Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism
What this study shows
4E-BP1 is phosphorylated by an ordered, priming two-step mechanism that controls its release of eIF4E.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Mammalian cells; 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 | Mammalian cells; in vitro |
| Journal | Genes & development |
| Year | 1999 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1101/gad.13.11.1422 · PMID 10364159 · Free full text (PMC316780) |
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 / 4E-BP1) |
| Target | mTOR / 4E-BP1 / eIF4E |
| Model | Mammalian cells; in vitro |
| Effect | 4E-BP1 phosphorylation follows a two-step mechanism that regulates its binding to eIF4E |
In the Atlas
Related topics
Links in the pathway map
- Supports mTORC1 inhibits 4E-BP1
More studies on this topic
- Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin (1997)
- 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)
- Autism-related deficits via dysregulated eIF4E-dependent translational control (2013)
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