Welsh, Gavin I.; Miller, Christa M.; Loughlin, Jane A.; Price, Nigel T. and Proud, Christopher G.
Regulation of eukaryotic initiation factor eIF2B: glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin.
FEBS Letters, 421(2) pp. 125–130.
Eukaryotic initiation factor eIF2B catalyses a key regulatory step in mRNA translation. eIF2B and total protein synthesis are acutely activated by insulin, and this requires phosphatidylinositol 3-kinase (PI 3-kinase). The ε-subunit of eIF2B is phosphorylated by glycogen synthase kinase-3 (GSK-3), which is inactivated by insulin in a PI 3-kinase-dependent manner. Here we identify the phosphorylation site in eIF2Bε as Ser540 and show that treatment of eIF2B with GSK-3 inhibits its activity. Ser540 is phosphorylated in intact cells and undergoes dephosphorylation in response to insulin. This is blocked by PI 3-kinase inhibitors. Insulin-induced dephosphorylation of this inhibitory site in eIF2B seems likely to be important in the overall activation of translation by this hormone.
||1998 Federation of European Biochemical Societies
|Project Funding Details:
|Funded Project Name||Project ID||Funding Body|
|Not Set||Not Set||Wellcome Trust|
||eukaryotic initiation factor; phosphorylation; insulin; glycogen synthase kinase-3
||Science > Life, Health and Chemical Sciences
|Interdisciplinary Research Centre:
||Biomedical Research Network (BRN)
||20 Apr 2011 12:26
||07 Mar 2014 13:47
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