ArticleProceedings of the National Academy of Sciences of the United States of America2020
Micellar TIA1 with folded RNA binding domains as a model for reversible stress granule formation.
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 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Biomolecular Condensates Dictate the Folding Landscape of Proteins.bioRxiv : the preprint server for biology · 2026Article
- Structured protein domains enter the spotlight: modulators of biomolecular condensate form and function.Trends in biochemical sciences · 2025Review
- Structural Characteristics and Properties of the RNA-Binding Protein hnRNPK at Multiple Physical States.International journal of molecular sciences · 2025Article
- Crucial role of the cGAS N terminus in mediating flowable and functional cGAS-DNA condensate formation via DNA interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Solid-state NMR studies of proteins in condensed phases.Magnetic resonance letters · 2024Review
- Liquid Droplet Aging and Seeded Fibril Formation of the Cytotoxic Granule Associated RNA Binding Protein TIA1 Low Complexity Domain.Journal of the American Chemical Society · 2023Article
- Phase separation and pathologic transitions of RNP condensates in neurons: implications for amyotrophic lateral sclerosis, frontotemporal dementia and other neurodegenerative disorders.Frontiers in molecular neuroscience · 2023Review
- Monitoring protein unfolding transitions by NMR-spectroscopy.Journal of biomolecular NMR · 2022Article
- Article
- The Multifunctional Faces of T-Cell Intracellular Antigen 1 in Health and Disease.International journal of molecular sciences · 2022Review
- Regulation of TIA-1 Condensates: ZnFrontiers in molecular biosciences · 2022Article
- On the specificity of protein-protein interactions in the context of disorder.The Biochemical journal · 2021Review
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
TIA1, a protein critical for eukaryotic stress response and stress granule formation, is structurally characterized in full-length form. TIA1 contains three RNA recognition motifs (RRMs) and a C-terminal low-complexity domain, sometimes referred to as a "prion-related domain" or associated with amyloid formation. Under mild conditions, full-length (fl) mouse TIA1 spontaneously oligomerizes to form a metastable colloid-like suspension. RRM2 and RRM3, known to be critical for function, are folded similarly in excised domains and this oligomeric form of apo fl TIA1, based on NMR chemical shifts. By contrast, the termini were not detected by NMR and are unlikely to be amyloid-like. We were able to assign the NMR shifts with the aid of previously assigned solution-state shifts for the RRM2,3 isolated domains and homology modeling. We present a micellar model of fl TIA1 wherein RRM2 and RRM3 are colocalized, ordered, hydrated, and available for nucleotide binding. At the same time, the termini are disordered and phase separated, reminiscent of stress granule substructure or nanoscale liquid droplets.
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