期刊
DEVELOPMENTAL CELL
卷 55, 期 1, 页码 45-68出版社
CELL PRESS
DOI: 10.1016/j.devcel.2020.09.014
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资金
- Swiss National Science Foundation (SNSF) [CRSII5_170976 11]
- Swiss National Science Foundation (SNF) [CRSII5_170976] Funding Source: Swiss National Science Foundation (SNF)
Protein aggregation is the main hallmark of neurodegenerative diseases. Many proteins found in pathological inclusions are known to undergo liquid-liquid phase separation, a reversible process of molecular self-assembly. Emerging evidence supports the hypothesis that aberrant phase separation behavior may serve as a trigger of protein aggregation in neurodegeneration, and efforts to understand and control the underlying mechanisms are underway. Here, we review similarities and differences among four main proteins, alpha-synuclein, FUS, tau, and TDP-43, which are found aggregated in different diseases and were independently shown to phase separate. We discuss future directions in the field that will help shed light on the molecular mechanisms of aggregation and neurodegeneration.
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