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Regulation of the phosphorylation of elongation factor 2 by MEK‐dependent signalling in adult rat cardiomyocytes
Author(s) -
Wang Lijun,
Proud Christopher G
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03536-6
Subject(s) - dephosphorylation , phosphorylation , microbiology and biotechnology , mapk/erk pathway , elongation factor , kinase , chemistry , biology , biochemistry , phosphatase , ribosome , rna , gene
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.