eIF4EBP1 Mouse Monoclonal Antibody [3G1]

Function

The translation of proteins from eukaryotic mRNA is initiated by the multisubunit complex eIF-4F, which associates with the mRNA 5' cap structure. eIF-4E, a component of eIF-4F, is responsible for binding to the 5' cap structure and for the assembly of the eIF-4F complex. The regulatory protein 4E-BP1, also referred to as PHAS-I, inhibits eIF-4E function. Phosphorylation of 4E-BP1 by S6 kinase p70, MAP kinases or PKCs causes the disassociation of 4E-BP1 from eIF-4E, promoting translation. A protein that is functionally related to 4E-BP1, designated 4E-BP2, also associates with eIF-4E.

Background References

1. von Manteuffel, S.R., et al.1996. 4E-BP1 phosphorylation is mediated by the FRAP-p70s6k pathway and is independent of mitogen-activated protein kinase. Proc. Natl. Acad. Sci. USA 93: 4076-4080.

2. Mendez, R., et al. 1996. Stimulation of protein synthesis, eukaryotic translation initiation factor 4E phosphorylation, and PHAS-I phosphorylation by Insulin requires Insulin receptor substrate 1 and phosphatidylinositol 3- kinase. Mol. Cell. Biol. 16: 2857-2864.

3. Whalen, S.G., et al.1996. Phosphorylation of eIF-4E on serine 209 by protein kinase C is inhibited by the translational repressors, 4E-binding proteins. J. Biol. Chem. 271: 11831-11837.

Subcellular Location

Cytoplasm cytosol nucleoplasm

UNIPROT

SwissProt: Q13541 Human

Synonyms