Insulin-stimulated phosphorylation of initiation factor 4E is mediated by the MAP kinase pathway

Flynn, A. and Proud, C.G. (1996) Insulin-stimulated phosphorylation of initiation factor 4E is mediated by the MAP kinase pathway. Febs Letters, 389 (2). pp. 162-166. ISSN 0014-5793. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1016/0014-5793(96)00564-9

Abstract

The cap-binding initiation factor 4E (eIF4E) is regulated by phosphorylation and by the inhibitory binding protein 4E-BP1, Here we show that insulin-induced phosphorylation of cIF4E is not significantly affected by rapamycin, but is sensitive to wortmannin, which inhibits phosphatidglinositol 3'-kinase and blocks the activation of MAP kinase. Since PD098059, an inhibitor of MAP kinase activation, also blocks insulin-induced phosphorylation of eIF4E, the MAP kinase pathway seems to mediate this effect, Phosphorylated eIF4E can still bind to 4E-BP1. These data illustrate that (i) distinct signalling pathways mediate the phosphorylation of eIF4E and 4E-BP1 and (ii) phosphorylation of eIF4E, unlike that of 4E-BP1, does not lead directly to the release of 4E-BP1.

Item Type: Article
Uncontrolled keywords: MAP kinase; insulin; translation; eIF; rapamycin
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: R.F. Xu
Date Deposited: 08 Jun 2009 15:21
Last Modified: 08 Jun 2009 15:21
Resource URI: http://kar.kent.ac.uk/id/eprint/19182 (The current URI for this page, for reference purposes)
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