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Tau aggregates are RNA-protein assemblies that mislocalize multiple nuclear speckle components

Lester, Evan, Ooi, Felicia K., Bakkar, Nadine, Ayers, Jacob, Woerman, Amanda L., Wheeler, Joshua, Bowser, Robert, Carlson, George A., Prusiner, Stanley B., Parker, Roy·2021·Neuron
DOI 10.1016/j.neuron.2021.03.026PMC PMC8141031

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  1. Allen, 2002, Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein, J. Neurosci., 22, 9340, 10.1523/JNEUROSCI.22-21-09340.2002 · DOI
  2. Aoyagi, 2019, Aβ and tau prion-like activities decline with longevity in the Alzheimer’s disease human brain, Sci. Transl. Med., 11, eaat8462, 10.1126/scitranslmed.aat8462 · DOI
  3. Apicco, 2019, Dysregulation of RNA Splicing in Tauopathies, Cell Rep., 29, 4377, 10.1016/j.celrep.2019.11.093 · DOI
  4. Bengoa-Vergniory, 2021, Tau-proximity ligation assay reveals extensive previously undetected pathology prior to neurofibrillary tangles in preclinical Alzheimer’s disease, Acta Neuropathol. Commun., 9, 18, 10.1186/s40478-020-01117-y · DOI
  5. Berg, 2019, ilastik: interactive machine learning for (bio)image analysis, Nat. Methods, 16, 1226, 10.1038/s41592-019-0582-9 · DOI
  6. Brady, 1995, Presence of tau in isolated nuclei from human brain, Neurobiol. Aging, 16, 479, 10.1016/0197-4580(95)00023-8 · DOI
  7. Brandt, 1995, Interaction of tau with the neural plasma membrane mediated by tau’s amino-terminal projection domain, J. Cell Biol., 131, 1327, 10.1083/jcb.131.5.1327 · DOI
  8. Broccolini, 2000, Paired helical filaments of inclusion-body myositis muscle contain RNA and survival motor neuron protein, Am. J. Pathol., 156, 1151, 10.1016/S0002-9440(10)64983-8 · DOI
  9. Buée, 2000, Tau protein isoforms, phosphorylation and role in neurodegenerative disorders, Brain Res. Brain Res. Rev., 33, 95, 10.1016/S0165-0173(00)00019-9 · DOI
  10. Burke, 2019, RNase L Reprograms Translation by Widespread mRNA Turnover Escaped by Antiviral mRNAs, Mol. Cell, 75, 1203, 10.1016/j.molcel.2019.07.029 · DOI
  11. Campeau, 2009, A versatile viral system for expression and depletion of proteins in mammalian cells, PLoS ONE, 4, e6529, 10.1371/journal.pone.0006529 · DOI
  12. Chen, 1992, Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons, Nature, 360, 674, 10.1038/360674a0 · DOI · Paper page
  13. Criscione, 2014, Transcriptional landscape of repetitive elements in normal and cancer human cells, BMC Genomics, 15, 583, 10.1186/1471-2164-15-583 · DOI
  14. Delaval, 2010, Pericentrin in cellular function and disease, J. Cell Biol., 188, 181, 10.1083/jcb.200908114 · DOI
  15. DeVos, 2018, Tau reduction in the presence of amyloid-β prevents tau pathology and neuronal death in vivo, Brain, 141, 2194, 10.1093/brain/awy117 · DOI · Paper page
  16. Diner, 2017, Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain, J. Vis. Exp.
  17. 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
  18. Dinkel, 2015, RNA Binds to Tau Fibrils and Sustains Template-Assisted Growth, Biochemistry, 54, 4731, 10.1021/acs.biochem.5b00453 · DOI
  19. Dobin, 2013, STAR: ultrafast universal RNA-seq aligner, Bioinformatics, 29, 15, 10.1093/bioinformatics/bts635 · DOI · Paper page
  20. Falcon, 2018, Structures of filaments from Pick’s disease reveal a novel tau protein fold, Nature, 561, 137, 10.1038/s41586-018-0454-y · DOI
  21. Falcon, 2019, Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules, Nature, 568, 420, 10.1038/s41586-019-1026-5 · DOI
  22. Galganski, 2017, Nuclear speckles: molecular organization, biological function and role in disease, Nucleic Acids Res., 45, 10350, 10.1093/nar/gkx759 · DOI
  23. Gärtner, 1998, Postmortem changes in the phosphorylation state of tau-protein in the rat brain, Neurobiol. Aging, 19, 535, 10.1016/S0197-4580(98)00094-3 · DOI
  24. Gaspar, 2017, Enzymatic production of single-molecule FISH and RNA capture probes, RNA, 23, 1582, 10.1261/rna.061184.117 · DOI
  25. Gil, 2017, Aging dependent effect of nuclear tau, Brain Res., 1677, 129, 10.1016/j.brainres.2017.09.030 · DOI
  26. Ginsberg, 1997, Sequestration of RNA in Alzheimer’s disease neurofibrillary tangles and senile plaques, Ann. Neurol., 41, 200, 10.1002/ana.410410211 · DOI
  27. Ginsberg, 1998, RNA sequestration to pathological lesions of neurodegenerative diseases, Acta Neuropathol., 96, 487, 10.1007/s004010050923 · DOI
  28. Goedert, 2005, Tau gene mutations and their effects, Mov. Disord., 20, S45, 10.1002/mds.20539 · DOI
  29. Goedert, 2000, Tau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer’s disease, Biochim. Biophys. Acta, 1502, 110, 10.1016/S0925-4439(00)00037-5 · DOI
  30. Grainger, 2009, Physical and genetic interactions of yeast Cwc21p, an ortholog of human SRm300/SRRM2, suggest a role at the catalytic center of the spliceosome, RNA, 15, 2161, 10.1261/rna.1908309 · DOI
  31. Graser, 2007, Cep164, a novel centriole appendage protein required for primary cilium formation, J. Cell Biol., 179, 321, 10.1083/jcb.200707181 · 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 · Paper page
  33. Guthrie, 2011, MSUT2 is a determinant of susceptibility to tau neurotoxicity, Hum. Mol. Genet., 20, 1989, 10.1093/hmg/ddr079 · DOI
  34. Hanseeuw, 2019, Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study, JAMA Neurol., 76, 915, 10.1001/jamaneurol.2019.1424 · DOI · Paper page
  35. Holmes, 2014, Proteopathic tau seeding predicts tauopathy in vivo, Proc. Natl. Acad. Sci. USA, 111, E4376, 10.1073/pnas.1411649111 · DOI · Paper page
  36. Hoover, 2010, Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration, Neuron, 68, 1067, 10.1016/j.neuron.2010.11.030 · DOI · Paper page
  37. Huang, 1994, In vivo analysis of the stability and transport of nuclear poly(A)+ RNA, J. Cell Biol., 126, 877, 10.1083/jcb.126.4.877 · DOI
  38. Ilik, 2020, SON and SRRM2 are essential for nuclear speckle formation, eLife, 9, e60579, 10.7554/eLife.60579 · DOI
  39. Jiang, 2019, TIA1 regulates the generation and response to toxic tau oligomers, Acta Neuropathol., 137, 259, 10.1007/s00401-018-1937-5 · DOI · Paper page
  40. Johnson, 2017, Evidence for sortilin modulating regional accumulation of human tau prions in transgenic mice, Proc. Natl. Acad. Sci. USA, 114, E11029, 10.1073/pnas.1717193114 · DOI
  41. 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
  42. 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
  43. Khong, 2017, The Stress Granule Transcriptome Reveals Principles of mRNA Accumulation in Stress Granules, Mol. Cell, 68, 808, 10.1016/j.molcel.2017.10.015 · DOI
  44. Kinsella, 2011, Ensembl BioMarts: a hub for data retrieval across taxonomic space, Database (Oxford), 2011, bar030, 10.1093/database/bar030 · DOI
  45. Kiss, 2002, Small nucleolar RNAs: an abundant group of noncoding RNAs with diverse cellular functions, Cell, 109, 145, 10.1016/S0092-8674(02)00718-3 · DOI
  46. Kota, 2008, Binding of ATP to UAP56 is necessary for mRNA export, J. Cell Sci., 121, 1526, 10.1242/jcs.021055 · DOI
  47. Lagier-Tourenne, 2012, Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs, Nat. Neurosci., 15, 1488, 10.1038/nn.3230 · DOI
  48. Lee, 1998, Tau interacts with src-family non-receptor tyrosine kinases, J. Cell Sci., 111, 3167, 10.1242/jcs.111.21.3167 · DOI
  49. Li, 2020, iREAD: a tool for intron retention detection from RNA-seq data, BMC Genomics, 21, 128, 10.1186/s12864-020-6541-0 · DOI
  50. Liu, 2013, Profiling murine tau with 0N, 1N and 2N isoform-specific antibodies in brain and peripheral organs reveals distinct subcellular localization, with the 1N isoform being enriched in the nucleus, PLoS ONE, 8, e84849, 10.1371/journal.pone.0084849 · DOI
  51. Love, 2014, Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2, Genome Biol., 15, 550, 10.1186/s13059-014-0550-8 · DOI · Paper page
  52. Maj, 2010, Expression of TAU in insulin-secreting cells and its interaction with the calcium-binding protein secretagogin, J. Endocrinol., 205, 25, 10.1677/JOE-09-0341 · DOI
  53. McQuin, 2018, CellProfiler 3.0: Next-generation image processing for biology, PLoS Biol., 16, e2005970, 10.1371/journal.pbio.2005970 · DOI
  54. Metuzals, 1988, Paired helical filaments and the cytoplasmic-nuclear interface in Alzheimer’s disease, J. Neurocytol., 17, 827, 10.1007/BF01216709 · DOI
  55. Montalbano, 2020, RNA-binding proteins Musashi and tau soluble aggregates initiate nuclear dysfunction, Nat. Commun., 11, 4305, 10.1038/s41467-020-18022-6 · DOI · Paper page
  56. Motameny, 2010, Next Generation Sequencing of miRNAs - Strategies, Resources and Methods, Genes (Basel), 1, 70, 10.3390/genes1010070 · DOI
  57. Orr, 2017, A Brief Overview of Tauopathy: Causes, Consequences, and Therapeutic Strategies, Trends Pharmacol. Sci., 38, 637, 10.1016/j.tips.2017.03.011 · DOI
  58. Papasozomenos, 1995, Nuclear tau immunoreactivity in presenile dementia with motor neuron disease: a case report, Clin. Neuropathol., 14, 100
  59. Park, 2016, Tau mis-splicing in the pathogenesis of neurodegenerative disorders, BMB Rep., 49, 405, 10.5483/BMBRep.2016.49.8.084 · DOI
  60. Ramaswami, 2013, Altered ribostasis: RNA-protein granules in degenerative disorders, Cell, 154, 727, 10.1016/j.cell.2013.07.038 · DOI
  61. Ramsden, 2005, Age-dependent neurofibrillary tangle formation, neuron loss, and memory impairment in a mouse model of human tauopathy (P301L), J. Neurosci., 25, 10637, 10.1523/JNEUROSCI.3279-05.2005 · DOI · Paper page
  62. Rino, 2007, A stochastic view of spliceosome assembly and recycling in the nucleus, PLoS Comput. Biol., 3, 2019, 10.1371/journal.pcbi.0030201 · DOI
  63. 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
  64. Santa-Maria, 2012, Paired helical filaments from Alzheimer disease brain induce intracellular accumulation of Tau protein in aggresomes, J. Biol. Chem., 287, 20522, 10.1074/jbc.M111.323279 · DOI
  65. Schmid-Burgk, 2016, CRISPaint allows modular base-specific gene tagging using a ligase-4-dependent mechanism, Nat. Commun., 7, 12338, 10.1038/ncomms12338 · DOI
  66. Schröder, 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
  67. Sepulveda, 2018, Co-translational protein targeting facilitates centrosomal recruitment of PCNT during centrosome maturation in vertebrates, eLife, 7, e34959, 10.7554/eLife.34959 · DOI
  68. Siano, 2019, Tau Modulates VGluT1 Expression, J. Mol. Biol., 431, 873, 10.1016/j.jmb.2019.01.023 · DOI
  69. Spector, 2011, Nuclear speckles, Cold Spring Harb. Perspect. Biol., 3, a000646, 10.1101/cshperspect.a000646 · DOI
  70. Tanaka, 2018, The intellectual disability gene PQBP1 rescues Alzheimer’s disease pathology, Mol. Psychiatry, 23, 2090, 10.1038/s41380-018-0253-8 · DOI
  71. Taylor, 2016, Decoding ALS: from genes to mechanism, Nature, 539, 197, 10.1038/nature20413 · DOI
  72. Ulrich, 2018, Phosphorylation of nuclear Tau is modulated by distinct cellular pathways, Sci. Rep., 8, 17702, 10.1038/s41598-018-36374-4 · DOI
  73. 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 · Paper page
  74. Vaquero-Garcia, 2016, A new view of transcriptome complexity and regulation through the lens of local splicing variations, eLife, 5, e11752, 10.7554/eLife.11752 · DOI · Paper page
  75. Violet, 2014, A major role for Tau in neuronal DNA and RNA protection in vivo under physiological and hyperthermic conditions, Front. Cell. Neurosci., 8, 84, 10.3389/fncel.2014.00084 · DOI · Paper page
  76. Violet, 2015, Prefibrillar Tau oligomers alter the nucleic acid protective function of Tau in hippocampal neurons in vivo, Neurobiol. Dis., 82, 540, 10.1016/j.nbd.2015.09.003 · DOI
  77. Wagner, 2004, In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160, J. Cell Biol., 164, 843, 10.1083/jcb.200307002 · DOI
  78. 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
  79. Wegmann, 2013, The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush, Proc. Natl. Acad. Sci. USA, 110, E313, 10.1073/pnas.1212100110 · DOI
  80. Wheeler, 2019, Activity of the poly(A) binding protein MSUT2 determines susceptibility to pathological tau in the mammalian brain, Sci. Transl. Med., 11, eaao6545, 10.1126/scitranslmed.aao6545 · DOI · Paper page
  81. Wingett, 2018, FastQ Screen: A tool for multi-genome mapping and quality control, F1000Res., 7, 1338, 10.12688/f1000research.15931.1 · DOI
  82. Wischik, 1988, Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease, Proc. Natl. Acad. Sci. USA, 85, 4506, 10.1073/pnas.85.12.4506 · DOI · Paper page
  83. Woerman, 2016, Tau prions from Alzheimer’s disease and chronic traumatic encephalopathy patients propagate in cultured cells, Proc. Natl. Acad. Sci. USA, 113, E8187, 10.1073/pnas.1616344113 · DOI
  84. Xu, 2019, Improved TGIRT-seq methods for comprehensive transcriptome profiling with decreased adapter dimer formation and bias correction, Sci. Rep., 9, 7953, 10.1038/s41598-019-44457-z · DOI
  85. Zhang, 2016, Coordinated dynamics of RNA splicing speckles in the nucleus, J. Cell. Physiol., 231, 1269, 10.1002/jcp.25224 · DOI
  86. Zhang, 2017, RNA stores tau reversibly in complex coacervates, PLoS Biol., 15, e2002183, 10.1371/journal.pbio.2002183 · DOI · Paper page
  87. Zhang, 2018, Structure of the human activated spliceosome in three conformational states, Cell Res., 28, 307, 10.1038/cr.2018.14 · DOI
  88. Zhang, 2020, Novel tau filament fold in corticobasal degeneration, Nature, 580, 283, 10.1038/s41586-020-2043-0 · DOI
  89. Zimowska, 2003, Pinin/DRS/memA interacts with SRp75, SRm300 and SRrp130 in corneal epithelial cells, Invest. Ophthalmol. Vis. Sci., 44, 4715, 10.1167/iovs.03-0240 · DOI

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Metadata

Authors
Lester, E., Ooi, F. K., Bakkar, N., Ayers, J., Woerman, A. L., Wheeler, J., Bowser, R., Carlson, G. A., Prusiner, S. B., & Parker, R.
Venue
Neuron
Publisher
Elsevier BV
Published
2021-05
Volume
109
Issue
10
Pages
1675-1691.e9
ISSN
0896-6273
DOI
10.1016/j.neuron.2021.03.026
PMC
PMC8141031
Cited by
232
References
15
Language
en
Licence
Funders
  • NIST (70NANB15H226)
  • Howard Hughes Medical Institute
  • National Institutes of Health (2P01AG002132-39, 1F30AG063468-01, 5R01GM045443-31, P50AG023501, P01AG019724)
  • Brockman Foundation
  • Sherman Fairchild Foundation

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