期刊
CELL REPORTS
卷 25, 期 11, 页码 3204-+出版社
CELL PRESS
DOI: 10.1016/j.celrep.2018.11.063
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资金
- National Institutes of Health, United States [R01AI118736, R01AI101437]
- Clinical and Translational Proteomics Service Center of the University of Texas Health Science Center at Houston
- NIH [R01AI21786]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI118736, R01AI101437] Funding Source: NIH RePORTER
Protein translation in eukaryotes is cell-cycle dependent, with translation rates more robust in G1 phase of the cell cycle than in mitosis. However, whether the fundamental cell-cycle control machinery directly activates protein translation during the G1/S cell-cycle transition remains unknown. Using the early divergent eukaryote Trypanosoma brucei as a model organism, we report that the G1 cyclin-dependent kinase CRK1 phosphorylates two translation initiation factors, eIF4E4 and PABP1, to promote the G1/S cell-cycle transition and global protein translation. Phosphorylation of eIF4E4 by CRK1 enhances binding to them 7 G cap structure and interaction with eIF4E4 and eIF4G3, and phosphorylation of PABP1 by CRK1 promotes association with the poly(A) sequence, self-interaction, and interaction with eIF4E4. These findings demonstrate that cyclin-dependent kinase-mediated regulation of translation initiation factors couples global protein translation with the G1/S cell-cycle transition.
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