Welsh, G.I. and Miller, C.M. and Loughlin, A.J. and Price, N.T. and Proud, C.G. (1998) 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. ISSN 0014-5793.
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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 epsilon-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 eIF2B epsilon as Ser(540) and show that treatment of eIF2B with GSK-3 inhibits its activity. Ser(540) 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.
|Uncontrolled keywords:||eukaryotic initiation factor; phosphorylation; insulin; glycogen synthase kinase-3|
|Subjects:||Q Science > QH Natural history > QH301 Biology
Q Science > QR Microbiology
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Tara Puri|
|Date Deposited:||25 Mar 2009 17:33|
|Last Modified:||25 Mar 2009 17:33|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/17273 (The current URI for this page, for reference purposes)|
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