論文 - 詳細
| RRC ID | 64121 |
|---|---|
| 著者 | Inoue H, Horiguchi M, Ono K, Kanoh J. |
| タイトル | Casein kinase 2 regulates telomere protein complex formation through Rap1 phosphorylation. |
| ジャーナル | Nucleic Acids Res |
| Abstract |
Telomeres located at the ends of linear chromosomes play important roles in the maintenance of life. Rap1, a component of the shelterin telomere protein complex, interacts with multiple proteins to perform various functions; further, formation of shelterin requires Rap1 binding to other components such as Taz1 and Poz1, and telomere tethering to the nuclear envelope (NE) involves interactions between Rap1 and Bqt4, a nuclear membrane protein. Although Rap1 is a hub for telomere protein complexes, the regulatory mechanisms of its interactions with partner proteins are not fully understood. Here, we show that Rap1 is phosphorylated by casein kinase 2 (CK2) at multiple sites, which promotes interactions with Bqt4 and Poz1. Among the multiple CK2-mediated phosphorylation sites of Rap1, phosphorylation at Ser496 was found to be crucial for both Rap1-Bqt4 and Rap1-Poz1 interactions. These mechanisms mediate proper telomere tethering to the NE and the formation of the silenced chromatin structure at chromosome ends. |
| 巻・号 | 47(13) |
| ページ | 6871-6884 |
| 公開日 | 2019-7-26 |
| DOI | 10.1093/nar/gkz458 |
| PII | 5498753 |
| PMID | 31131414 |
| PMC | PMC6648331 |
| MeSH | CDC2 Protein Kinase / physiology Casein Kinase II / physiology* Cell Cycle Chromatin / ultrastructure DNA-Binding Proteins / metabolism Meiosis Membrane Proteins / metabolism Multiprotein Complexes Nuclear Envelope / metabolism* Nuclear Proteins / metabolism Phosphorylation Protein Processing, Post-Translational Schizosaccharomyces pombe Proteins / metabolism Schizosaccharomyces pombe Proteins / physiology* Shelterin Complex Telomere / metabolism* Telomere-Binding Proteins / metabolism* |
| IF | 11.502 |
| 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 | 2 |
| 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 | |
| 酵母 | FY21204 |