PDCD4
Translation inhibitor that blocks the eIF4A helicase. S6K1 marks it for degradation, giving mTORC1 a second, 4E-BP-independent route to raising protein synthesis.
Another brake on protein-making. A protein that blocks the translation helper eIF4A. mTORC1's downstream partner S6K1 tags it for destruction, giving the pathway a second way - separate from 4E-BP1 - to boost protein production.
S6K1 phosphorylates S67, creating a βTRCP degron – an mTORC1 output that works by destroying a repressor rather than activating an enzyme.
TL;DR. PDCD4 appears in 2 curated studies in Oliver's mTOR Atlas: 2 at the molecular level (cells, biochemistry, structure). No study in people is recorded for it in the Atlas yet. It has 3 interactions in the curated pathway model.
In the pathway model
| Interaction | Mechanism | Evidence | Studies |
|---|---|---|---|
| PDCD4 inhibits Protein synthesis mechanism: functional-consequence · this link in full · on the map table | 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. PDCD4 blocks the eIF4A helicase, so mRNAs with structured 5' ends cannot be unwound and translated. 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. plausible in people, not shown directly · settled in the literature | M | SUZ2008 |
| PDCD4 inhibits mTORC2 mechanism: complex-assembly · this link in full · on the map table | PDCD4 grabs Rictor and keeps mTORC2 from working. PDCD4 binds the mTORC2 subunit Rictor through three basic residues, which stops mTORC2 from assembling properly and lowers its kinase activity. PDCD4 binds the mTORC2 subunit Rictor through three basic residues, which stops mTORC2 from assembling properly and lowers its kinase activity. Holds under: Human NSCLC cell lines and mouse xenografts; not shown in normal tissue. Single study. plausible in people, not shown directly · emerging, few independent studies | M | WANG2026B |
| S6K1 inhibits PDCD4 mechanism: degradation · this link in full · on the map table | S6K1 marks PDCD4, itself a brake on protein-building, for destruction – a second way mTORC1 releases the brake. S6K1 tags PDCD4 for destruction. PDCD4 is itself a translation inhibitor, so removing it is a second, parallel way mTORC1 lifts a brake on protein synthesis. S6K1 tags PDCD4 for destruction. PDCD4 is itself a translation inhibitor, so removing it is a second, parallel way mTORC1 lifts a brake on protein synthesis. Holds under: Single-study edge in this corpus. plausible in people, not shown directly · emerging, few independent studies | M | DOR2006 |
Evidence at a glance
| Evidence | What it means | Studies |
|---|---|---|
| M | Molecular — cells, biochemistry, structure | 2 |
No direct human evidence in the Atlas for this entity yet — everything below rests on animal or molecular work.
Studies
| Year | Evidence | Study |
|---|---|---|
| 2026 | M | Pdcd4-Rictor interaction suppresses mTORC2-PFKFB3 axis and tumorigenesis in NSCLC. WANG2026B Pdcd4 binds Rictor via residues R105/K108/R110 to disrupt mTORC2 assembly and kinase activity, lowering PFKFB3 levels and suppressing glycolysis and NSCLC tumour growth. |
| 2006 | M | S6K1- and betaTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth DOR2006 S6K1 triggers betaTRCP-mediated degradation of the tumour suppressor PDCD4 to promote translation. |
Related entities
Thank you. Your answer was counted anonymously.