Regulation of the phosphorylation of elongation factor 2 by MEK-dependent signalling in adult rat cardiomyocytes
Regulation of the phosphorylation of elongation factor 2 by MEK-dependent signalling in adult rat cardiomyocytes
The Gq-coupled agonists phenylephrine and endothelin-1 each activate protein synthesis in cardiomyocytes as part of the programme that leads to cardiac hypertrophy. Here we show that they each induce the dephosphorylation of elongation factor (eEF) 2, a protein that in its dephosphorylated state mediates the translocation step of elongation. The ability of both agonists to induce dephosphorylation of eEF2 requires signalling via the mTOR and MEK/Erk signalling pathways, but is independent of phosphoinositide 3-kinase. Expression of an activated form of MEK leads to dephosphorylation of eEF2, in an mTOR independent manner, indicating that signalling via MEK/Erk suffices to cause dephosphorylation of eEF2.
translation, elongation, eEF2, MEK, cardiomyocyte, hypertrophy
285-289
Wang, Lijun
55ff0417-5993-46ee-8e5f-01a972c72f6a
Proud, Christopher G.
59dabfc8-4b44-4be8-a17f-578a58550cb3
6 November 2002
Wang, Lijun
55ff0417-5993-46ee-8e5f-01a972c72f6a
Proud, Christopher G.
59dabfc8-4b44-4be8-a17f-578a58550cb3
Wang, Lijun and Proud, Christopher G.
(2002)
Regulation of the phosphorylation of elongation factor 2 by MEK-dependent signalling in adult rat cardiomyocytes.
FEBS Letters, 531 (2), .
(doi:10.1016/S0014-5793(02)03536-6).
Abstract
The Gq-coupled agonists phenylephrine and endothelin-1 each activate protein synthesis in cardiomyocytes as part of the programme that leads to cardiac hypertrophy. Here we show that they each induce the dephosphorylation of elongation factor (eEF) 2, a protein that in its dephosphorylated state mediates the translocation step of elongation. The ability of both agonists to induce dephosphorylation of eEF2 requires signalling via the mTOR and MEK/Erk signalling pathways, but is independent of phosphoinositide 3-kinase. Expression of an activated form of MEK leads to dephosphorylation of eEF2, in an mTOR independent manner, indicating that signalling via MEK/Erk suffices to cause dephosphorylation of eEF2.
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Submitted date: 22 August 2002
Published date: 6 November 2002
Keywords:
translation, elongation, eEF2, MEK, cardiomyocyte, hypertrophy
Identifiers
Local EPrints ID: 56811
URI: http://eprints.soton.ac.uk/id/eprint/56811
ISSN: 0014-5793
PURE UUID: 37b97eeb-c6c7-4636-a3a0-b68bf88ec7e3
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Date deposited: 07 Aug 2008
Last modified: 15 Mar 2024 11:03
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Author:
Lijun Wang
Author:
Christopher G. Proud
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