Journal
MOLECULAR CELL
Volume 43, Issue 6, Pages 962-972Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2011.08.008
Keywords
-
Categories
Funding
- National Institutes of Health (NIH) [GM45443, GM067700]
- Howard Hughes Medical Institute
- Leukemia and Lymphoma Society
Ask authors/readers for more resources
The translation, localization, and degradation of cytoplasmic mRNAs are controlled by the formation and rearrangement of their mRNPs. The conserved Ded1/DDX3 DEAD-box protein functions in an unknown manner to affect both translation initiation and repression. We demonstrate that Ded1 first functions by directly interacting with elF4G to assemble a Ded1-mRNA-elF4F complex, which accumulates in stress granules. After ATP hydrolysis by Ded1, the mRNP exits stress granules and completes translation initiation. Thus, Ded1 functions both as a repressor of translation, by assembling an mRNP stalled in translation initiation, and as an ATP-dependent activator of translation, by resolving the stalled mRNP. These results identify Ded1 as a translation initiation factor that assembles and remodels an intermediate complex in translation initiation.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available