ArticleProceedings of the National Academy of Sciences of the United States of America2020
Composition-based prediction and rational manipulation of prion-like domain recruitment to stress granules.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 41 citations in OpenAlex.
- A composition-matching algorithm, MatchIDR, identifies prion-like domains that localize to stress granules.Protein science : a publication of the Protein Society · 2026Article
- Role of CPEBs in Learning and Memory.Journal of neurochemistry · 2025Review
- Large-scale discovery of chromatin dysregulation induced by oncofusions and other protein-coding variants.Nature biotechnology · 2025Article
- Understanding Amyotrophic Lateral Sclerosis: Pathophysiology, Diagnosis, and Therapeutic Advances.International journal of molecular sciences · 2024Review
- Rational Tuning of the Concentration-independent Enrichment of Prion-like Domains in Stress Granules.Journal of molecular biology · 2024Article
- Heterotypic interactions can drive selective co-condensation of prion-like low-complexity domains of FET proteins and mammalian SWI/SNF complex.Nature communications · 2024Article
- Article
- Time-resolved proteomic profiling reveals compositional and functional transitions across the stress granule life cycle.Nature communications · 2023Article
- Heterotypic interactions in the dilute phase can drive co-condensation of prion-like low-complexity domains of FET proteins and mammalian SWI/SNF complex.bioRxiv : the preprint server for biology · 2023Article
- Phase separation of protein mixtures is driven by the interplay of homotypic and heterotypic interactions.Nature communications · 2023Article
- Cauliflower mosaic virus protein P6 is a multivalent node for RNA granule proteins and interferes with stress granule responses during plant infection.The Plant cell · 2023Article
- Translocation of cytosolic human Cdc73 to stress granules plays a role in arsenic stress-induced stabilization of p53 mRNA.Journal of cell science · 2023Article
- Phase Separation in Mixtures of Prion-Like Low Complexity Domains is Driven by the Interplay of Homotypic and Heterotypic Interactions.Research square · 2023Article
- Understanding the link between the actin cytoskeleton and prion biology.PLoS pathogens · 2023Article
- New Insights into Phase Separation Processes and Membraneless Condensates of EIN2.Plants (Basel, Switzerland) · 2022Article
- Lsm7 phase-separated condensates trigger stress granule formation.Nature communications · 2022Article
- Exploring cryptic amyloidogenic regions in prion-like proteins from plants.Frontiers in plant science · 2022Article
- Defining the Caprin-1 Interactome in Unstressed and Stressed Conditions.Journal of proteome research · 2021Article
- From Prions to Stress Granules: Defining the Compositional Features of Prion-Like Domains That Promote Different Types of Assemblies.International journal of molecular sciences · 2021Review
- Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets.iScience · 2021Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Mutations in a number of stress granule-associated proteins have been linked to various neurodegenerative diseases. Several of these mutations are found in aggregation-prone prion-like domains (PrLDs) within these proteins. In this work, we examine the sequence features governing PrLD localization to stress granules upon stress. We demonstrate that many yeast PrLDs are sufficient for stress-induced assembly into microscopically visible foci that colocalize with stress granule markers. Additionally, compositional biases exist among PrLDs that assemble upon stress, and these biases are consistent across different stressors. Using these biases, we have developed a composition-based prediction method that accurately predicts PrLD assembly into foci upon heat shock. We show that compositional changes alter PrLD assembly behavior in a predictable manner, while scrambling primary sequence has little effect on PrLD assembly and recruitment to stress granules. Furthermore, we were able to design synthetic PrLDs that were efficiently recruited to stress granules, and found that aromatic amino acids, which have previously been linked to PrLD phase separation, were dispensable for this recruitment. These results highlight the flexible sequence requirements for stress granule recruitment and suggest that PrLD localization to stress granules is driven primarily by amino acid composition, rather than primary sequence.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.