Journal
CELL REPORTS
Volume 11, Issue 9, Pages 1425-1436Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2015.04.065
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Funding
- Canadian Institutes of Health Research (CIHR) [MOP-130425]
- Natural Sciences and Engineering Research Council of Canada (NSERC) Discovery grant [RGPIN-2015-03712]
- NSERC Discovery and Accelerator Supplement [RGPIN-2014-06434, RGPAS 462169]
- Fonds de recherche du Quebec-Sante (FRQS) Chercheur-Boursier Junior 1
- CIHR New Investigator awards
- McGill Integrated Cancer Research Training Program
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Eukaryotic mRNA degradation often initiates with the recruitment of the CCR4-NOT deadenylase complex and decay factors to the mRNA 30 terminus. How the 3'-proximal decay machinery interacts with the 5'-terminal cap structure in order to engender mRNA decapping and 5'-3' degradation is unclear. Human 4E-T is an eIF4E-binding protein that has been reported to promote mRNA decay, albeit via an unknown mechanism. Here, we show that 4E-T is a component of the mRNA decay machinery and interacts with factors including DDX6, LSM14, and the LSM1-7-PAT1 complex. We also provide evidence that 4E-T associates with, and enhances the decay of, mRNAs targeted by the CCR4-NOT deadenylase complex, including microRNA targets. Importantly, we demonstrate that 4E-T must interact with eIF4E to engender mRNA decay. Taken together, our data support a model where 4E-T promotes mRNA turnover by physically linking the 3'-terminal mRNA decay machinery to the 5' cap via its interaction with eIF4E.
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