論文 - 詳細
| RRC ID | 76345 |
|---|---|
| 著者 | Zheng H, Peng K, Gou X, Ju C, Zhang H. |
| タイトル | RNA recruitment switches the fate of protein condensates from autophagic degradation to accumulation. |
| ジャーナル | J Cell Biol |
| Abstract |
Protein condensates can evade autophagic degradation under stress or pathological conditions. However, the underlying mechanisms are unclear. Here, we demonstrate that RNAs switch the fate of condensates in Caenorhabditis elegans. PGL granules undergo autophagic degradation in embryos laid under normal conditions and accumulate in embryos laid under heat stress conditions to confer stress adaptation. In heat-stressed embryos, mRNAs and RNA control factors partition into PGL granules. Depleting proteins involved in mRNA biogenesis and stability suppresses PGL granule accumulation and triggers their autophagic degradation, while loss of activity of proteins involved in RNA turnover facilitates accumulation. RNAs facilitate LLPS of PGL granules, enhance their liquidity, and also inhibit recruitment of the gelation-promoting scaffold protein EPG-2 to PGL granules. Thus, RNAs are important for controlling the susceptibility of phase-separated protein condensates to autophagic degradation. Our work provides insights into the accumulation of ribonucleoprotein aggregates associated with the pathogenesis of various diseases. |
| 巻・号 | 222(6) |
| 公開日 | 2023-6-5 |
| DOI | 10.1083/jcb.202210104 |
| PII | 213995 |
| PMID | 37014300 |
| PMC | PMC10075224 |
| MeSH | Animals Autophagy* Caenorhabditis elegans / genetics Caenorhabditis elegans / metabolism Caenorhabditis elegans Proteins* / genetics Caenorhabditis elegans Proteins* / metabolism Cytoplasmic Granules / genetics Cytoplasmic Granules / metabolism Heat-Shock Response RNA* / metabolism RNA-Binding Proteins / genetics RNA-Binding Proteins / metabolism Ribonucleoproteins / genetics Ribonucleoproteins / metabolism |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 30 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 線虫 | tm6608 |