Nature. 1988 Jul 14;334(6178):170-3.

Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation.

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Institute of Protein Research, Academy of Sciences of the USSR, Moscow Region.

Abstract

A new Ca2+/calmodulin-dependent protein kinase has been recently discovered in mammalian cells. The major substrate of this kinase, a protein of relative molecular mass (Mr) approximately equal to 100,000 (100K), has been identified as elongation factor 2 (EF-2), 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 cAMP. 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.

PMID:: 3386756; [PubMed - indexed for MEDLINE]

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Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation.
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Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation.

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