作者: X. Bu , D.W. Haas , C.H. Hagedorn
DOI: 10.1016/S0021-9258(18)53491-8
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摘要: Only serine phosphorylation of eukaryotic initiation factor-4E (eIF-4E) has been previously reported in intact cells. We found that treatment HepG2 cells with okadaic acid resulted as much 20% factor (eIF)-4E occurring on threonine residues and tryptic phosphopeptide maps showed several unrecognized phosphopeptides. Analysis p220 from control acid-treated demonstrated under both conditions. However, a unique pattern phosphopeptides was observed. The most notable finding hyperphosphorylation eIF-4E increased binding but not to the m7GTP cap structure. suggest is more complicated than recognized recruits into protein complex associates mRNA caps. A better understanding these protein-protein protein-mRNA interactions may aid design anti-sense directed chemistries disrupt such for specific target (Baker, B.F., Miraglia, L., Hagedorn, C. H. (1992) J. Biol. Chem. 267, 11495-11499).