Abstract
A new Ca2+/calmodulin-dependent protein kinase has been recently discovered in mammalian cells1,2. The major substrate of this kinase, a protein of relative molecular mass (Mr) ≈100,000 (100K), has been identified as elongation factor 2 (EF-2)3,4, which participates in protein synthesis. The in vivo activity of the EF-2 kinase depends upon growth factors and other agents affecting the level of Ca2+ and cAMP5,6. Its effect on EF-2 activity, however, remained obscure. This work shows that the phosphorylation of EF-2 by the EF-2 kinase results in a drastic inhibition of polyphenylalanine synthesis in poly(U)-directed translation. Phosphorylated EF-2 is completely inactive in translation and, moreover, inhibits the activity of non-phosphorylated EF-2. Dephosphorylation of EF-2 by phosphatase restores its activity. Hence, the phosphorylation of EF-2 directly affects the elongation stage of translation and thus represents a novel mechanism of translational control.
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Ryazanov, A., Shestakova, E. & Natapov, P. Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation. Nature 334, 170–173 (1988). https://doi.org/10.1038/334170a0
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DOI: https://doi.org/10.1038/334170a0
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