An Additive-Free Model for Tau Self-Assembly.
Atomic force microscopy
Circular dichroism
Cross-beta
Electron microscopy
Paired helical filament
Self-assembly
Tau
Thioflavin S fluorescence
Tyrosine fluorescence
X-ray fibre diffraction
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2023
2023
Historique:
entrez:
31
10
2022
pubmed:
1
11
2022
medline:
2
11
2022
Statut:
ppublish
Résumé
Tau is a natively unfolded protein that contributes to the stability of microtubules. Under pathological conditions such as Alzheimer's disease (AD), tau protein misfolds and self-assembles to form paired helical filaments (PHFs) and straight filaments (SFs). Full-length tau protein assembles poorly and its self-assembly is enhanced with polyanions such as heparin and RNA in vitro, but a role for heparin or other polyanions in vivo remains unclear. Recently, a truncated form of tau (297-391) has been shown to self-assemble in the absence of additives which provides an alternative in vitro PHF model system. Here we describe methods to prepare in vitro PHFs and SFs from tau (297-391) named dGAE. We also discuss the range of biophysical/biochemical techniques used to monitor tau filament assembly and structure.
Identifiants
pubmed: 36310203
doi: 10.1007/978-1-0716-2597-2_12
doi:
Substances chimiques
tau Proteins
0
polyanions
0
Heparin
9005-49-6
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
163-188Informations de copyright
© 2023. Springer Science+Business Media, LLC, part of Springer Nature.
Références
Weingarten MD, Lockwood AH, Hwo SY et al (1975) A protein factor essential for microtubule assembly. Proc Natl Acad Sci U S A 72(5):1858–1862. https://doi.org/10.1073/pnas.72.5.1858
doi: 10.1073/pnas.72.5.1858
pubmed: 1057175
pmcid: 432646
Mukrasch MD, Bibow S, Korukottu J et al (2009) Structural polymorphism of 441-residue tau at single residue resolution. PLoS Biol 7(2):e34. https://doi.org/10.1371/journal.pbio.1000034
doi: 10.1371/journal.pbio.1000034
pubmed: 19226187
Wang Y, Mandelkow E (2016) Tau in physiology and pathology. Nat Rev Neurosci 17(1):5–21. https://doi.org/10.1038/nrn.2015.1
doi: 10.1038/nrn.2015.1
pubmed: 26631930
Goedert M, Spillantini MG, Jakes R et al (1989) Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer’s disease. Neuron 3(4):519–526. https://doi.org/10.1016/0896-6273(89)90210-9
doi: 10.1016/0896-6273(89)90210-9
pubmed: 2484340
Fichou Y, Al-Hilaly YK, Devred F et al (2019) The elusive tau molecular structures: can we translate the recent breakthroughs into new targets for intervention? Acta Neuropathol Commun 7(1):31. https://doi.org/10.1186/s40478-019-0682-x
doi: 10.1186/s40478-019-0682-x
pubmed: 30823892
pmcid: 6397507
Bukar Maina M, Al-Hilaly YK, Serpell LC (2016) Nuclear tau and its potential role in Alzheimer’s disease. Biomol Ther 6(1):9. https://doi.org/10.3390/biom6010009
doi: 10.3390/biom6010009
Kimura T, Sharma G, Ishiguro K et al (2018) Phospho-tau bar code: analysis of phosphoisotypes of tau and its application to tauopathy. Front Neurosci 12:44. https://doi.org/10.3389/fnins.2018.00044
doi: 10.3389/fnins.2018.00044
pubmed: 29467609
pmcid: 5808175
Iqbal K, Liu F, Gong CX et al (2010) Tau in Alzheimer disease and related tauopathies. Curr Alzheimer Res 7(8):656–664. https://doi.org/10.2174/156720510793611592
doi: 10.2174/156720510793611592
pubmed: 20678074
pmcid: 3090074
Wischik CM, Novak M, Thogersen HC et al (1988) Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease. Proc Natl Acad Sci U S A 85(12):4506–4510. https://doi.org/10.1073/pnas.85.12.4506
doi: 10.1073/pnas.85.12.4506
pubmed: 3132715
pmcid: 280459
Goedert M (1993) Tau protein and the neurofibrillary pathology of Alzheimer’s disease. Trends Neurosci 16(11):460–465. https://doi.org/10.1016/0166-2236(93)90078-z
doi: 10.1016/0166-2236(93)90078-z
pubmed: 7507619
Berriman J, Serpell LC, Oberg KA et al (2003) Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure. Proc Natl Acad Sci U S A 100(15):9034–9038
doi: 10.1073/pnas.1530287100
pubmed: 12853572
pmcid: 166433
Fitzpatrick AWP, Falcon B, He S et al (2017) Cryo-EM structures of tau filaments from Alzheimer’s disease. Nature 547(7662):185–190. https://doi.org/10.1038/nature23002
doi: 10.1038/nature23002
pubmed: 28678775
pmcid: 5552202
Falcon B, Zivanov J, Zhang W et al (2019) Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules. Nature 568(7752):420–423. https://doi.org/10.1038/s41586-019-1026-5
doi: 10.1038/s41586-019-1026-5
pubmed: 30894745
pmcid: 6472968
Falcon B, Zhang W, Murzin AG et al (2018) Structures of filaments from Pick’s disease reveal a novel tau protein fold. Nature 561(7721):137–140. https://doi.org/10.1038/s41586-018-0454-y
doi: 10.1038/s41586-018-0454-y
pubmed: 30158706
pmcid: 6204212
Perez M, Valpuesta JM, Medina M et al (1996) Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau-tau interaction. J Neurochem 67(3):1183–1190. https://doi.org/10.1046/j.1471-4159.1996.67031183.x
doi: 10.1046/j.1471-4159.1996.67031183.x
pubmed: 8752125
Kampers T, Friedhoff P, Biernat J et al (1996) RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett 399(3):344–349. https://doi.org/10.1016/s0014-5793(96)01386-5
doi: 10.1016/s0014-5793(96)01386-5
pubmed: 8985176
Dregni AJ, Mandala VS, Wu H et al (2019) In vitro 0N4R tau fibrils contain a monomorphic β-sheet core enclosed by dynamically heterogeneous fuzzy coat segments. Proc Natl Acad Sci U S A 116(33):16357. https://doi.org/10.1073/pnas.1906839116
doi: 10.1073/pnas.1906839116
pubmed: 31358628
pmcid: 6697781
Zhang W, Falcon B, Murzin AG et al (2019) Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer’s and Pick’s diseases. elife 8:e43584. https://doi.org/10.7554/eLife.43584
doi: 10.7554/eLife.43584
pubmed: 30720432
pmcid: 6375701
Fichou Y, Vigers M, Goring AK et al (2018) Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer’s disease filaments. Chem Commun 54(36):4573–4576. https://doi.org/10.1039/c8cc01355a
doi: 10.1039/c8cc01355a
Al-Hilaly YK, Foster BE, Biasetti L et al (2020) Tau (297-391) forms filaments that structurally mimic the core of paired helical filaments in Alzheimer’s disease brain. FEBS Lett 594(5):944–950. https://doi.org/10.1002/1873-3468.13675
doi: 10.1002/1873-3468.13675
pubmed: 31721178
Al-Hilaly YK, Pollack SJ, Vadukul DM et al (2017) Alzheimer’s disease-like paired helical filament assembly from truncated tau protein is independent of disulfide crosslinking. J Mol Biol 429(23):3650–3665. https://doi.org/10.1016/j.jmb.2017.09.007
doi: 10.1016/j.jmb.2017.09.007
pubmed: 28919235
Lövestam S et al (2022) Assembly of recombinant tau into filaments identical to those of Alzheimer’s disease and chronic traumatic encephalopathy. eLife, 11: p. e76494
Lutter L et al (2022) Structural Identification of Individual Helical Amyloid Filaments by Integration of Cryo-Electron Microscopy-Derived Maps in Comparative Morphometric Atomic Force Microscopy Image Analysis. Journal of Molecular Biology, 434(7): p. 167466
Vadukul DM, Al-Hilaly YK, Serpell LC (2019) Methods for structural analysis of amyloid fibrils in Misfolding diseases. Methods Mol Biol 1873:109–122. https://doi.org/10.1007/978-1-4939-8820-4_7
doi: 10.1007/978-1-4939-8820-4_7
pubmed: 30341606
Rickard JE, Horsley D, Wischik CM et al (2017) Assays for the screening and characterization of tau aggregation inhibitors. Methods Mol Biol 1523:129–140. https://doi.org/10.1007/978-1-4939-6598-4_8
doi: 10.1007/978-1-4939-6598-4_8
pubmed: 27975248
Novak M, Kabat J, Wischik CM (1993) Molecular characterization of the minimal protease resistant tau unit of the Alzheimer’s disease paired helical filament. EMBO J 12(1):365–370
doi: 10.1002/j.1460-2075.1993.tb05665.x
pubmed: 7679073
pmcid: 413214
Novak M, Jakes R, Edwards PC et al (1991) Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51. Proc Natl Acad Sci U S A 88(13):5837–5841. https://doi.org/10.1073/pnas.88.13.5837
doi: 10.1073/pnas.88.13.5837
pubmed: 1712107
pmcid: 51973
Leslie AGW (1992) Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 + ESF-EAMCB Newsletter on Protein Crystallography 26
Zibaee S, Makin OS, Goedert M et al (2007) A simple algorithm locates beta-strands in the amyloid fibril core of alpha-synuclein, Abeta, and tau using the amino acid sequence alone. Protein Sci 16(5):906–918
doi: 10.1110/ps.062624507
pubmed: 17456743
pmcid: 2206631
Makin OS, Atkins E, Sikorski P et al (2005) Molecular basis for amyloid fibril formation and stability. Proc Natl Acad Sci U S A 102(2):315–320
doi: 10.1073/pnas.0406847102
pubmed: 15630094
pmcid: 544296
Morris KL, Serpell LC (2012) X-ray fibre diffraction studies of amyloid fibrils. Methods Mol Biol 849:121–135. https://doi.org/10.1007/978-1-61779-551-0_9
doi: 10.1007/978-1-61779-551-0_9
pubmed: 22528087
Makin OS, Serpell LC (2005) X-ray diffraction studies of amyloid structure. Methods Mol Biol 299:67–80
pubmed: 15980596