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Distinct differences in prion-like seeding and aggregation between Tau protein variants provide mechanistic insights into tauopathies

Strang, Kevin H., Croft, Cara L., Sorrentino, Zachary A., Chakrabarty, Paramita, Golde, Todd E., Giasson, Benoit I.·2018·Journal of Biological Chemistry

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  1. Wang, 2016, Tau in physiology and pathology, Nat. Rev. Neurosci., 17, 5, 10.1038/nrn.2015.1 · DOI · Paper page
  2. Iqbal, 2016, Tau and neurodegenerative disease: the story so far, Nat. Rev. Neurol., 12, 15, 10.1038/nrneurol.2015.225 · DOI · Paper page
  3. Goedert, 2017, Propagation of Tau aggregates and neurodegeneration, Annu. Rev. Neurosci., 40, 189, 10.1146/annurev-neuro-072116-031153 · DOI · Paper page
  4. Cleveland, 1977, Physical and chemical properties of purified Tau factor and the role of Tau in microtubule assembly, J. Mol. Biol., 116, 227, 10.1016/0022-2836(77)90214-5 · DOI · Paper page
  5. LoPresti, 1995, Functional implications for the microtubule-associated protein Tau: localization in oligodendrocytes, Proc. Natl. Acad. Sci. U.S.A., 92, 10369, 10.1073/pnas.92.22.10369 · DOI · Paper page
  6. Binder, 1985, The distribution of Tau in the mammalian central nervous system, J. Cell Biol., 101, 1371, 10.1083/jcb.101.4.1371 · DOI · Paper page
  7. Weingarten, 1975, A protein factor essential for microtubule assembly, Proc. Natl. Acad. Sci. U.S.A., 72, 1858, 10.1073/pnas.72.5.1858 · DOI · Paper page
  8. Guo, 2017, Roles of Tau protein in health and disease, Acta Neuropathol., 133, 665, 10.1007/s00401-017-1707-9 · DOI · Paper page
  9. Goedert, 1989, Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein Tau containing four tandem repeats: differential expression of Tau protein mRNAs in human brain, EMBO J., 8, 393, 10.1002/j.1460-2075.1989.tb03390.x · DOI · Paper page
  10. Goedert, 1989, Multiple isoforms of human microtubule-associated protein Tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease, Neuron., 3, 519, 10.1016/0896-6273(89)90210-9 · DOI · Paper page
  11. Ghetti, 2015, Frontotemporal dementia caused by microtubule-associated protein Tau gene (MAPT) mutations: a chameleon for neuropathology and neuroimaging, Neuropathol. Appl. Neurobiol., 41, 24, 10.1111/nan.12213 · DOI
  12. Hasegawa, 1998, Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly, FEBS Lett., 437, 207, 10.1016/S0014-5793(98)01217-4 · DOI
  13. Barghorn, 2000, Structure, microtubule interactions, and paired helical filament aggregation by Tau mutants of frontotemporal dementias, Biochemistry., 39, 11714, 10.1021/bi000850r · DOI
  14. Hong, 1998, Mutation-specific functional impairments in distinct Tau isoforms of hereditary FTDP-17, Science., 282, 1914, 10.1126/science.282.5395.1914 · DOI
  15. Magnani, 2007, Interaction of Tau protein with the dynactin complex, EMBO J., 26, 4546, 10.1038/sj.emboj.7601878 · DOI
  16. Alonso Adel, 2004, Promotion of hyperphosphorylation by frontotemporal dementia Tau mutations, J. Biol. Chem., 279, 34873, 10.1074/jbc.M405131200 · DOI
  17. Nacharaju, 1999, Accelerated filament formation from Tau protein with specific FTDP-17 missense mutations, FEBS Lett., 447, 195, 10.1016/S0014-5793(99)00294-X · DOI
  18. Goedert, 1999, Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of Tau filaments, FEBS Lett., 450, 306, 10.1016/S0014-5793(99)00508-6 · DOI
  19. Friedhoff, 1998, A nucleated assembly mechanism of Alzheimer paired helical filaments, Proc. Natl. Acad. Sci. U.S.A., 95, 15712, 10.1073/pnas.95.26.15712 · DOI · Paper page
  20. Prusiner, 1998, Nobel lecture: prions, Proc. Natl. Acad. Sci., 95, 13363, 10.1073/pnas.95.23.13363 · DOI · Paper page
  21. Eisenberg, 2012, The amyloid state of proteins in human diseases, Cell., 148, 1188, 10.1016/j.cell.2012.02.022 · DOI
  22. Aguzzi, 2007, Insights into prion strains and neurotoxicity, Nat. Rev. Mol. Cell Biol., 8, 552, 10.1038/nrm2204 · DOI
  23. Lewis, 2016, Propagation of Tau pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies, Acta Neuropathol., 131, 27, 10.1007/s00401-015-1507-z · DOI
  24. Ayers, 2018, Prion-like spreading in tauopathies, Biol. Psychiatry., 83, 337, 10.1016/j.biopsych.2017.04.003 · DOI
  25. Wu, 2013, Small misfolded Tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons, J. Biol. Chem., 288, 1856, 10.1074/jbc.M112.394528 · DOI · Paper page
  26. Nonaka, 2010, Seeded aggregation and toxicity of α-synuclein and Tau: cellular models of neurodegenerative diseases, J. Biol. Chem., 285, 34885, 10.1074/jbc.M110.148460 · DOI
  27. Clavaguera, 2013, Brain homogenates from human tauopathies induce Tau inclusions in mouse brain, Proc. Natl. Acad. Sci. U.S.A., 110, 9535, 10.1073/pnas.1301175110 · DOI
  28. von Bergen, 2005, Tau aggregation is driven by a transition from random coil to beta sheet structure, Biochim. Biophys. Acta., 1739, 158, 10.1016/j.bbadis.2004.09.010 · DOI
  29. von Bergen, 2000, Assembly of Tau protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming beta structure, Proc. Natl. Acad. Sci. U.S.A., 97, 5129, 10.1073/pnas.97.10.5129 · DOI · Paper page
  30. Li, 2006, Characterization of two VQIXXK motifs for Tau fibrillization in vitro, Biochemistry., 45, 15692, 10.1021/bi061422+ · DOI
  31. Ganguly, 2015, Tau assembly: the dominant role of PHF6 (VQIVYK) in microtubule binding region repeat R3, J. Phys. Chem. B., 119, 4582, 10.1021/acs.jpcb.5b00175 · DOI
  32. Smit, 2017, Primary fibril nucleation of aggregation prone Tau fragments PHF6 and PHF6, J. Phys. Chem. B., 121, 3250, 10.1021/acs.jpcb.6b07045 · DOI
  33. Sanders, 2014, Distinct Tau prion strains propagate in cells and mice and define different tauopathies, Neuron., 82, 1271, 10.1016/j.neuron.2014.04.047 · DOI · Paper page
  34. Kaufman, 2016, Tau prion strains dictate patterns of cell pathology, progression rate, and regional vulnerability in vivo, Neuron., 92, 796, 10.1016/j.neuron.2016.09.055 · DOI · Paper page
  35. Meyer, 2014, Single mutations in Tau modulate the populations of fibril conformers through seed selection, Angew. Chem. Int. Ed. Engl., 53, 1590, 10.1002/anie.201308473 · DOI · Paper page
  36. Roberson, 2012, Mouse models of frontotemporal dementia, Ann. Neurol., 72, 837, 10.1002/ana.23722 · DOI
  37. Lim, 2014, Cell-based models to investigate Tau aggregation, Comput. Struct. Biotechnol. J., 12, 7, 10.1016/j.csbj.2014.09.011 · DOI
  38. Holmes, 2014, Proteopathic Tau seeding predicts tauopathy in vivo, Proc. Natl. Acad. Sci. U.S.A., 111, E4376, 10.1073/pnas.1411649111 · DOI · Paper page
  39. Waxman, 2011, Induction of intracellular Tau aggregation is promoted by α-synuclein seeds and provides novel insights into the hyperphosphorylation of Tau, J. Neurosci., 31, 7604, 10.1523/JNEUROSCI.0297-11.2011 · DOI
  40. Elbaum-Garfinkle, 2014, Tau mutants bind tubulin heterodimers with enhanced affinity, Proc. Natl. Acad. Sci. U.S.A., 111, 6311, 10.1073/pnas.1315983111 · DOI
  41. Deramecourt, 2012, Clinical, neuropathological, and biochemical characterization of the novel Tau mutation P332S, J. Alzheimers Dis., 31, 741, 10.3233/JAD-2012-120160 · DOI
  42. Yu, 2012, Cross-seeding and conformational selection between three- and four-repeat human Tau proteins, J. Biol. Chem., 287, 14950, 10.1074/jbc.M112.340794 · DOI
  43. Falcon, 2015, Conformation determines the seeding potencies of native and recombinant Tau aggregates, J. Biol. Chem., 290, 1049, 10.1074/jbc.M114.589309 · DOI
  44. Khlistunova, 2006, Inducible expression of Tau repeat domain in cell models of tauopathy: aggregation is toxic to cells but can be reversed by inhibitor drugs, J. Biol. Chem., 281, 1205, 10.1074/jbc.M507753200 · DOI
  45. Wang, 2007, Stepwise proteolysis liberates Tau fragments that nucleate the Alzheimer-like aggregation of full-length Tau in a neuronal cell model, Proc. Natl. Acad. Sci. U.S.A., 104, 10252, 10.1073/pnas.0703676104 · DOI
  46. D'Souza, 1999, Missense and silent Tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements, Proc. Natl. Acad. Sci. U.S.A., 96, 5598, 10.1073/pnas.96.10.5598 · DOI
  47. Liu, 2008, Tau exon 10 alternative splicing and tauopathies, Mol. Neurodegener., 3, 8, 10.1186/1750-1326-3-8 · DOI · Paper page
  48. Denk, 2009, Knock-out and transgenic mouse models of tauopathies, Neurobiol. Aging., 30, 1, 10.1016/j.neurobiolaging.2007.05.010 · DOI
  49. Ahmed, 2014, A novel in vivo model of Tau propagation with rapid and progressive neurofibrillary tangle pathology: The pattern of spread is determined by connectivity, not proximity, Acta Neuropathol., 127, 667, 10.1007/s00401-014-1254-6 · DOI
  50. Boluda, 2015, Differential induction and spread of Tau pathology in young PS19 Tau transgenic mice following intracerebral injections of pathological Tau from Alzheimer's disease or corticobasal degeneration brains, Acta Neuropathol., 129, 221, 10.1007/s00401-014-1373-0 · DOI
  51. Jackson, 2016, Short fibrils constitute the major species of seed-competent Tau in the brains of mice transgenic for human P301S Tau, J. Neurosci., 36, 762, 10.1523/JNEUROSCI.3542-15.2016 · DOI
  52. Miyasaka, 2001, Selective deposition of mutant Tau in the FTDP-17 brain affected by the P301L mutation, J. Neuropathol. Exp. Neurol., 60, 872, 10.1093/jnen/60.9.872 · DOI
  53. Spillantini, 1998, Tau pathology in two Dutch families with mutations in the microtubule-binding region of Tau, Am. J. Pathol., 153, 1359, 10.1016/S0002-9440(10)65721-5 · DOI
  54. Aoyagi, 2007, Fibrillogenic nuclei composed of P301L mutant Tau induce elongation of P301L Tau but not wild-type Tau, J. Biol. Chem., 282, 20309, 10.1074/jbc.M611876200 · DOI
  55. Rossi, 2012, New mutations in MAPT gene causing frontotemporal lobar degeneration: biochemical and structural characterization, Neurobiol. Aging., 33, 834.e1, 10.1016/j.neurobiolaging.2011.08.008 · DOI
  56. Hasegawa, 1999, FTDP-17 mutations N279K and S305N in Tau produce increased splicing of exon 10, FEBS Lett., 443, 93, 10.1016/S0014-5793(98)01696-2 · DOI · Paper page
  57. Steward, 2002, Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily, J. Mol. Biol., 318, 935, 10.1016/S0022-2836(02)00184-5 · DOI
  58. Monsellier, 2007, Prevention of amyloid-like aggregation as a driving force of protein evolution, EMBO Rep., 8, 737, 10.1038/sj.embor.7401034 · DOI
  59. Jeganathan, 2006, Global hairpin folding of Tau in solution, Biochemistry., 45, 2283, 10.1021/bi0521543 · DOI · Paper page
  60. Hasegawa, 1997, Alzheimer-like changes in microtubule-associated protein Tau induced by sulfated glycosaminoglycans: inhibition of microtubule binding stimulation of phosphorylation filament assembly depend on the degree of sulfation, J. Biol. Chem., 272, 33118, 10.1074/jbc.272.52.33118 · DOI
  61. Crystal, 2003, A comparison of amyloid fibrillogenesis using the novel fluorescent compound K114, J. Neurochem., 86, 1359, 10.1046/j.1471-4159.2003.01949.x · DOI
  62. Waxman, 2010, Residue Glu83 plays a major role in negatively regulating α-synuclein amyloid formation, Biochem. Biophys. Res. Commun., 391, 1415, 10.1016/j.bbrc.2009.12.079 · DOI
  63. Poepsel, 2015, Determinants of amyloid fibril degradation by the PDZ protease HTRA1, Nat. Chem. Biol., 11, 862, 10.1038/nchembio.1931 · DOI
  64. Strang, 2017, Generation and characterization of new monoclonal antibodies targeting the PHF1 and AT8 epitopes on human Tau, Acta Neuropathol. Commun., 5, 58, 10.1186/s40478-017-0458-0 · DOI

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Metadata

Authors
Strang, K. H., Croft, C. L., Sorrentino, Z. A., Chakrabarty, P., Golde, T. E., & Giasson, B. I.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2018-02
Volume
293
Issue
7
Pages
2408-2421
ISSN
0021-9258
Cited by
124
References
19
Language
en
Funders
National Institutes of Health (R01NS089022)

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Strang, K. H., Croft, C. L., Sorrentino, Z. A., Chakrabarty, P., Golde, T. E., & Giasson, B. I. (2018). Distinct differences in prion-like seeding and aggregation between Tau protein variants provide mechanistic insights into tauopathies. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m117.815357

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