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Volumn 139, Issue 6, 2016, Pages 1163-1174

Formation, release, and internalization of stable tau oligomers in cells

Author keywords

dimerization; Gaussia luciferase assay; oligomers; tau protein

Indexed keywords

DIMER; OLIGOMER; TAU PROTEIN; PROTEIN BINDING;

EID: 85000783258     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.13866     Document Type: Article
Times cited : (49)

References (52)
  • 1
    • 0037126688 scopus 로고    scopus 로고
    • Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
    • Barghorn S. and Mandelkow E. (2002) Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments. Biochemistry 41, 14885–14896.
    • (2002) Biochemistry , vol.41 , pp. 14885-14896
    • Barghorn, S.1    Mandelkow, E.2
  • 2
    • 22844445324 scopus 로고    scopus 로고
    • Purification of recombinant tau protein and preparation of Alzheimer-paired helical filaments in vitro
    • Barghorn S., Biernat J. and Mandelkow E. (2005) Purification of recombinant tau protein and preparation of Alzheimer-paired helical filaments in vitro. Methods Mol. Biol. 299, 35–51.
    • (2005) Methods Mol. Biol. , vol.299 , pp. 35-51
    • Barghorn, S.1    Biernat, J.2    Mandelkow, E.3
  • 7
    • 84857275902 scopus 로고    scopus 로고
    • Propagation of tau pathology in a model of early Alzheimer's disease
    • de Calignon A., Polydoro M., Suarez-Calvet M. et al. (2012) Propagation of tau pathology in a model of early Alzheimer's disease. Neuron 73, 685–697.
    • (2012) Neuron , vol.73 , pp. 685-697
    • de Calignon, A.1    Polydoro, M.2    Suarez-Calvet, M.3
  • 8
    • 84865663663 scopus 로고    scopus 로고
    • beta-Sheet core of tau paired helical filaments revealed by solid-state NMR
    • Daebel V., Chinnathambi S., Biernat J. et al. (2012) beta-Sheet core of tau paired helical filaments revealed by solid-state NMR. J. Am. Chem. Soc. 134, 13982–13989.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 13982-13989
    • Daebel, V.1    Chinnathambi, S.2    Biernat, J.3
  • 9
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel D. N., Hyman A. A., Cobb M. H. and Kirschner M. W. (1992) Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell 3, 1141–1154.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 10
    • 0032516493 scopus 로고    scopus 로고
    • Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution
    • Friedhoff P., Schneider A., Mandelkow E. M. and Mandelkow E. (1998a) Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution. Biochemistry 37, 10223–10230.
    • (1998) Biochemistry , vol.37 , pp. 10223-10230
    • Friedhoff, P.1    Schneider, A.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 12
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B., Jacks R. L. and Diamond M. I. (2009a) Propagation of tau misfolding from the outside to the inside of a cell. J. Biol. Chem. 284, 12845–12852.
    • (2009) J. Biol. Chem. , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 13
    • 63649160214 scopus 로고    scopus 로고
    • Conformational diversity of wild-type Tau fibrils specified by templated conformation change
    • Frost B., Ollesch J., Wille H. and Diamond M. I. (2009b) Conformational diversity of wild-type Tau fibrils specified by templated conformation change. J. Biol. Chem. 284, 3546–3551.
    • (2009) J. Biol. Chem. , vol.284 , pp. 3546-3551
    • Frost, B.1    Ollesch, J.2    Wille, H.3    Diamond, M.I.4
  • 15
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M., Spillantini M. G., Jakes R., Rutherford D. and Crowther R. A. (1989) Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3, 519–526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 16
    • 79961000597 scopus 로고    scopus 로고
    • Characterization of oligomer formation of amyloid-beta peptide using a split-luciferase complementation assay
    • Hashimoto T., Adams K. W., Fan Z., McLean P. J. and Hyman B. T. (2011) Characterization of oligomer formation of amyloid-beta peptide using a split-luciferase complementation assay. J. Biol. Chem. 286, 27081–27091.
    • (2011) J. Biol. Chem. , vol.286 , pp. 27081-27091
    • Hashimoto, T.1    Adams, K.W.2    Fan, Z.3    McLean, P.J.4    Hyman, B.T.5
  • 17
    • 84882306577 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
    • Holmes B. B., DeVos S. L., Kfoury N. et al. (2013) Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds. Proc. Natl Acad. Sci. USA 110, E3138–E3147.
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E3138-E3147
    • Holmes, B.B.1    DeVos, S.L.2    Kfoury, N.3
  • 18
    • 78650251838 scopus 로고    scopus 로고
    • Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration
    • Hoover B. R., Reed M. N., Su J. et al. (2010) Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration. Neuron 68, 1067–1081.
    • (2010) Neuron , vol.68 , pp. 1067-1081
    • Hoover, B.R.1    Reed, M.N.2    Su, J.3
  • 19
    • 53349144370 scopus 로고    scopus 로고
    • The natively unfolded character of tau and its aggregation to Alzheimer-like paired helical filaments
    • Jeganathan S., von Bergen M., Mandelkow E. M. and Mandelkow E. (2008) The natively unfolded character of tau and its aggregation to Alzheimer-like paired helical filaments. Biochemistry 47, 10526–10539.
    • (2008) Biochemistry , vol.47 , pp. 10526-10539
    • Jeganathan, S.1    von Bergen, M.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 20
    • 0031025396 scopus 로고    scopus 로고
    • The tau protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments
    • Johnson G. V., Seubert P., Cox T. M., Motter R., Brown J. P. and Galasko D. (1997) The tau protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments. J. Neurochem. 68, 430–433.
    • (1997) J. Neurochem. , vol.68 , pp. 430-433
    • Johnson, G.V.1    Seubert, P.2    Cox, T.M.3    Motter, R.4    Brown, J.P.5    Galasko, D.6
  • 21
    • 79951925183 scopus 로고    scopus 로고
    • Ubiquitinylation of alpha-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5)
    • Kalia L. V., Kalia S. K., Chau H., Lozano A. M., Hyman B. T. and McLean P. J. (2011) Ubiquitinylation of alpha-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5). PLoS ONE 6, e14695.
    • (2011) PLoS ONE , vol.6
    • Kalia, L.V.1    Kalia, S.K.2    Chau, H.3    Lozano, A.M.4    Hyman, B.T.5    McLean, P.J.6
  • 22
    • 84944339538 scopus 로고    scopus 로고
    • Identification of disulfide cross-linked tau dimer responsible for tau propagation
    • Kim D., Lim S., Haque M. M. et al. (2015) Identification of disulfide cross-linked tau dimer responsible for tau propagation. Sci. Rep. 5, 15231.
    • (2015) Sci. Rep. , vol.5 , pp. 15231
    • Kim, D.1    Lim, S.2    Haque, M.M.3
  • 25
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall G. and Cole R. D. (1984) Phosphorylation affects the ability of tau protein to promote microtubule assembly. J. Biol. Chem. 259, 5301–5305.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 26
    • 1942509627 scopus 로고    scopus 로고
    • Heparin-induced cancer cell death
    • Linhardt R. J. (2004) Heparin-induced cancer cell death. Chem. Biol. 11, 420–422.
    • (2004) Chem. Biol. , vol.11 , pp. 420-422
    • Linhardt, R.J.1
  • 28
    • 84931281486 scopus 로고    scopus 로고
    • Tau trimers are the minimal propagation unit spontaneously internalized to seed intracellular aggregation
    • Mirbaha H., Holmes B. B., Sanders D. W., Bieschke J. and Diamond M. I. (2015) Tau trimers are the minimal propagation unit spontaneously internalized to seed intracellular aggregation. J. Biol. Chem. 290, 14893–14903.
    • (2015) J. Biol. Chem. , vol.290 , pp. 14893-14903
    • Mirbaha, H.1    Holmes, B.B.2    Sanders, D.W.3    Bieschke, J.4    Diamond, M.I.5
  • 30
    • 0033583176 scopus 로고    scopus 로고
    • Heparin-induced conformational change in microtubule-associated protein Tau as detected by chemical cross-linking and phosphopeptide mapping
    • Paudel H. K. and Li W. (1999) Heparin-induced conformational change in microtubule-associated protein Tau as detected by chemical cross-linking and phosphopeptide mapping. J. Biol. Chem. 274, 8029–8038.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8029-8038
    • Paudel, H.K.1    Li, W.2
  • 31
    • 84876459364 scopus 로고    scopus 로고
    • Physiological release of endogenous tau is stimulated by neuronal activity
    • Pooler A. M., Phillips E. C., Lau D. H., Noble W. and Hanger D. P. (2013) Physiological release of endogenous tau is stimulated by neuronal activity. EMBO Rep. 14, 389–394.
    • (2013) EMBO Rep. , vol.14 , pp. 389-394
    • Pooler, A.M.1    Phillips, E.C.2    Lau, D.H.3    Noble, W.4    Hanger, D.P.5
  • 32
    • 0030913980 scopus 로고    scopus 로고
    • The ‘jaws’ model of tau-microtubule interaction examined in CHO cells
    • Preuss U., Biernat J., Mandelkow E. M. and Mandelkow E. (1997) The ‘jaws’ model of tau-microtubule interaction examined in CHO cells. J. Cell Sci. 110(Pt 6), 789–800.
    • (1997) J. Cell Sci. , vol.110 , pp. 789-800
    • Preuss, U.1    Biernat, J.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 33
    • 33751208345 scopus 로고    scopus 로고
    • A highly sensitive protein-protein interaction assay based on Gaussia luciferase
    • Remy I. and Michnick S. W. (2006) A highly sensitive protein-protein interaction assay based on Gaussia luciferase. Nat. Methods 3, 977–979.
    • (2006) Nat. Methods , vol.3 , pp. 977-979
    • Remy, I.1    Michnick, S.W.2
  • 34
    • 44949259180 scopus 로고    scopus 로고
    • Complementary dimerization of microtubule-associated tau protein: Implications for microtubule bundling and tau-mediated pathogenesis
    • Rosenberg K. J., Ross J. L., Feinstein H. E., Feinstein S. C. and Israelachvili J. (2008) Complementary dimerization of microtubule-associated tau protein: Implications for microtubule bundling and tau-mediated pathogenesis. Proc. Natl Acad. Sci. USA 105, 7445–7450.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 7445-7450
    • Rosenberg, K.J.1    Ross, J.L.2    Feinstein, H.E.3    Feinstein, S.C.4    Israelachvili, J.5
  • 35
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • SantaCruz K., Lewis J., Spires T. et al. (2005) Tau suppression in a neurodegenerative mouse model improves memory function. Science 309, 476–481.
    • (2005) Science , vol.309 , pp. 476-481
    • SantaCruz, K.1    Lewis, J.2    Spires, T.3
  • 36
    • 0029114196 scopus 로고
    • Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments
    • Schweers O., Mandelkow E. M., Biernat J. and Mandelkow E. (1995) Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments. Proc. Natl Acad. Sci. USA 92, 8463–8467.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8463-8467
    • Schweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 38
    • 84944088611 scopus 로고    scopus 로고
    • Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer's disease brain
    • Takeda S., Wegmann S., Cho H. et al. (2015) Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer's disease brain. Nat. Commun. 6, 8490.
    • (2015) Nat. Commun. , vol.6 , pp. 8490
    • Takeda, S.1    Wegmann, S.2    Cho, H.3
  • 39
    • 84985947118 scopus 로고    scopus 로고
    • Seed-competent high-molecular-weight tau species accumulates in the cerebrospinal fluid of Alzheimer's disease mouse model and human patients
    • Takeda S., Commins C., DeVos S. L. et al. (2016) Seed-competent high-molecular-weight tau species accumulates in the cerebrospinal fluid of Alzheimer's disease mouse model and human patients. Ann. Neurol. 80, 355–367.
    • (2016) Ann. Neurol. , vol.80 , pp. 355-367
    • Takeda, S.1    Commins, C.2    DeVos, S.L.3
  • 40
    • 84917706097 scopus 로고    scopus 로고
    • Oligomer formation of tau protein hyperphosphorylated in cells
    • Tepper K., Biernat J., Kumar S. et al. (2014) Oligomer formation of tau protein hyperphosphorylated in cells. J. Biol. Chem. 289, 34389–34407.
    • (2014) J. Biol. Chem. , vol.289 , pp. 34389-34407
    • Tepper, K.1    Biernat, J.2    Kumar, S.3
  • 41
    • 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. and Mandelkow E. M. (2007) Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1. J. Neurosci. 27, 2896–2907.
    • (2007) J. Neurosci. , vol.27 , pp. 2896-2907
    • Thies, E.1    Mandelkow, E.M.2
  • 42
    • 0032799381 scopus 로고    scopus 로고
    • Tau regulates the attachment/detachment but not the speed of motors in microtubule-dependent transport of single vesicles and organelles
    • Trinczek B., Ebneth A., Mandelkow E. M. and Mandelkow E. (1999) Tau regulates the attachment/detachment but not the speed of motors in microtubule-dependent transport of single vesicles and organelles. J. Cell Sci. 112(Pt 14), 2355–2367.
    • (1999) J. Cell Sci. , vol.112 , pp. 2355-2367
    • Trinczek, B.1    Ebneth, A.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 43
    • 77956242962 scopus 로고    scopus 로고
    • Human Tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability
    • Wegmann S., Jung Y. J., Chinnathambi S., Mandelkow E. M., Mandelkow E. and Muller D. J. (2010) Human Tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability. J. Biol. Chem. 285, 27302–27313.
    • (2010) J. Biol. Chem. , vol.285 , pp. 27302-27313
    • Wegmann, S.1    Jung, Y.J.2    Chinnathambi, S.3    Mandelkow, E.M.4    Mandelkow, E.5    Muller, D.J.6
  • 44
    • 84875279731 scopus 로고    scopus 로고
    • The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush
    • Wegmann S., Medalsy I. D., Mandelkow E. and Muller D. J. (2013) The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush. Proc. Natl Acad. Sci. USA 110, E313–E321.
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E313-E321
    • Wegmann, S.1    Medalsy, I.D.2    Mandelkow, E.3    Muller, D.J.4
  • 45
    • 84955184686 scopus 로고    scopus 로고
    • Removing endogenous tau does not prevent tau propagation yet reduces its neurotoxicity
    • Wegmann S., Maury E. A., Kirk M. J. et al. (2015) Removing endogenous tau does not prevent tau propagation yet reduces its neurotoxicity. EMBO J. 34, 3028–3041.
    • (2015) EMBO J. , vol.34 , pp. 3028-3041
    • Wegmann, S.1    Maury, E.A.2    Kirk, M.J.3
  • 47
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro
    • Wille H., Drewes G., Biernat J., Mandelkow E. M. and Mandelkow E. (1992) Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J. Cell Biol. 118, 573–584.
    • (1992) J. Cell Biol. , vol.118 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 48
    • 84859525656 scopus 로고    scopus 로고
    • Distinct dendritic spine and nuclear phases of calcineurin activation after exposure to amyloid-beta revealed by a novel fluorescence resonance energy transfer assay
    • Wu H. Y., Hudry E., Hashimoto T., Uemura K., Fan Z. Y., Berezovska O., Grosskreutz C. L., Bacskai B. J. and Hyman B. T. (2012) Distinct dendritic spine and nuclear phases of calcineurin activation after exposure to amyloid-beta revealed by a novel fluorescence resonance energy transfer assay. J. Neurosci. 32, 5298–5309.
    • (2012) J. Neurosci. , vol.32 , pp. 5298-5309
    • Wu, H.Y.1    Hudry, E.2    Hashimoto, T.3    Uemura, K.4    Fan, Z.Y.5    Berezovska, O.6    Grosskreutz, C.L.7    Bacskai, B.J.8    Hyman, B.T.9
  • 49
    • 84872714502 scopus 로고    scopus 로고
    • Small misfolded Tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons
    • Wu J. W., Herman M., Liu L. et al. (2013) Small misfolded Tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons. J. Biol. Chem. 288, 1856–1870.
    • (2013) J. Biol. Chem. , vol.288 , pp. 1856-1870
    • Wu, J.W.1    Herman, M.2    Liu, L.3
  • 50
    • 80052940324 scopus 로고    scopus 로고
    • In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice
    • Yamada K., Cirrito J. R., Stewart F. R. et al. (2011) In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice. J. Neurosci. 31, 13110–13117.
    • (2011) J. Neurosci. , vol.31 , pp. 13110-13117
    • Yamada, K.1    Cirrito, J.R.2    Stewart, F.R.3
  • 51
    • 34247547924 scopus 로고    scopus 로고
    • Tau in cerebrospinal fluid: a sensitive sandwich enzyme-linked immunosorbent assay using tyramide signal amplification
    • Yamamori H., Khatoon S., Grundke-Iqbal I., Blennow K., Ewers M., Hampel H. and Iqbal K. (2007) Tau in cerebrospinal fluid: a sensitive sandwich enzyme-linked immunosorbent assay using tyramide signal amplification. Neurosci. Lett. 418, 186–189.
    • (2007) Neurosci. Lett. , vol.418 , pp. 186-189
    • Yamamori, H.1    Khatoon, S.2    Grundke-Iqbal, I.3    Blennow, K.4    Ewers, M.5    Hampel, H.6    Iqbal, K.7
  • 52
    • 84935917108 scopus 로고    scopus 로고
    • Towards understanding the roles of heparan sulfate proteoglycans in Alzheimer's disease
    • Zhang G. L., Zhang X., Wang X. M. and Li J. P. (2014) Towards understanding the roles of heparan sulfate proteoglycans in Alzheimer's disease. Biomed. Res. Int. 2014, 516028.
    • (2014) Biomed. Res. Int. , vol.2014 , pp. 516028
    • Zhang, G.L.1    Zhang, X.2    Wang, X.M.3    Li, J.P.4


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