ArticleProceedings of the National Academy of Sciences of the United States of America2015
Dictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed, 79 citations in OpenAlex.
- Biomolecular coacervation-mediated materials: Phase states, phase transitions, and biomedical applications.Bioactive materials · 2027Review
- Nutrient and heat stress induce changes to the solubility of predicted prion-like proteins in Dictyostelium discoideum.BMC molecular and cell biology · 2026Article
- Phase separation in plants: mechanisms, functions, and a simplified workflow for investigation.Frontiers in plant science · 2026Review
- Identification of Low-Complexity Domains by Compositional Signatures Reveals Class-Specific Frequencies and Functions Across the Domains of Life.PLoS computational biology · 2024Article
- Glutathionylation on RNA-binding proteins: a regulator of liquid‒liquid phase separation in the pathogenesis of amyotrophic lateral sclerosis.Experimental & molecular medicine · 2023Review
- Mechanistic Insight into the Suppression of Polyglutamine Aggregation by SRCP1.ACS chemical biology · 2023Article
- Katnip is needed to maintain microtubule function and lysosomal delivery to autophagosomes and phagosomes.Molecular biology of the cell · 2023Article
- Uncovering the molecular mechanism for dual effect of ATP on phase separation in FUS solution.Science advances · 2022Article
- Phylogenetic convergence of phase separation and mitotic function in the disordered protein BuGZ.Protein science : a publication of the Protein Society · 2022Article
- Insights on Microsatellite Characteristics, Evolution, and Function From the Social AmoebaFrontiers in neuroscience · 2022Review
- HP1β carries an acidic linker domain and requires H3K9me3 for phase separation.Nucleus (Austin, Tex.) · 2021Article
- Prion-like proteins: from computational approaches to proteome-wide analysis.FEBS open bio · 2021Review
- LCD-Composer: an intuitive, composition-centric method enabling the identification and detailed functional mapping of low-complexity domains.NAR genomics and bioinformatics · 2021Article
- Assessing the necessity of a family of genes that encode small proteins inmicroPublication biology · 2021Article
- Development of a Positive Selection High Throughput Genetic Screen inFrontiers in cell and developmental biology · 2021Article
- The Evolution of the Hallmarks of Aging.Frontiers in genetics · 2021Review
- Review
- Eukaryotic life without tQCUG: the role of Elongator-dependent tRNA modifications in Dictyostelium discoideum.Nucleic acids research · 2020Article
- Amino acid homorepeats in proteins.Nature reviews. Chemistry · 2020Review
- Unusual Occurrence of Two Bona-Fide CCA-Adding Enzymes inInternational journal of molecular sciences · 2020Article
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many protein-misfolding diseases are caused by proteins carrying prion-like domains. These proteins show sequence similarity to yeast prion proteins, which can interconvert between an intrinsically disordered and an aggregated prion state. The natural presence of prions in yeast has provided important insight into disease mechanisms and cellular proteostasis. However, little is known about prions in other organisms, and it is not yet clear whether the findings in yeast can be generalized. Using bioinformatics tools, we show that Dictyostelium discoideum has the highest content of prion-like proteins of all organisms investigated to date, suggesting that its proteome has a high overall aggregation propensity. To study mechanisms regulating these proteins, we analyze the behavior of several well-characterized prion-like proteins, such as an expanded version of human huntingtin exon 1 (Q103) and the prion domain of the yeast prion protein Sup35 (NM), in D. discoideum. We find that these proteins remain soluble and are innocuous to D. discoideum, in contrast to other organisms, where they form cytotoxic cytosolic aggregates. However, when exposed to conditions that compromise molecular chaperones, these proteins aggregate and become cytotoxic. We show that the disaggregase Hsp101, a molecular chaperone of the Hsp100 family, dissolves heat-induced aggregates and promotes thermotolerance. Furthermore, prion-like proteins accumulate in the nucleus, where they are targeted by the ubiquitin-proteasome system. Our data suggest that D. discoideum has undergone specific adaptations that increase the proteostatic capacity of this organism and allow for an efficient regulation of its prion-like proteome.
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