Andrea Flynn

TL;DR: Mnk1 may define a convergence point between the growth factor‐activated and one of the stress‐activated protein kinase cascades and is a candidate to phosphorylate eIF‐4E in cells.

TL;DR: It is shown, using specific inhibitors, that this involves both the p38 mitogen-activated protein (MAP) kinase and Erk signaling pathways, and that this blocks the phosphorylation of eIF4E by Mnk1 in vitro, which may explain the absence of an increase in eIF 4E phosphorylated under these conditions.

TL;DR: The data imply that stresses do not interfere with mTOR function but act in different ways on these three proteins, which can be regulated through the mammalian target of rapamycin, 4E-BP1, p70 S6 kinase and eEF2.

TL;DR: Comigration of the synthetic peptide SGS(P)TTK with the radiolabeled tryptic product on reverse-phase chromatography and two-dimensional mapping at different pH values confirmed that Ser-209 is the major phosphorylation site in eIF-4E in serum-stimulated Chinese hamster ovary cells.

TL;DR: Glucose was found to increase the activity of the guanine nucleotide-exchange factor eIF-2B over a rapid time course and over the same range of glucose concentrations as those that stimulate insulin synthesis (3-20 mM).