Ca2+/calmodulin‐dependent phosphorylation of elongation factor 2
- 20 April 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 214 (2) , 331-334
- https://doi.org/10.1016/0014-5793(87)80081-9
Abstract
Incubation of a ribosome‐free extract of rabbit reticulocytes or rat liver with [γ‐32P]ATP and Ca2+ results in incorporation of 32P predominantly into a single polypeptide of Mr ∼ 100 000. This polypeptide is identified as elongation factor 2 (EF‐2). Phosphorylation of EF‐2 is strictly Ca2+‐dependent and can be inhibited by the calmodulin antagonist trifluoperazine. It is suggested that the Ca2+/calmodulin‐dependent phosphorylation of EF‐2 is involved in regulation of protein biosynthesis.Keywords
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