FUS and TDP-43 phases in health and disease
The distinct prion-like domains (PrLDs) of FUS and TDP-43, modulate phase transitions that
result in condensates with a range of material states. These assemblies are implicated in
both health and disease. In this review, we examine how sequence, structure, post-
translational modifications, and RNA can affect the self-assembly of these RNA-binding
proteins (RBPs). We discuss how our emerging understanding of FUS and TDP-43 liquid–
liquid phase separation (LLPS) and aggregation, could be leveraged to design new …
result in condensates with a range of material states. These assemblies are implicated in
both health and disease. In this review, we examine how sequence, structure, post-
translational modifications, and RNA can affect the self-assembly of these RNA-binding
proteins (RBPs). We discuss how our emerging understanding of FUS and TDP-43 liquid–
liquid phase separation (LLPS) and aggregation, could be leveraged to design new …
The distinct prion-like domains (PrLDs) of FUS and TDP-43, modulate phase transitions that result in condensates with a range of material states. These assemblies are implicated in both health and disease. In this review, we examine how sequence, structure, post-translational modifications, and RNA can affect the self-assembly of these RNA-binding proteins (RBPs). We discuss how our emerging understanding of FUS and TDP-43 liquid–liquid phase separation (LLPS) and aggregation, could be leveraged to design new therapies for neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and limbic-predominant age-related TDP-43 encephalopathy (LATE).
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