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CA2 — EEF2

Text-mined interactions from Literome

Gschwendt et al., Skin Pharmacol 1988 (Cell Transformation, Neoplastic...) : Phosphorylation of EF-2 is dependent on Ca2+ and calmodulin, and inhibition of EF-2 phosphorylation by CsA is due to an interaction of CsA with calmodulin ... Since CsA inhibits specifically 12-O-tetradecanoylphorbol-13-acetate (TAP) stimulated but not basal protein synthesis in epidermis, it is proposed that Ca2+/calmodulin dependent phosphorylation of EF-2 is involved in the induction of the hyperplastic response by TPA and that CsA suppresses TPA effects by inhibition of EF-2-phosphorylation and perhaps other calmodulin dependent processes
Gschwendt et al., Biochem Biophys Res Commun 1988 : The weak immunosuppressant cyclosporine D as well as the immunologically inactive cyclosporine H are potent inhibitors in vivo of phorbol ester TPA induced biological effects in mouse skin and of Ca2+/calmodulin dependent EF-2 phosphorylation in vitro ... Furthermore, CsH, like CsA, inhibits the Ca2+/calmodulin dependent phosphorylation of the elongation factor 2 (EF-2) in vitro and the TPA induced increases in the amount of EF-2 in vivo
Ryazanov et al., FEBS Lett 1987 : 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
Albarracin et al., J Biol Chem 1994 : PRL treatment enhanced the Ca2+/calmodulin (CaM) dependent phosphorylation of endogenous EF-2 in luteal cytoplasmic extracts
Matsuda et al., J Biol Chem 1998 : It is suggested that the binding of Ca2+ to EF-3 is probably required for EF-2 to be a functional Ca2+ binding site and to induce exposure of the myristoyl group ; and that the binding of Ca2+ to EF-2 is important for the interaction with rhodopsin kinase