Source

Rabbit

Reactivity

Human;Mouse;Rat;Monkey;Bovine

Background

Translation repressor protein 4E-BP1 inhibits cap-dependent translation by binding to the translation initiation factor eIF4E. Hyperphosphorylation of 4E-BP1 disrupts this interaction and results in activation of cap-dependent translation. Both the PI3 kinase/Akt pathway and FRAP/mTOR kinase regulate 4E-BP1 activity. Multiple 4E-BP1 residues are phosphorylated in vivo. While phosphorylation by FRAP/mTOR at Thr37 and Thr46 does not prevent the binding of 4E-BP1 to eIF4E, it is thought to prime 4E-BP1 for subsequent phosphorylation at Ser65 and Thr70.4E-BP2 and 4E-BP3 share high sequence homology with 4E-BP1, including conservation of the major FRAP/mTOR-dependent phosphorylation sites. Preliminary data suggests that phosphorylation of 4E-BP2 is regulated in a similar manner to that of 4E-BP1, although phosphorylation of this protein has not been as extensively studied.

References

[1] Pause, A. et al. (1994) Nature 371, 762-7.
[2] Brunn, G.J. et al. (1997) Science 277, 99-101.
[3] Gingras, A.C. et al. (1998) Genes Dev 12, 502-13.
[4] Fadden, P. et al. (1997) J Biol Chem 272, 10240-7.
[5] Gingras, A.C. et al. (1999) Genes Dev 13, 1422-37.
[6] Lin, T-A. and Lawrence, Jr, J.C. (1996) J. Biol. Chem. 271, 30199-30204.

Raw materials

Preparation Products