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EIF4G1 — INS

Text-mined interactions from Literome

Tuxworth et al., Am J Physiol 1999 : Both insulin and phorbol ester increased eIF-4F complex formation, but these increases were unaffected by BDM
Wang et al., Am J Physiol Heart Circ Physiol 2000 : Concomitant with this, insulin increased the binding of eIF4E to eIF4G
Proud et al., Biochem Soc Trans 2001 : Insulin activates several of these proteins including the following : the guanine-nucleotide exchange factor eIF2B ; the eIF4F complex, which ( through eIF4E ) interacts with the cap of the mRNA ; p70 S6 kinase ; and elongation factor eEF2, which mediates the translocation step of elongation
O'Connor et al., Am J Physiol Endocrinol Metab 2003 : Both insulin and amino acids increased the phosphorylation of ribosomal protein S6 kinase ( S6K1 ) and the eIF4E binding protein ( 4E-BP1 ), decreased the binding of 4E-BP1 to eIF4E, increased eIF4E binding to eIF4G , and increased fractional protein synthesis rates but did not affect eIF2B activity
Williamson et al., Am J Physiol Endocrinol Metab 2005 : This appeared to be due to an attenuation of insulin stimulated eIF4E.eIF4G association, because other stimulatory effects of INS, e.g., phosphorylation of ERK1/2, 4E-BP1, S6K1, eIF4G, and eIF4E and eIF4E.4E-BP1 association, were unaffected
Suryawan et al., Am J Physiol Endocrinol Metab 2007 : Both INS and AA decreased the binding of 4E-BP1 to eIF4E and increased eIF4E binding to eIF4G ; these effects were greater in 6-day-old than in 26-day-old pigs
Kimball et al., Am J Physiol 1997 : However, the insulin induced association of eIF-4E and eIF-4G was not due to increased net phosphorylation of eIF-4E because insulin decreased the amount present in the phosphorylated form from 86 to 59 % of total eIF-4E