Eukaryotic translation initiation factor 4E-binding protein 1 (also known as 4E-BP1) is a protein that in humans is encoded by the EIF4EBP1 gene. [5] inhibits cap-dependent translation by binding to translation initiation factor eIF4E.

2023年6月7日 · 真核翻译起始因子4E结合蛋白1 (eIF4E-bind-ing protein 1,4E-BP1)是一种高度保守的小分子蛋白，在蛋白翻译起始途径选择中发挥重要的功能。 4E-BP1通过与脚手架蛋白elF4G竞争性结合转录起始因elF4E,抑制elF4E的功能及帽依赖性蛋白质翻译起始。 4E-BP¹受PI3K/AKT

Eukaryotic translation initiation factor 4E (eIF4E)-binding protein 1 (4E-BP1) is a member of a family of translation repressor proteins, and a well-known substrate of mechanistic target of rapamycin (mTOR) signaling pathway. Phosphorylation of 4E-BP1 causes its release from eIF4E to allow cap-depen …

Eukaryotic translation initiation factor 4E (eIF4E)-binding protein 1 (4E-BP1) is a member of a family of translation repressor proteins, and a well-known substrate of mechanistic target of rapamycin (mTOR) signaling pathway.

2024年12月24日 · EIF4EBP1 (Eukaryotic Translation Initiation Factor 4E Binding Protein 1) is a Protein Coding gene. Diseases associated with EIF4EBP1 include Tuberous Sclerosis and Rhabdomyosarcoma. Among its related pathways are Translation Insulin regulation of translation and Peptide chain elongation.

The mechanistic/mammalian target of rapamycin (mTOR) is the crucial hub of signalling pathways that regulate essential steps in the cell life cycle. Once incorporated in the mTORC1 complex, mTOR phosphorylates the eukaryotic initiation factor 4E (eIF4E)- binding protein 1 (4E-BP1), which then releas …

2021年6月3日 · Böhm et al. resolve how the intrinsically disordered protein substrate 4E-BP1 is processed by the large kinase complex mTORC1. A well-adjusted interplay of two-site tethering, stepwise phosphorylation, and structural switches ensures rapid release of the bound protein eIF4E, which in turn initiates cap-dependent translation.

该蛋白质直接与真核翻译起始因子 4E (eIF4E) 相互作用，后者是将 40S 核糖体亚基募集到 mRNA 5' 端的多亚基复合物的限制成分。

1999年6月1日 · Binding of the 4E-BPs to eIF4E is regulated by phosphorylation: Hypophosphorylated 4E-BP isoforms interact strongly with eIF4E, whereas hyperphosphorylated isoforms do not. 4E-BP1 is hypophosphorylated in quiescent cells, but is hyperphosphorylated on multiple sites following exposure to a variety of extracellular stimuli.

To study the role of Akt in the phosphorylation of 4E-BP1, a hemagglutinin-tagged 4E-BP1 (HA–4E-BP1) was generated. We first examined whether the transiently expressed HA–4E-BP1 exhibits a change in electrophoretic mobility after phosphorylation, as was observed for the endogenous 4E-BP1.