Casein kinase 2 regulates telomere protein complex formation through Rap1 phosphorylation
| Autor: | Kota Ono, Haruna Inoue, Mayuri Horiguchi, Junko Kanoh |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
endocrine system
Nuclear Envelope Telomere-Binding Proteins Biology Shelterin Complex 03 medical and health sciences 0302 clinical medicine CDC2 Protein Kinase Genetics medicine Phosphorylation Nuclear membrane Casein Kinase II Molecular Biology 030304 developmental biology 0303 health sciences Cell Cycle Membrane Proteins Nuclear Proteins Telomere Cell cycle Shelterin Chromatin Cell biology DNA-Binding Proteins Meiosis enzymes and coenzymes (carbohydrates) medicine.anatomical_structure Multiprotein Complexes Rap1 Schizosaccharomyces pombe Proteins Casein kinase 2 Protein Processing Post-Translational 030217 neurology & neurosurgery |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/gkz458 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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