Welsh, Gavin I. and Stokes, C.M. and Wang, X.M. and Sakaue, H. and Ogawa, W. and Kasuga, M. and Proud, C.G. (1997) Activation of translation initiation factor eIF2B by insulin requires phosphatidyl inositol 3-kinase. Febs Letters, 410 (2-3). pp. 418-422. ISSN 0014-5793.
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Eukaryotic initiation factor eIF2B mediates a key regulatory step in peptide-chain initiation and is acutely activated by insulin, although it is not clear how, Inhibitors of phosphatidylinositide 3-kinase blocked activation of eIF2B, although rapamycin, which inhibits the p70 S6 kinase pathway, did not, Furthermore, a dominant negative mutant of PI 3-kinase also prevented activation of eIF2B, while a Sos-mutant, which blocks MAP kinase activation, did not. The data demonstrate that a pathway distinct from MAP and p70 S6 kinases regulates eIF2B, Glycogen synthase kinase-3 (GSK-3) phosphorylates and inactivates eIF2B, In all cases, eIF2B and GSK-3 were regulated reciprocally, Dominant negative PI 3-kinase abolished the insulin-induced inhibition of GSK-3, These data strongly support the hypothesis that insulin activates eIF2B through a signalling pathway involving PI 3-kinase and inhibition of GSK-3. (C) 1997 Federation of European Biochemical Societies.
|Subjects:||Q Science > QD Chemistry
Q Science > QR Microbiology
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||T.J. Sango|
|Date Deposited:||29 Apr 2009 12:55|
|Last Modified:||29 Apr 2009 12:55|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/18038 (The current URI for this page, for reference purposes)|
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