Oliver's mTOR Atlas Evidence Platform
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Pathway link PDCD4-TRANSL

PDCD4 Protein synthesis

PDCD4 inhibits Protein synthesis.

PDCD4 jams a helper enzyme so some mRNAs can't be unwound and read.

PDCD4 blocks the eIF4A helicase, so mRNAs with structured 5' ends cannot be unwound and translated.

The conditions it holds under

SUZ2008 shows by structure and binding assays that PDCD4 binds the N-terminal domain of eIF4A and displaces eIF4G and RNA, which is the step asserted here. Cell-level evidence that PDCD4 loss changes translation of structured mRNAs is not in this corpus.

Time it takes
minutes
Step
direct (one molecule acts on the other)
Measured in
mammalian cells
Where in the cell
cytosol
Reaches people?
plausible in people, not shown directly
How settled
settled in the literature

Studies behind it

YearEvidenceStudy
2008 M PDCD4 inhibits translation initiation by binding to eIF4A using both its MA3 domainsSUZ2008 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.

Points the other way

No study in the Atlas contradicts this link. That means none in this curated set, not none in the literature.

Who has checked this

Checked by
No researcher outside the project has checked this link yet.
Curator sign-off
Not signed off yet. This link was drafted with AI help and has not been reviewed link by link; treat it as a proposal until it is.
Curated by
Oliver Barton, with AI help for drafting; see how links are checked.

“Inhibits” describes the effect on the target's activity, not on how much of it there is.

“How settled” describes how far researchers in the field agree. It is not the same as the sign-off above, which only says whether a named curator has checked this page.

If this link rests on your own work: a click on “This looks right” below, or a short note through “Report an error”, helps us more than anything else on this page.

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