Stress granules (SGs) are a type of biomolecular condensate that consist of membraneless compartments formed in cells through liquid–liquid phase separation (LLPS). They have been shown to concentrate proteins such as RNA-binding proteins (RBPs) to enable biochemical reactions. When cells are exposed to acute biotic and abiotic stress, nuclear RBPs translocate to the cytoplasm and nucleate to form SGs and promote cell survival. Mutations in SG proteins, including TIA1, FUS, TDP43, and hnRNPA1, have been observed in neurodegenerative disorders such as Alzheimer’s disease, Parkinson’s disease, amyotrophic lateral sclerosis (ALS), and frontotemporal dementia (FTD), indicating a potential link between the mechanisms that regulate LLPS and disease progression. Studies suggest that the SG liquid–liquid state undergoes an aberrant phase transition to a more solid-like state, potentially leading to the formation of tau and other protein aggregates. Thus, further understanding of the mechanisms that control LLPS, such as nucleocytoplasmic transport or posttranslational modification, presents a new paradigm for aggregate formation that can lead to new, transformative therapeutics.
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