
    • Utton, M.A., Noble, W.J., Hill, J.E., Anderton, B.H. and Hanger, D.P. (2005) Molecular motors implicated in the axonal transport of tau and alpha-synuclein. J. Cell Sci., 118, 4645-4654.
    • (2005) J. Cell Sci. , vol.118 , pp. 4645-4654
    • Utton, M.A.1    Noble, W.J.2    Hill, J.E.3    Anderton, B.H.4    Hanger, D.P.5
  • 34
    • 36448995426 scopus 로고    scopus 로고
    • Split GFP complementation assay: a novel approach to quantitatively measure aggregation of tau in situ: effects of GSK3b activation and caspase 3 cleavage
    • Chun, W., Waldo, G.S. and Johnson, G.V.W. (2007) Split GFP complementation assay: a novel approach to quantitatively measure aggregation of tau in situ: effects of GSK3b activation and caspase 3 cleavage. J. Neurochem., 103, 2529-2539.
    • (2007) J. Neurochem. , vol.103 , pp. 2529-2539
    • Chun, W.1    Waldo, G.S.2    Johnson, G.V.W.3
  • 35
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte, S. and Cordelieres, F.P. (2006) A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc., 224, 213-232.
    • (2006) J. Microsc. , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelieres, F.P.2
  • 36
    • 6344272892 scopus 로고    scopus 로고
    • Distinct patterns of tau-dependent process formation in mammalian cell lines
    • Bruijn, L.I., Krishnamurthy, P.K. and Gallo, J.M. (2004) Distinct patterns of tau-dependent process formation in mammalian cell lines. Neuroreport, 15, 2223-2226.
    • (2004) Neuroreport , vol.15 , pp. 2223-2226
    • Bruijn, L.I.1    Krishnamurthy, P.K.2    Gallo, J.M.3
  • 37
    • 0029013727 scopus 로고
    • Staging of Alzheimer's disease-related neurofibrillary changes
    • Braak, H. and Braak, E. (1995) Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol. Aging, 16, 271-278.
    • (1995) Neurobiol. Aging , vol.16 , pp. 271-278
    • Braak, H.1    Braak, E.2
  • 38
    • 79960626322 scopus 로고    scopus 로고
    • Axonal varicosity density as an index of local neuronal interactions
    • Zhang, Z-W., Kang, J.I. and Vaucher, E. (2011) Axonal varicosity density as an index of local neuronal interactions. PLoS ONE., 6, e22543.
    • (2011) PLoS ONE , vol.6
    • Zhang, Z.-W.1    Kang, J.I.2    Vaucher, E.3
  • 39
    • 0028989895 scopus 로고
    • Neurons bearing neurofibrillary tangles are responsible for selected synaptic deficits in Alzheimer's disease
    • Callahan, L.M. and Coleman, P.D. (1995) Neurons bearing neurofibrillary tangles are responsible for selected synaptic deficits in Alzheimer's disease. Neurobiol. Aging, 16, 311-314.
    • (1995) Neurobiol. Aging , vol.16 , pp. 311-314
    • Callahan, L.M.1    Coleman, P.D.2
  • 41
    • 59349096934 scopus 로고    scopus 로고
    • The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition
    • Kalveram, B., Schmidtke, G. and Groettrup, M. (2008) The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition. J. Cell Sci., 121, 4079-4088.
    • (2008) J. Cell Sci. , vol.121 , pp. 4079-4088
    • Kalveram, B.1    Schmidtke, G.2    Groettrup, M.3
  • 42
    • 9144244348 scopus 로고    scopus 로고
    • The Leber congenital amaurosis protein AIPL1 modulates the nuclear translocation of NUB1 and suppresses inclusion formation by NUB1 fragments
    • van der Spuy, J. and Cheetham, M.E. (2004) The Leber congenital amaurosis protein AIPL1 modulates the nuclear translocation of NUB1 and suppresses inclusion formation by NUB1 fragments. J. Biol. Chem., 279, 48038-48047.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48038-48047
    • van der Spuy, J.1    Cheetham, M.E.2
  • 43
    • 0028675873 scopus 로고
    • Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells
    • Lovestone, S., Reynolds, C.H., Latimer, D., Davis, D.R., Anderton, B.H., Gallo, J.M., Hanger, D., Mulot, S., Marquardt, B. and Stabel, S. (1994) Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells. Curr. Biol., 4, 1077-1086.
    • (1994) Curr. Biol. , vol.4 , pp. 1077-1086
    • Lovestone, S.1    Reynolds, C.H.2    Latimer, D.3    Davis, D.R.4    Anderton, B.H.5    Gallo, J.M.6    Hanger, D.7    Mulot, S.8    Marquardt, B.9    Stabel, S.10
  • 44
  • 45
    • 34248353520 scopus 로고    scopus 로고
    • Tumor suppressor PTEN affects tau phosphorylation: deficiency in the phosphatase activity of PTEN increases aggregation of an FTDP-17 mutant tau
    • Zhang, X., Zhang, Y., Liu, S., Bulloj, A., Tong, G.G., Zhang, Z., Liao, F-F. and Xu, H. (2006) Tumor suppressor PTEN affects tau phosphorylation: deficiency in the phosphatase activity of PTEN increases aggregation of an FTDP-17 mutant tau. Mol. Neurodegen., 1, 7.
    • (2006) Mol. Neurodegen. , vol.1 , pp. 7
    • Zhang, X.1    Zhang, Y.2    Liu, S.3    Bulloj, A.4    Tong, G.G.5    Zhang, Z.6    Liao, F.-F.7    Xu, H.8
  • 46
    • 77952531435 scopus 로고    scopus 로고
    • The retinitis pigmentosa protein RP2 links pericentriolar vesicle transport between the Golgi and the primary cilium
    • Evans, R.J., Schwarz, N., Nagel-Wolfrum, K., Wolfrum, U., Hardcastle, A.J. and Cheetham, M.E. (2010) The retinitis pigmentosa protein RP2 links pericentriolar vesicle transport between the Golgi and the primary cilium. Hum. Mol. Genet., 19, 1358-1367
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 1358-1367
    • Evans, R.J.1    Schwarz, N.2    Nagel-Wolfrum, K.3    Wolfrum, U.4    Hardcastle, A.J.5    Cheetham, M.E.6


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