Abstract

Prion-like domains (PrLDs) are low-complexity protein domains with compositional similarity to yeast prion domains. PrLDs are highly enriched in small and polar amino acids and therefore tend to be intrinsically disordered. They are common in eukaryotic proteomes, and mutations in these domains are linked to various degenerative disorders, including amyotrophic lateral sclerosis and frontotemporal dementia. PrLDs have been proposed to contribute to the formation of diverse molecular assemblies, ranging from highly ordered amyloid aggregates to dynamic, multicomponent biomolecular condensates. PrLDs have also been proposed to help proteins maintain solubility in fluctuating environments. In this chapter, we will examine these diverse activities of PrLDs.

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