EIF4EBP1
This gene encodes one member of a family of translation repressor proteins. The protein directly interacts with eukaryotic translation initiation factor 4E (eIF4E), which is a limiting component of the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs. Interaction of this protein with eIF4E inhibits complex assembly and represses translation. This protein is phosphorylated in response to various signals including UV irradiation and insulin signaling, resulting in its dissociation from eIF4E and activation of mRNA translation. [provided by RefSeq, Jul 2008]
Full Name
Eukaryotic Translation Initiation Factor 4E Binding Protein 1
Research Area
Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways.
Biological Process
Cellular response to hypoxia Source: Ensembl
G1/S transition of mitotic cell cycle Source: UniProtKB
Lung development Source: Ensembl
Negative regulation of protein-containing complex assembly Source: Ensembl
Negative regulation of translational initiation Source: UniProtKB
Positive regulation of mitotic cell cycle Source: UniProtKB
Response to amino acid starvation Source: Ensembl
Response to ethanol Source: Ensembl
Response to ischemia Source: Ensembl
TOR signaling Source: UniProtKB
Cellular Location
Cytosol; Postsynaptic cytosol; Nucleus; Cytoplasm; Glutamatergic synapse; Protein-containing complex
PTM
Phosphorylated on serine and threonine residues in response to insulin, EGF and PDGF. Phosphorylation at Thr-37, Thr-46, Ser-65 and Thr-70, corresponding to the hyperphosphorylated form, is regulated by mTORC1 and abolishes binding to EIF4E.
Ubiquitinated: when eIF4E levels are low, hypophosphorylated form is ubiquitinated by the BCR(KLHL25) complex, leading to its degradation and serving as a homeostatic mechanism to maintain translation and prevent eIF4E inhibition when eIF4E levels are low. Not ubiquitinated when hyperphosphorylated (at Thr-37, Thr-46, Ser-65 and Thr-70) or associated with eIF4E.
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