Ca2+/calmodulin‐dependent phosphorylation of elongation factor 2

FEBS Letters

Ryazanov, Alexey G.¹ 

[1] Institute of Protein Research, Academy of Sciences of the USSR, 142292 Pushchino, Moscow Region, USSR

关键词: Protein phosphorylation;    Calmodulin;    Ca2+;    Elongation factor 2;    Translation regulation;   

DOI  :  10.1016/0014-5793(87)80081-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 M_r ∼ 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.

【 授权许可】

Unknown