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Review
. 2024 Sep;8(9):686-700.
doi: 10.1038/s41570-024-00635-w. Epub 2024 Aug 12.

The role of biomolecular condensates in protein aggregation

Brent S Visser  1 , Wojciech P Lipiński  1 , Evan Spruijt  2
Affiliations
Review

The role of biomolecular condensates in protein aggregation

Brent S Visser et al. Nat Rev Chem. 2024 Sep.

Abstract

There is an increasing amount of evidence that biomolecular condensates are linked to neurodegenerative diseases associated with protein aggregation, such as Alzheimer's disease and amyotrophic lateral sclerosis, although the mechanisms underlying this link remain elusive. In this Review, we summarize the possible connections between condensates and protein aggregation. We consider both liquid-to-solid transitions of phase-separated proteins and the partitioning of proteins into host condensates. We distinguish five key factors by which the physical and chemical environment of a condensate can influence protein aggregation, and we discuss their relevance in studies of protein aggregation in the presence of biomolecular condensates: increasing the local concentration of proteins, providing a distinct chemical microenvironment, introducing an interface wherein proteins can localize, changing the energy landscape of aggregation pathways, and the presence of chaperones in condensates. Analysing the role of biomolecular condensates in protein aggregation may be essential for a full understanding of amyloid formation and offers a new perspective that can help in developing new therapeutic strategies for the prevention and treatment of neurodegenerative diseases.

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References

    1. Ross, C. A. & Poirier, M. A. Protein aggregation and neurodegenerative disease. Nat. Med. 10, S10–S17 (2004). - PubMed - DOI
    1. Willbold, D., Strodel, B., Schröder, G. F., Hoyer, W. & Heise, H. Amyloid-type protein aggregation and prion-like properties of amyloids. Chem. Rev. 121, 8285–8307 (2021). - PubMed - DOI
    1. Dobson, C. M. The amyloid phenomenon and its links with human disease. Cold Spring Harb. Perspect. Biol. 9, a023648 (2017). - PubMed - PMC - DOI
    1. Emin, D. et al. Small soluble α-synuclein aggregates are the toxic species in Parkinson’s disease. Nat. Commun. 13, 5512 (2022). - PubMed - PMC - DOI
    1. Cascella, R. et al. Probing the origin of the toxicity of oligomeric aggregates of α-synuclein with antibodies. ACS Chem. Biol. 14, 1352–1362 (2019). - PubMed - PMC - DOI

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