Regulation of translation elongation factor-2 by insulin via a rapamycin-sensitive signalling pathway

Redpath, N.T. and Foulstone, E.J. and Proud, C.G. (1996) Regulation of translation elongation factor-2 by insulin via a rapamycin-sensitive signalling pathway. EMBO Journal, 15 (9). pp. 2291-2297. ISSN 0261-4189. (The full text of this publication is not available from this repository)

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Abstract

It is well established that insulin and serum stimulate gene expression at the level of mRNA translation in animal cells, and previous studies have mainly focused on the initiation process. Here we show that, in Chinese hamster ovary cells expressing the human insulin receptor, insulin causes decreased phosphorylation of elongation factor eEF-2 and that this is associated with stimulation of the rate of peptide-chain elongation, eEF-2 is phosphorylated by a very specific Ca2+/calmodulin-dependent protein kinase (eEF-2 kinase) causing its complete inactivation. The decrease in eEF-2 phosphorylation induced by insulin reflects a fall in eEF-2 kinase activity. Rapamycin, a macrolide immunosuppressant which blocks the signalling pathway leading to the stimulation of the 70/85 kDa ribosomal protein S6 kinases, substantially blocks the activation of elongation, the fall in eEF-2 phosphorylation and the decrease in eEF-2 kinase activity, suggesting that p70 S6 kinase (p70(S6k)) and eEF-2 kinase may lie on a common signalling pathway. Wortmannin, an inhibitor of phosphatidylinositide-3-OH kinase, had similar effects, eEF-2 kinase was phosphorylated in vitro by purified p70(S6k) but this had no significant effect on the in vitro activity of eEF-2 kinase.

Item Type: Article
Uncontrolled keywords: elongation factor-2; elongation factor-2 kinase; insulin; phosphorylation; rapamycin
Subjects: Q Science > QD Chemistry
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: F.D. Zabet
Date Deposited: 09 May 2009 09:46
Last Modified: 09 May 2009 09:46
Resource URI: http://kar.kent.ac.uk/id/eprint/18752 (The current URI for this page, for reference purposes)
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