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Regulatory mechanisms of tau protein fibrillation under the conditions of liquid–liquid phase separation
Abstract
Significance: One of the major pathogenic events in Alzheimer’s disease and several other neurodegenerative disorders is the aggregation of tau protein into fibrillar structures. Recent reports demonstrated that tau can undergo liquid–liquid phase separation, forming liquid droplets. The key finding of the present study is that liquid–liquid phase separation uniquely regulates the rate of tau fibrillation in mixtures containing tau isoforms with different aggregation propensities. Given that, due to alternative splicing, the proportions of fast and slowly aggregating tau isoforms in brain vary substantially in different tauopathies, this previously unrecognized regulatory mechanism may play an important role as one of the major determinants of phenotypic variability within this class of neurodegenerative diseases.
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“as well as the de novo formation of seeding competent Tau oligomers (Wegmann et al, 2018; Boyko et al, 2020; Kanaan et al, 2020).”
From Molecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates (2022) · cites this paper as Boyko et al, 2020
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“Crowding‐induced biomolecular Tau condensates have been suggested to harbor pathological seeding potential since they can convert—at least in vitro—into oligomeric Tau species with properties similar to in vitro generated Tau aggregates (Wegmann et al, 2018; Boyko et al, 2020; Kanaan et al, 2020).”
From Molecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates (2022) · cites this paper as Boyko et al, 2020
In the citing paper
“In addition to functional MT binding and bundling, Tau condensates have also been implicated in the generation of pathological Tau species that have the ability to seed Tau aggregation (Wegmann et al, 2018; Boyko et al, 2020; Kanaan et al, 2020).”
From Molecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates (2022) · cites this paper as Boyko et al, 2020
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Cites
Structural Polymorphism of 441-Residue Tau at Single Residue Resolution
Mukrasch, M. D., Bibow, S., Korukottu, J., Jeganathan, S., Biernat, J., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000034 · Cited by 652
Microtubules gate tau condensation to spatially regulate microtubule functions
Tan, R., Lam, A. J., Tan, T., Han, J., Nowakowski, D. W., Vershinin, M., Simó, S., Ori-McKenney, K. M., & McKenney, R. J. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0375-5 · Cited by 231
Acetylation Disfavors Tau Phase Separation
Ferreon, J. C., Jain, A., Choi, K.-J., Tsoi, P. S., MacKenzie, K. R., Jung, S. Y., & Ferreon, A. C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051360 · Cited by 183
Baas, P. W., & Qiang, L. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.02.007 · Cited by 123
Tau isoform composition influences rate and extent of filament formation
Zhong, Q., Congdon, E. E., Nagaraja, H. N., & Kuret, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.364067 · Cited by 122
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Cited by
Hochmair, J., Exner, C., Franck, M., Dominguez‐Baquero, A., Diez, L., Brognaro, H., Kraushar, M. L., Mielke, T., Radbruch, H., Kaniyappan, S., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2021108882 · Cited by 106
Ainani, H., Bouchmaa, N., Ben Mrid, R., & El Fatimy, R. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106011 · Cited by 54
Liquid-liquid phase separation in Alzheimer’s disease
Fu, Q., Zhang, B., Chen, X., & Chu, L. (2024) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02407-3 · Cited by 33
Liquid − liquid phase separation of tau: Driving forces, regulation, and biological implications
Li, P., Chen, J., Wang, X., Su, Z., Gao, M., & Huang, Y. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106167 · Cited by 30
Tau liquid–liquid phase separation: At the crossroads of tau physiology and tauopathy
Islam, M., Shen, F., Regmi, D., Petersen, K., Karim, M. R. U., & Du, D. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.30853 · Cited by 28
Metadata
- Authors
- Boyko, S., Surewicz, K., & Surewicz, W. K.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2020-12
- Volume
- 117
- Issue
- 50
- Pages
- 31882-31890
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 144
- References
- 6
- Language
- en
- Funders
- HHS | NIH | National Institute on Aging (RF1 AG061797)
- HHS | NIH | NIH Office of the Director (OD024996)
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- Boyko, S., Surewicz, K., & Surewicz, W. K. (2020). Regulatory mechanisms of tau protein fibrillation under the conditions of liquid–liquid phase separation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.2012460117
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