Beschreibung:
<jats:title>Significance</jats:title>
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Proteins carrying aggregation-prone prion-like domains cause many neurodegenerative diseases. The presence of prions in yeast has provided important insights into these disease processes and mechanisms of cellular proteostasis. However, it is not known whether these findings extend to other organisms. In this paper, we show that
<jats:italic>Dictyostelium discoideum</jats:italic>
has the highest content of prion-like proteins of all organisms investigated to date. Remarkably, overexpressed prion-like proteins remain soluble and are innocuous to
<jats:italic>D. discoideum</jats:italic>
, in contrast to yeast and other organisms, where they form cytotoxic cytosolic aggregates. However, when exposed to conditions that compromise proteostasis, these proteins aggregate and become cytotoxic. This indicates that
<jats:italic>D. discoideum</jats:italic>
has undergone specific adaptations in its proteostasis machinery to control its highly aggregation-prone prion-like proteome.
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