PDCD4 inhibits translation initiation by binding to eIF4A using both its MA3 domains
What this study shows
Both MA3 domains of PDCD4 bind the N-terminal domain of eIF4A and compete with eIF4G and RNA for it, which explains how PDCD4 blocks translation initiation.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Structural and biophysical work on human proteins) rather than a whole-organism health-outcome study. That is often exactly where causal biology gets established -- the code says which system the finding was shown in, and nothing about how good the work is. |
| Study type | 5 - Mechanistic / In Vitro |
| Model system | Structural and biophysical work on human proteins |
| Journal | Proceedings of the National Academy of Sciences |
| Year | 2008 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1073/pnas.0712235105 · PMID 18296639 · Free full text (PMC2265113) |
In the Atlas
Links in the pathway map
- Supports PDCD4 inhibits Protein synthesis
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