Specific threonine-4 phosphorylation and function of RNA polymerase II CTD during M phase progression
| Autor: | Ignasi Forné, Corinna Hintermair, Martin Heidemann, Elisabeth Kremmer, Andrew Flatley, Dirk Eick, Axel Imhof, Kirsten Voß |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Threonine
0301 basic medicine viruses Cell Cycle Proteins RNA polymerase II Protein Serine-Threonine Kinases Biology environment and public health Article Cell Line 03 medical and health sciences chemistry.chemical_compound Protein Domains Transcription (biology) Proto-Oncogene Proteins RNA polymerase Humans Phosphorylation Mitosis Centrosome Multidisciplinary Molecular biology Cell biology Molecular Weight Midbody enzymes and coenzymes (carbohydrates) 030104 developmental biology chemistry Mutation biology.protein RNA Polymerase II CTD Cell Division Cytokinesis |
| Zdroj: | Sci. Rep. 6:27401 (2016) Scientific Reports |
| Popis: | Dynamic phosphorylation of Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 heptad-repeats in the C-terminal domain (CTD) of the large subunit coordinates progression of RNA polymerase (Pol) II through the transcription cycle. Here, we describe an M phase-specific form of Pol II phosphorylated at Thr4, but not at Tyr1, Ser2, Ser5 and Ser7 residues. Thr4 phosphorylated Pol II binds to centrosomes and midbody and interacts with the Thr4-specific Polo-like kinase 1. Binding of Pol II to centrosomes does not require the CTD but may involve subunits of the non-canonical R2TP-Prefoldin-like complex, which bind to and co-localize with Pol II at centrosomes. CTD Thr4 mutants, but not Ser2 and Ser5 mutants, display severe mitosis and cytokinesis defects characterized by multipolar spindles and polyploid cells. We conclude that proper M phase progression of cells requires binding of Pol II to centrosomes to facilitate regulation of mitosis and cytokinesis in a CTD Thr4-P dependent manner. |
| Databáze: | OpenAIRE |
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