NATURE

TAF15 amyloid filaments in frontotemporal lobar degeneration

  • Grossman, M. et al. Frontotemporal lobar degeneration. Nat. Rev. Dis. Primers 9, 40 (2023).

    PubMed 

    Google Scholar
     

  • Neumann, M. & Mackenzie, I. R. A. Review: neuropathology of non-tau frontotemporal lobar degeneration. Neuropath. Appl. Neurobiol. 45, 19–40 (2019).

    CAS 

    Google Scholar
     

  • Shi, Y. et al. Structure-based classification of tauopathies. Nature 598, 359–363 (2021).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Arseni, D. et al. TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP. Nature 620, 898–903 (2023).

  • Arseni, D. et al. Structure of pathological TDP-43 filaments from ALS with FTLD. Nature 601, 139–143 (2022).

    ADS 
    CAS 
    PubMed 

    Google Scholar
     

  • Borroni, B. et al. Mutation within TARDBP leads to frontotemporal dementia without motor neuron disease. Hum. Mutat. 30, E974–E983 (2009).

    CAS 
    PubMed 

    Google Scholar
     

  • Kovacs, G. G. et al. TARDBP variation associated with frontotemporal dementia, supranuclear gaze palsy, and chorea. Mov. Disord. 24, 1842–1847 (2009).


    Google Scholar
     

  • Hutton, M. et al. Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393, 702–705 (1998).

    ADS 
    CAS 
    PubMed 

    Google Scholar
     

  • Poorkaj, P. et al. Tau is a candidate gene for chromosome 17 frontotemporal dementia. Ann. Neurol. 43, 815–825 (1998).

    CAS 
    PubMed 

    Google Scholar
     

  • Spillantini, M. G. et al. Mutation in the tau gene in familial multiple system tauopathy with presenile dementia. Proc. Natl Acad. Sci. USA 95, 7737–7741 (1998).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Lashley, T., Rohrer, J. D., Mead, S. & Revesz, T. An update on clinical, genetic and pathological aspects of frontotemporal lobar degenerations. Neuropath. Appl. Neurobiol. 41, 858–881 (2015).


    Google Scholar
     

  • Neumann, M. et al. A new subtype of frontotemporal lobar degeneration with FUS pathology. Brain 132, 2922–2931 (2009).

    PubMed 
    PubMed Central 

    Google Scholar
     

  • Neumann, M. et al. Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease. Acta Neuropathol. 118, 605–616 (2009).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Munoz, D. G. et al. FUS pathology in basophilic inclusion body disease. Acta Neuropathol. 118, 617–627 (2009).

    CAS 
    PubMed 

    Google Scholar
     

  • Lashley, T. et al. A comparative clinical, pathological, biochemical and genetic study of fused in sarcoma proteinopathies. Brain 134, 2548–2564 (2011).

    PubMed 
    PubMed Central 

    Google Scholar
     

  • Kwiatkowski, T. J. et al. Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323, 1205–1208 (2009).

    ADS 
    CAS 
    PubMed 

    Google Scholar
     

  • Vance, C. et al. Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323, 1208–1211 (2009).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Murray, D. T. et al. Structure of FUS protein fibrils and its relevance to self-assembly and phase separation of low-complexity domains. Cell 171, 615–627 (2017).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Lee, M., Ghosh, U., Thurber, K. R., Kato, M. & Tycko, R. Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS. Nat. Commun. 11, 5735 (2020).

    ADS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Sun, Y. et al. Molecular structure of an amyloid fibril formed by FUS low-complexity domain. iScience 25, 103701 (2022).

    ADS 
    CAS 
    PubMed 

    Google Scholar
     

  • Langenhove, T. V. et al. Genetic contribution of FUS to frontotemporal lobar degeneration. Neurology 74, 366–371 (2010).

    PubMed 

    Google Scholar
     

  • Snowden, J. S. et al. The most common type of FTLD-FUS (aFTLD-U) is associated with a distinct clinical form of frontotemporal dementia but is not related to mutations in the FUS gene. Acta Neuropathol. 122, 99–110 (2011).

    CAS 
    PubMed 

    Google Scholar
     

  • Neumann, M. et al. FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations. Brain 134, 2595–2609 (2011).

    PubMed 
    PubMed Central 

    Google Scholar
     

  • Brelstaff, J. et al. Transportin1: a marker of FTLD-FUS. Acta Neuropathol. 122, 591–600 (2011).

    CAS 
    PubMed 

    Google Scholar
     

  • Neumann, M. et al. Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations. Acta Neuropathol. 124, 705–716 (2012).

    CAS 
    PubMed 

    Google Scholar
     

  • Davidson, Y. S. et al. Nuclear carrier and RNA-binding proteins in frontotemporal lobar degeneration associated with fused in sarcoma (FUS) pathological changes. Neuropathol. Appl. Neurobiol. 39, 157–165 (2013).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Gami-Patel, P., Bandopadhyay, R., Brelstaff, J., Revesz, T. & Lashley, T. The presence of heterogeneous nuclear ribonucleoproteins in frontotemporal lobar degeneration with FUS-positive inclusions. Neurobiol. Aging 46, 192–203 (2016).

    CAS 
    PubMed 

    Google Scholar
     

  • Schwartz, J. C., Cech, T. R. & Parker, R. R. Biochemical properties and biological functions of FET proteins. Annu. Rev. Biochem. 84, 355–379 (2015).

    CAS 
    PubMed 

    Google Scholar
     

  • Couthouis, J. et al. A yeast functional screen predicts new candidate ALS disease genes. Proc. Natl Acad. Sci. USA 108, 20881–20890 (2011).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Couthouis, J. et al. Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis. Hum. Mol. Genet. 21, 2899–2911 (2012).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Kwon, I. et al. Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains. Cell 155, 1049–1060 (2013).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Chen, J. et al. The SGYS motif of TAF15 prion-like domain is critical to amyloid fibril formation. Biophys. J. 121, 2613–2623 (2022).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Lee, B. J. et al. Rules for nuclear localization sequence recognition by karyopherinβ2. Cell 126, 543–558 (2006).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Murray, K. A. et al. De novo designed protein inhibitors of amyloid aggregation and seeding. Proc. Natl Acad. Sci. USA 119, e2206240119 (2022).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Seidler, P. M. et al. Structure-based discovery of small molecules that disaggregate Alzheimer’s disease tissue derived tau fibrils in vitro. Nat. Commun. 13, 5451 (2022).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Schweighauser, M. et al. Structures of α-synuclein filaments from multiple system atrophy. Nature 585, 464–469 (2020).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Yang, Y. et al. Cryo-EM structures of amyloid-β 42 filaments from human brains. Science 375, 167–172 (2022).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Schweighauser, M. et al. Age-dependent formation of TMEM106B amyloid filaments in human brains. Nature 605, 310–314 (2022).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Chang, A. et al. Homotypic fibrillization of TMEM106B across diverse neurodegenerative diseases. Cell 185, 1346–1355 (2022).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Jiang, Y. X. et al. Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43. Nature 605, 304–309 (2022).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Perneel, J. et al. Accumulation of TMEM106B C-terminal fragments in neurodegenerative disease and aging. Acta Neuropathol. 145, 285–302 (2022).

    PubMed 

    Google Scholar
     

  • Fan, Y. et al. Generic amyloid fibrillation of TMEM106B in patient with Parkinson’s disease dementia and normal elders. Cell Res. 32, 585–588 (2022).

    PubMed 
    PubMed Central 

    Google Scholar
     

  • Scheres, S. H. W. Amyloid structure determination in RELION-3.1. Acta Crystallogr. D Struct. Biol. 76, 94–101 (2020).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Jahn, T. R. et al. The common architecture of cross-β amyloid. J. Mol. Biol. 395, 717–727 (2010).

    CAS 
    PubMed 

    Google Scholar
     

  • Scheres, S. H. W., Ryskeldi-Falcon, B. & Goedert, M. Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids. Nature 621, 701–710 (2023).

    ADS 
    CAS 
    PubMed 

    Google Scholar
     

  • Falcon, B. et al. Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules. Nature 568, 420–423 (2019).

    ADS 
    CAS 
    PubMed Central 

    Google Scholar
     

  • Laferrière, F. et al. TDP-43 extracted from frontotemporal lobar degeneration subject brains displays distinct aggregate assemblies and neurotoxic effects reflecting disease progression rates. Nat. Neurosci. 22, 65–77 (2019).

    PubMed 

    Google Scholar
     

  • Takeuchi, R. et al. Transportin 1 accumulates in FUS inclusions in adult-onset ALS without FUS mutation. Neuropath. Appl. Neurobiol. 39, 580–584 (2013).

    CAS 

    Google Scholar
     

  • Borrego-Écija, S. et al. Does ALS-FUS without FUS mutation represent ALS-FET? Report of three cases. Neuropathol. Appl. Neurobiol. 45, 421–426 (2019).

    PubMed 

    Google Scholar
     

  • Ticozzi, N. et al. Mutational analysis reveals the FUS homolog TAF15 as a candidate gene for familial amyotrophic lateral sclerosis. Am. J. Med. Genet. B Neuropsychiatr. Genet. 156, 285–290 (2011).

    CAS 

    Google Scholar
     

  • Van Daele, S. H. et al. Genetic variability in sporadic amyotrophic lateral sclerosis. Brain 146, 3760–3769 (2023).

  • Dormann, D. et al. Arginine methylation next to the PY-NLS modulates transportin binding and nuclear import of FUS. EMBO J. 31, 4258–4275 (2012).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Mackenzie, I. R. A. et al. Nomenclature for neuropathologic subtypes of frontotemporal lobar degeneration: consensus recommendations. Acta Neuropathol. 117, 15–18 (2009).

    PubMed 

    Google Scholar
     

  • Renton, A. E. et al. A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron 72, 257–268 (2011).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Demichev, V., Messner, C. B., Vernardis, S. I., Lilley, K. S. & Ralser, M. DIA-NN: neural networks and interference correction enable deep proteome coverage in high throughput. Nat. Methods 17, 41–44 (2020).

    CAS 
    PubMed 

    Google Scholar
     

  • Zivanov, J., Nakane, T. & Scheres, S. H. W. A Bayesian approach to beam-induced motion correction in cryo-EM single-particle analysis. IUCrJ 6, 5–17 (2019).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Rohou, A. & Grigorieff, N. CTFFIND4: fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216–221 (2015).

    PubMed 
    PubMed Central 

    Google Scholar
     

  • He, S. & Scheres, S. H. W. Helical reconstruction in RELION. J. Struct. Biol. 198, 163–176 (2017).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Kimanius, D., Dong, L., Sharov, G., Nakane, T. & Scheres, S. H. W. New tools for automated cryo-EM single-particle analysis in RELION-4.0. Biochem. J 478, 4169–4185 (2021).

    CAS 
    PubMed 

    Google Scholar
     

  • Zivanov, J., Nakane, T. & Scheres, S. H. W. Estimation of high-order aberrations and anisotropic magnification from cryo-EM data sets in RELION-3.1. IUCrJ 7, 253–267 (2020).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Chen, S. et al. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 135, 24–35 (2013).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Casañal, A., Lohkamp, B. & Emsley, P. Current developments in Coot for macromolecular model building of electron cryo-microscopy and crystallographic data. Protein Sci. 29, 1055–1064 (2020).


    Google Scholar
     

  • Croll, T. I. ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps. Acta Crystallogr. D Struct. Biol. 74, 519–530 (2018).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Brown, A. et al. Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions. Acta Crystallogr. D Biol. Crystallogr. 71, 136–153 (2015).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Yamashita, K., Palmer, C. M., Burnley, T. & Murshudov, G. N. Cryo-EM single-particle structure refinement and map calculation using Servalcat. Acta Crystallogr. D Struct. Biol. 77, 1282–1291 (2021).

    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Williams, C. J. et al. MolProbity: more and better reference data for improved all-atom structure validation. Protein Sci. 27, 293–315 (2018).

    CAS 
    PubMed 

    Google Scholar
     

  • Pettersen, E. F. et al. UCSF ChimeraX: structure visualization for researchers, educators, and developers. Protein Sci. 30, 70–82 (2021).

    CAS 
    PubMed 

    Google Scholar
     


  • Source link

    Back to top button