ArticleNature communications2022
Low complexity RGG-motif sequence is required for Processing body (P-body) disassembly.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- The dynamic and heterogeneous composition of biomolecular condensates and its functional relevance.Nature reviews. Molecular cell biology · 2026Review
- The anti-viral protein Shiftless blocks p-body formation during KSHV infection.The Journal of general virology · 2026Article
- Sequence-dependent co-condensation of Lsr2 with DNA elucidates the mechanism of genome compaction in Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- Arginine methylation in cancer: mechanisms and therapeutic implications.Biomarker research · 2025Review
- Investigating the role of RNA-binding protein Ssd1 in aneuploidy tolerance through network analysis.RNA (New York, N.Y.) · 2024Article
- Biomolecular condensates and disease pathogenesis.Science China. Life sciences · 2024Review
- SOS1 tonoplast neo-localization and the RGG protein SALTY are important in the extreme salinity tolerance of Salicornia bigelovii.Nature communications · 2024Article
- The FomYjeF Protein Influences the Sporulation and Virulence ofInternational journal of molecular sciences · 2023Article
- Global profiling identifies a stress-responsive tyrosine site on EDC3 regulating biomolecular condensate formation.Cell chemical biology · 2022Article
- A brief guideline for studies of phase-separated biomolecular condensates.Nature chemical biology · 2022Review
- Assay to Study the Phase-transition Behavior of Edc3, a Conserved Processing Body (P-body) Marker Protein.Bio-protocol · 2022Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
P-bodies are conserved mRNP complexes that are implicated in determining mRNA fate by affecting translation and mRNA decay. In this report, we identify RGG-motif containing translation repressor protein Sbp1 as a disassembly factor of P-bodies since disassembly of P-bodies is defective in Δsbp1. RGG-motif is necessary and sufficient to rescue the PB disassembly defect in Δsbp1. Binding studies using purified proteins revealed that Sbp1 physically interacts with Edc3 and Sbp1-Edc3 interaction competes with Edc3-Edc3 interaction. Purified Edc3 forms assemblies, promoted by the presence of RNA and NADH and the addition of purified Sbp1, but not the RGG-deletion mutant, leads to significantly decreased Edc3 assemblies. We further note that the aggregates of human EWSR1 protein, implicated in neurodegeneration, are more persistent in the absence of Sbp1 and overexpression of EWSR1 in Δsbp1 leads to a growth defect. Taken together, our observations suggest a role of Sbp1 in disassembly, which could apply to disease-relevant heterologous protein-aggregates.
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Registered trials
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