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- W2000275654 abstract "It is well accepted that post-transcriptional control makes a significant contribution to the overall regulation of gene expression.1 One of the major ways in which translation can be regulated is by controlling the formation of the eukaryotic initiation factor (eIF)4F complex. This heterotrimeric complex is composed of the scaffold protein eIF4G, the cap-binding protein eIF4E and a DEAD-box helicase eIF4A1, which is required to unwind the structured regions of RNA that would otherwise be inhibitory to the scanning ribosome. Other proteins that also interact with this complex include poly(A)-binding protein (PABP) (which interacts with both the poly(A) tail and eIF4G), eIF4B, which stimulates eIF4A1 and helps circularization of the complex via its interaction with PABP, and eIF3, which interacts with the 40S ribosomal subunit. Thus, via the interaction of eIF4F with 7-methylguanylate (m7G) cap at the 5' end of the mRNA and eIF3, this complex is able to coordinate the binding of the mRNA with the 40S ribosomal subunit (Figure 1). Signalling through the PI3K/mTOR pathway activates translation by phosphorylating 4EBP1, a negative regulator of eIF4E. In its hypophosphorylated state 4EBP1 binds and limits the bioavailability of eIF4E and therefore eIF4F complex formation." @default.
- W2000275654 created "2016-06-24" @default.
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- W2000275654 date "2015-01-23" @default.
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- W2000275654 title "eIF4A1 is a promising new therapeutic target in ER-negative breast cancer" @default.
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- W2000275654 doi "https://doi.org/10.1038/cdd.2014.210" @default.
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