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CALM3 — 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
:
It is suggested that the
Ca2+/calmodulin dependent phosphorylation of
EF-2 is involved in regulation of protein biosynthesis
Nairn et al., J Biol Chem 1987
:
These results suggest that intracellular Ca2+ inhibits protein synthesis in mammalian cells via
CaM dependent protein kinase III catalyzed phosphorylation of
EF-2
Bagaglio et al., Cell Growth Differ 1994
(Glioma) :
To determine whether
CaM dependent phosphorylation of
EF-2 is linked, in general, to cellular division, we studied the phosphorylation of EF-2 in proliferating and growth arrested C6 cells and in proliferating, primary cultures of normal glia ... Therefore, the
CaM dependent phosphorylation of
EF-2 appears to be associated with cellular proliferation in normal and malignant glia in the rat
Albarracin et al., J Biol Chem 1994
:
PRL treatment enhanced the
Ca2+/calmodulin (CaM) dependent phosphorylation of endogenous
EF-2 in luteal cytoplasmic extracts