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Tau-mediated dysregulation of RNA: Evidence for a common molecular mechanism of toxicity in frontotemporal dementia and other tauopathies

Koren, Shon A., Galvis-Escobar, Sara, Abisambra, Jose F.·2020·Neurobiology of Disease

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  • The potential reason of reduced neuronal activity in neurons accumulated with pathological tau is the repression of translation by abnormal tau accumulation.

    “The potential reason of reduced neuronal activity in neurons accumulated with pathological tau is the repression of translation91 by abnormal tau accumulation.”

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  1. Abisambra, 2013, Tau accumulation activates the unfolded protein response by impairing endoplasmic reticulum-associated degradation, J. Neurosci., 33, 9498, 10.1523/JNEUROSCI.5397-12.2013 · DOI
  2. Ambadipudi, 2017, Liquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein tau, Nat. Commun., 8, 275, 10.1038/s41467-017-00480-0 · DOI · Paper page
  3. An, 2003, Up-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer’s disease, Am. J. Pathol., 163, 591, 10.1016/S0002-9440(10)63687-5 · DOI · Paper page
  4. Apicco, 2019, Dysregulation of RNA splicing in tauopathies, Cell Rep., 29
  5. Bancher, 1989, Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer’s disease, Brain Res., 477, 90, 10.1016/0006-8993(89)91396-6 · DOI · Paper page
  6. Banerjee, 2020, Tau protein- induced sequestration of the eukaryotic ribosome: implications in neurodegenerative disease, Sci. Rep., 10, 5225, 10.1038/s41598-020-61777-7 · DOI
  7. Bell, 2016, PERK-opathies: An endoplasmic reticulum stress mechanism underlying neurodegeneration, Curr. Alzheimer Res., 13, 150, 10.2174/1567205013666151218145431 · DOI
  8. Bentmann, 2012, Requirements for stress granule recruitment of fused in sarcoma (FUS) and TAR DNA-binding protein of 43 kDa (TDP-43), J. Biol. Chem., 287, 23079, 10.1074/jbc.M111.328757 · DOI
  9. Berry, 2015, RNA transcription modulates phase transition-driven nuclear body assembly, Proc. Natl. Acad. Sci. U. S. A., 112, E5237, 10.1073/pnas.1509317112 · DOI · Paper page
  10. 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
  11. Boyko, 2019, Liquid-liquid phase separation of tau protein: the crucial role of electrostatic interactions, J. Biol. Chem., 294, 11054, 10.1074/jbc.AC119.009198 · DOI
  12. Brandt, 1993, Functional organization of microtubule-associated protein tau. Identification of regions which affect microtubule growth, nucleation, and bundle formation in vitro, J. Biol. Chem., 268, 3414, 10.1016/S0021-9258(18)53710-8 · DOI
  13. Brion, 1995, Distribution and expression of the alpha-tubulin mRNA in the hippocampus and the temporal cortex in Alzheimer’s disease, Pathol. Res. Pract., 191, 490, 10.1016/S0344-0338(11)80867-8 · DOI
  14. Bryan, 1975, Inhibition of tubulin assembly by RNA and other polyanions: evidence for a required protein, Proc. Natl. Acad. Sci. U. S. A., 72, 3570, 10.1073/pnas.72.9.3570 · DOI
  15. Bukar Maina, 2016, Nuclear tau and its potential role in Alzheimer’s disease, Biomolecules., 6, 9, 10.3390/biom6010009 · DOI · Paper page
  16. Cairns, 2007, Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the consortium for frontotemporal lobar degeneration, Acta Neuropathol., 114, 5, 10.1007/s00401-007-0237-2 · DOI · Paper page
  17. Chen, 2019, RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy, Brain., 142, 3753, 10.1093/brain/awz313 · DOI
  18. Cruz, 2019, The pathophysiology of tau and stress granules in disease, Adv. Exp. Med. Biol., 1184, 359, 10.1007/978-981-32-9358-8_26 · DOI
  19. Dayan, 1973, Histometric observations on the metabolism of tangle-bearing neurons, J. Neurol. Sci., 19, 433, 10.1016/0022-510X(73)90040-3 · DOI
  20. Ding, 2005, Ribosome dysfunction is an early event in Alzheimer’s disease, J. Neurosci., 25, 9171, 10.1523/JNEUROSCI.3040-05.2005 · DOI · Paper page
  21. Ding, 2006, Decreased RNA, and increased RNA oxidation, in ribosomes from early Alzheimer’s disease, Neurochem. Res., 31, 705, 10.1007/s11064-006-9071-5 · DOI · Paper page
  22. Ding, 2012, Increased 5S rRNA oxidation in Alzheimer’s disease, J. Alzheimers Dis., 29, 201, 10.3233/JAD-2012-111058 · DOI
  23. Doebler, 1987, Neuronal RNA in relation to neuronal loss and neurofibrillary pathology in the hippocampus in Alzheimer’s disease, J. Neuropathol. Exp. Neurol., 46, 28, 10.1097/00005072-198701000-00003 · DOI
  24. Drechsel, 1992, Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau, Mol. Biol. Cell, 3, 1141, 10.1091/mbc.3.10.1141 · DOI
  25. Eftekharzadeh, 2018, Tau protein disrupts nucleocytoplasmic transport in Alzheimer’s disease, Neuron., 99
  26. Evans, 2019, Decreased synthesis of ribosomal proteins in tauopathy revealed by non-canonical amino acid labelling, EMBO J., 38, 10.15252/embj.2018101174 · DOI
  27. Ferrari, 2020, Arginine pi-stacking drives binding to fibrils of the Alzheimer protein tau, Nat. Commun., 11, 571, 10.1038/s41467-019-13745-7 · DOI
  28. Ginsberg, 1997, Sequestration of RNA in Alzheimer’s disease neurofibrillary tangles and senile plaques, Ann. Neurol., 41, 200, 10.1002/ana.410410211 · DOI
  29. Ginsberg, 1998, RNA sequestration to pathological lesions of neurodegenerative diseases, Acta Neuropathol., 96, 487, 10.1007/s004010050923 · DOI
  30. Grundke-Iqbal, 1986, Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology, Proc. Natl. Acad. Sci. U. S. A., 83, 4913, 10.1073/pnas.83.13.4913 · DOI · Paper page
  31. Guillemette, 1986, Characterization of messenger RNA from the cerebral cortex of control and Alzheimer-afflicted brain, J. Neurochem., 47, 987, 10.1111/j.1471-4159.1986.tb00708.x · DOI
  32. Gunawardana, 2015, The human tau Interactome: binding to the Ribonucleoproteome, and impaired binding of the proline-to-leucine mutant at position 301 (P301L) to chaperones and the proteasome, Mol. Cell. Proteomics, 14, 3000, 10.1074/mcp.M115.050724 · DOI
  33. Hales, 2014, Aggregates of small nuclear ribonucleic acids (snRNAs) in Alzheimer’s disease, Brain Pathol., 24, 344, 10.1111/bpa.12133 · DOI · Paper page
  34. Halliday, 2015, Partial restoration of protein synthesis rates by the small molecule ISRIB prevents neurodegeneration without pancreatic toxicity, Cell Death Dis., 6, 10.1038/cddis.2015.49 · DOI
  35. Halliday, 2017, Fine-tuning PERK signaling for neuroprotection, J. Neurochem., 142, 812, 10.1111/jnc.14112 · DOI
  36. Hasegawa, 1997, Alzheimer-like changes in microtubule-associated protein tau induced by sulfated glycosaminoglycans. Inhibition of microtubule binding, stimulation of phosphorylation, and filament assembly depend on the degree of sulfation, J. Biol. Chem., 272, 33118, 10.1074/jbc.272.52.33118 · DOI
  37. Hashimoto, 2018, Critical review: involvement of endoplasmic reticulum stress in the aetiology of Alzheimer’s disease, Open Biol., 8, 10.1098/rsob.180024 · DOI · Paper page
  38. Hernandez-Ortega, 2016, Altered machinery of protein synthesis in Alzheimer’s: from the nucleolus to the ribosome, Brain Pathol., 26, 593, 10.1111/bpa.12335 · DOI · Paper page
  39. Hoozemans, 2012, Endoplasmic reticulum: the unfolded protein response is tangled in neurodegeneration, Int. J. Biochem. Cell Biol., 44, 1295, 10.1016/j.biocel.2012.04.023 · DOI
  40. Hoozemans, 2005, The unfolded protein response is activated in Alzheimer’s disease, Acta Neuropathol., 110, 165, 10.1007/s00401-005-1038-0 · DOI
  41. Huang, 2013, Inhibition of TDP-43 aggregation by nucleic acid binding, PLoS One, 8
  42. Ihara, 1988, Massive somatodendritic sprouting of cortical neurons in Alzheimer’s disease, Brain Res., 459, 138, 10.1016/0006-8993(88)90293-4 · DOI
  43. Irwin, 2015, Frontotemporal lobar degeneration: defining phenotypic diversity through personalized medicine, Acta Neuropathol., 129, 469, 10.1007/s00401-014-1380-1 · DOI
  44. Jessus, 1984, In vitro inhibition of tubulin assembly by a ribonucleoprotein complex associated with the free ribosome fraction isolated from Xenopus laevis oocytes: effect at the level of microtubule-associated proteins, Cell Differ., 14, 179, 10.1016/0045-6039(84)90044-7 · DOI
  45. Jiang, 2015, Phase transition of spindle-associated protein regulate spindle apparatus assembly, Cell., 163, 108, 10.1016/j.cell.2015.08.010 · DOI
  46. Jiang, 2019, TIA1 regulates the generation and response to toxic tau oligomers, Acta Neuropathol., 137, 259, 10.1007/s00401-018-1937-5 · DOI
  47. Kadavath, 2015, Tau stabilizes microtubules by binding at the interface between tubulin heterodimers, Proc. Natl. Acad. Sci. U. S. A., 112, 7501, 10.1073/pnas.1504081112 · DOI · Paper page
  48. Kampers, 1996, RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments, FEBS Lett., 399, 344, 10.1016/S0014-5793(96)01386-5 · DOI · Paper page
  49. Kobayashi, 2017, Local Somatodendritic translation and hyperphosphorylation of tau protein triggered by AMPA and NMDA receptor stimulation, EBioMedicine., 20, 120, 10.1016/j.ebiom.2017.05.012 · DOI
  50. Koren, 2019, Proteomic techniques to examine neuronal translational dynamics, Int. J. Mol. Sci., 20, 10.3390/ijms20143524 · DOI
  51. Kosik, 1989, Tau in situ hybridization in normal and Alzheimer brain: localization in the somatodendritic compartment, Ann. Neurol., 26, 352, 10.1002/ana.410260308 · DOI
  52. Langstrom, 1989, Alzheimer’s disease-associated reduction of polysomal mRNA translation, Brain Res. Mol. Brain Res., 5, 259, 10.1016/0169-328X(89)90060-0 · DOI
  53. Lanzillotta, 2018, Early and selective activation and subsequent alterations to the unfolded protein response in down syndrome mouse models, J. Alzheimers Dis., 62, 347, 10.3233/JAD-170617 · DOI
  54. Li, 2017, Somatodendritic accumulation of tau in Alzheimer’s disease is promoted by Fyn-mediated local protein translation, EMBO J., 36, 3120, 10.15252/embj.201797724 · DOI
  55. Li, 2004, Phosphorylated eukaryotic translation factor 4E is elevated in Alzheimer brain, Neuroreport., 15, 2237, 10.1097/00001756-200410050-00019 · DOI · Paper page
  56. Lin, 2019, Narrow equilibrium window for complex coacervation of tau and RNA under cellular conditions, Elife., 8, 10.7554/eLife.42571 · DOI
  57. Loomis, 1990, Identification of nuclear tau isoforms in human neuroblastoma cells, Proc. Natl. Acad. Sci. U. S. A., 87, 8422, 10.1073/pnas.87.21.8422 · DOI
  58. Mackenzie, 2016, Molecular neuropathology of frontotemporal dementia: insights into disease mechanisms from postmortem studies, J. Neurochem., 138, 54, 10.1111/jnc.13588 · DOI
  59. Mackenzie, 2010, TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia, Lancet Neurol., 9, 995, 10.1016/S1474-4422(10)70195-2 · DOI
  60. Maina, 2018, The involvement of Abeta42 and tau in nucleolar and protein synthesis machinery dysfunction, Front. Cell. Neurosci., 12, 220, 10.3389/fncel.2018.00220 · DOI
  61. Maina, 2018, The involvement of tau in nucleolar transcription and the stress response, Acta Neuropathol. Commun., 6, 70, 10.1186/s40478-018-0565-6 · DOI
  62. Mann, 1978, The quantitative assessment of lipofuscin pigment, cytoplasmic RNA and nucleolar volume in senile dementia, Neuropathol. Appl. Neurobiol., 4, 129, 10.1111/j.1365-2990.1978.tb00553.x · DOI
  63. Mann, 1977, Cytophotometric mapping of neuronal changes in senile dementia, J. Neurol. Neurosurg. Psychiatry, 40, 299, 10.1136/jnnp.40.3.299 · DOI
  64. Mann, 1981, Alterations in protein synthetic capability of nerve cells in Alzheimer’s disease, J. Neurol. Neurosurg. Psychiatry, 44, 97, 10.1136/jnnp.44.2.97 · DOI
  65. Mann, 1981, Neurofibrillary pathology and protein synthetic capability in nerve cells in Alzheimer’s disease, Neuropathol. Appl. Neurobiol., 7, 37, 10.1111/j.1365-2990.1981.tb00230.x · DOI
  66. Marotta, 1989, Molecular biology in psychiatric research: Alzheimer’s disease as a paradigm, Am. J. Orthop., 59, 294, 10.1111/j.1939-0025.1989.tb01662.x · DOI
  67. Marotta, 1981, In vitro synthesis of human brain proteins including tubulin and actin by purified postmortem polysomes, J. Neurochem., 36, 966, 10.1111/j.1471-4159.1981.tb01688.x · DOI
  68. Marotta, 1986, Transcriptional and translational regulatory mechanisms during normal aging of the mammalian brain and in Alzheimer’s disease, Prog. Brain Res., 70, 303, 10.1016/S0079-6123(08)64312-5 · DOI
  69. Meier, 2015, Identification of novel tau interactions with endoplasmic reticulum proteins in Alzheimer’s disease brain, J. Alzheimers Dis., 48, 687, 10.3233/JAD-150298 · DOI
  70. Metuzals, 1988, Paired helical filaments and the cytoplasmic-nuclear interface in Alzheimer’s disease, J. Neurocytol., 17, 827, 10.1007/BF01216709 · DOI
  71. Meyuhas, 2015, Ribosomal protein S6 phosphorylation: four decades of research, Int. Rev. Cell Mol. Biol., 320, 41, 10.1016/bs.ircmb.2015.07.006 · DOI
  72. Milovanovic, 2017, Synaptic vesicle clusters at synapses: a distinct liquid phase?, Neuron., 93, 995, 10.1016/j.neuron.2017.02.013 · DOI
  73. Milovanovic, 2018, A liquid phase of synapsin and lipid vesicles, Science., 361, 604, 10.1126/science.aat5671 · DOI
  74. Mueed, 2018, Tau and mTOR: the hotspots for multifarious diseases in Alzheimer’s development, Front. Neurosci., 12, 1017, 10.3389/fnins.2018.01017 · DOI · Paper page
  75. Neary, 1986, Alzheimer’s disease: a correlative study, J. Neurol. Neurosurg. Psychiatry, 49, 229, 10.1136/jnnp.49.3.229 · DOI
  76. Nelson, 1995, Ultrastructure of neurofibrillary tangles in the cerebral cortex of sheep, Neurobiol. Aging, 16, 315, 10.1016/0197-4580(94)00175-Z · DOI
  77. Nelson, 1993, Alz-50 immunohistochemistry in the normal sheep striatum: a light and electron microscope study, Brain Res., 600, 285, 10.1016/0006-8993(93)91385-6 · DOI
  78. Nijholt, 2012, The unfolded protein response is associated with early tau pathology in the hippocampus of tauopathies, J. Pathol., 226, 693, 10.1002/path.3969 · DOI
  79. Nunomura, 1999, RNA oxidation is a prominent feature of vulnerable neurons in Alzheimer’s disease, J. Neurosci., 19, 1959, 10.1523/JNEUROSCI.19-06-01959.1999 · DOI
  80. Nygard, 1990, Kinetic determination of the effects of ADP-ribosylation on the interaction of eukaryotic elongation factor 2 with ribosomes, J. Biol. Chem., 265, 6030, 10.1016/S0021-9258(19)39286-5 · DOI
  81. Ohno, 2014, Roles of eIF2alpha kinases in the pathogenesis of Alzheimer’s disease, Front. Mol. Neurosci., 7, 22, 10.3389/fnmol.2014.00022 · DOI
  82. Oliveira, 2017, Protein phosphorylation is a key mechanism in Alzheimer’s disease, J. Alzheimers Dis., 58, 953, 10.3233/JAD-170176 · DOI
  83. Papanikolopoulou, 2019, Drosophila tau negatively regulates translation and olfactory long-term memory, but facilitates footshock habituation and cytoskeletal homeostasis, J. Neurosci., 39, 8315, 10.1523/JNEUROSCI.0391-19.2019 · DOI
  84. Patel, 2015, A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation, Cell., 162, 1066, 10.1016/j.cell.2015.07.047 · DOI
  85. Peng, 1986, Biochemical and immunological analyses of cytoskeletal domains of neurons, J. Cell Biol., 102, 252, 10.1083/jcb.102.1.252 · DOI
  86. Piao, 2002, Cerebellar cortical tau pathology in progressive supranuclear palsy and corticobasal degeneration, Acta Neuropathol., 103, 469, 10.1007/s00401-001-0488-2 · DOI
  87. Piatnitskaia, 2019, USP10 is a critical factor for tau-positive stress granule formation in neuronal cells, Sci. Rep., 9, 10591, 10.1038/s41598-019-47033-7 · DOI
  88. Pietrzak, 2011, Epigenetic silencing of nucleolar rRNA genes in Alzheimer’s disease, PLoS One, 6, 10.1371/journal.pone.0022585 · DOI · Paper page
  89. Pitera, 2019, Pathogenic tau does not drive activation of the unfolded protein response, J. Biol. Chem., 294, 9679, 10.1074/jbc.RA119.008263 · DOI
  90. Radford, 2015, PERK inhibition prevents tau-mediated neurodegeneration in a mouse model of frontotemporal dementia, Acta Neuropathol., 130, 633, 10.1007/s00401-015-1487-z · DOI
  91. Roux, 2007, RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation, J. Biol. Chem., 282, 14056, 10.1074/jbc.M700906200 · DOI · Paper page
  92. Sajdel-Sulkowska, 1984, Alzheimer’s disease brain: alterations in RNA levels and in a ribonuclease-inhibitor complex, Science., 225, 947, 10.1126/science.6206567 · DOI
  93. Schroder, 1984, Binding of polyribonucleotides and polydeoxyribonucleotides to bovine brain microtubule protein: age-dependent modulation via phosphorylation of high-molecular-weight microtubule-associated proteins and tau proteins, Mech. Ageing Dev., 24, 101, 10.1016/0047-6374(84)90178-7 · DOI
  94. Shi, 2017, Heterogeneous ribosomes preferentially translate distinct subpools of mRNAs genome-wide, Mol. Cell, 67
  95. Shigeoka, 2019, On-site ribosome remodeling by locally synthesized ribosomal proteins in axons, Cell Rep., 29
  96. Sotiropoulos, 2017, Atypical, non-standard functions of the microtubule associated tau protein, Acta Neuropathol. Commun., 5, 91, 10.1186/s40478-017-0489-6 · DOI
  97. Thompson, 2012, Analysis of the tau-associated proteome reveals that exchange of Hsp70 for Hsp90 is involved in tau degradation, ACS Chem. Biol., 7, 1677, 10.1021/cb3002599 · DOI
  98. Ukmar-Godec, 2019, Lysine/RNA-interactions drive and regulate biomolecular condensation, Nat. Commun., 10, 2909, 10.1038/s41467-019-10792-y · DOI
  99. Ukmar-Godec, 2020, Biomolecular condensation of the microtubule-associated protein tau, Semin. Cell Dev. Biol., 99, 202, 10.1016/j.semcdb.2019.06.007 · DOI
  100. Vanderweyde, 2012, Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies, J. Neurosci., 32, 8270, 10.1523/JNEUROSCI.1592-12.2012 · DOI
  101. Vanderweyde, 2016, Interaction of tau with the RNA-binding protein TIA1 regulates tau pathophysiology and toxicity, Cell Rep., 15, 1455, 10.1016/j.celrep.2016.04.045 · DOI
  102. Wang, 2006, The proline-rich domain and the microtubule binding domain of protein tau acting as RNA binding domains, Protein Pept. Lett., 13, 679, 10.2174/092986606777790566 · DOI
  103. Wegmann, 2018, Tau protein liquid-liquid phase separation can initiate tau aggregation, EMBO J., 37, 10.15252/embj.201798049 · DOI · Paper page
  104. 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
  105. Wheeler, 2019, Activity of the poly(a) binding protein MSUT2 determines susceptibility to pathological tau in the mammalian brain, Sci. Transl. Med., 11, 10.1126/scitranslmed.aao6545 · DOI
  106. Willi, 2018, Oxidative stress damages rRNA inside the ribosome and differentially affects the catalytic center, Nucleic Acids Res., 46, 1945, 10.1093/nar/gkx1308 · DOI
  107. Wolozin, 2012, Regulated protein aggregation: stress granules and neurodegeneration, Mol. Neurodegener., 7, 56, 10.1186/1750-1326-7-56 · DOI
  108. Wolozin, 2019, Stress granules and neurodegeneration, Nat. Rev. Neurosci., 20, 649, 10.1038/s41583-019-0222-5 · DOI · Paper page
  109. Yamashita, 2008, Comprehensive detection of human terminal oligo-pyrimidine (TOP) genes and analysis of their characteristics, Nucleic Acids Res., 36, 3707, 10.1093/nar/gkn248 · DOI
  110. Zacco, 2019, RNA as a key factor in driving or preventing self-assembly of the TAR DNA-binding protein 43, J. Mol. Biol., 431, 1671, 10.1016/j.jmb.2019.01.028 · DOI
  111. Zeng, 2016, Phase transition in postsynaptic densities underlies formation of synaptic complexes and synaptic plasticity, Cell., 166
  112. Zhang, 2017, RNA stores tau reversibly in complex coacervates, PLoS Biol., 15, 10.1371/journal.pbio.2002183 · DOI

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Authors
Koren, S. A., Galvis-Escobar, S., & Abisambra, J. F.
Venue
Neurobiology of Disease
Publisher
Elsevier BV
Published
2020-07
Volume
141
Pages
104939
ISSN
0969-9961
Cited by
49
References
13
Language
en
Funders
National Institutes of Health

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