Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin
What this study shows
mTOR directly phosphorylates 4E-BP1 (PHAS-I), releasing eIF4E and establishing mTOR's role in translational control.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: HEK293; in vitro) 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 | HEK293; in vitro |
| Journal | Science |
| Year | 1997 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1126/science.277.5322.99 · PMID 9204908 |
Extracted findings
These fields were extracted from the paper with AI assistance and have not been checked against the source. Read them as a pointer into the paper, not as curated claims; where they disagree with the curated summary above, the curated summary stands.
| Intervention | Biochemical (mTOR/PHAS-I) |
| Target | mTOR / PHAS-I (4E-BP1) / eIF4E |
| Model | HEK293; in vitro |
| Effect | mTOR is a terminal kinase phosphorylating the translational repressor PHAS-I (4E-BP1) |
In the Atlas
Related topics
Links in the pathway map
- Supports mTORC1 inhibits 4E-BP1
- Supports Rapamycin inhibits mTORC1
More studies on this topic
- Translational control of long-lasting synaptic plasticity and memory (2009)
- Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E (2002)
- Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism (1999)
- Autism-related deficits via dysregulated eIF4E-dependent translational control (2013)
Was this page useful?
Thank you. Your answer was counted anonymously.