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cAMP inhibits translation by inducing Ca 2+ /calmodulin‐independent elongation factor 2 kinase activity in IPC‐81 cells
Author(s) -
Hovland R.,
Eikhom T.S.,
Proud C.G.,
Cressey L.I.,
Lanotte M.,
Døskeland S.O.,
Houge G.
Publication year - 1999
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(99)00039-3
Subject(s) - calmodulin , elongation , elongation factor , translation (biology) , chemistry , kinase , eukaryotic translation elongation factor 1 alpha 1 , protein kinase a , microbiology and biotechnology , biochemistry , biophysics , biology , enzyme , gene , messenger rna , materials science , rna , ribosome , metallurgy , ultimate tensile strength
Treatment of IPC‐81 cells led to inhibition of protein synthesis, which was accompanied by an increase in the average size of polysomes and a decreased rate of elongation, indicating that it involved inhibition of peptide chain elongation. This inhibition was also associated with increased phosphorylation of elongation factor eEF2 (which inhibits its activity) and enhanced Ca 2+ /calmodulin‐independent activity of eEF2 kinase. Previous work has shown that phosphorylation of eEF2 kinase by cAMP‐dependent protein kinase (cAPK) in vitro induces such activator‐independent activity, and the present data show that such a mechanism can occur in intact cells to link physiological levels of cAPK activation with inhibition of protein synthesis.