eEF2 antibody Usage And Synthesis

Source

Rabbit

Reactivity

Human;Mouse;Rat;Monkey;D. melanogaster

Background

Eukaryotic elongation factor 2 catalyzes the translocation of peptidyl-tRNA from the A site to the P site on the ribosome. It has been shown that phosphorylation of eEF2 at threonine 56 by eEF2 kinase inhibits its activity. eEF2 kinase is normally dependent on Ca2+ ions and calmodulin. eEF2 kinase can also be activated by PKA in response to elevated cAMP levels, which are generally increased in stress- or starvation-related conditions. A variety of treatments known to raise intracellular Ca2+ or cAMP levels have been shown to result in increased phosphorylation of eEF2, and thus to inhibit peptide-chain elongation. The inactive phosphorylated eEF2 can be converted to its active nonphosphorylated form by a protein phosphatase, most likely a form of protein phosphatase-2A. Insulin, which activates protein synthesis in a wide range of cell types, induces rapid dephosphorylation of eEF2 through mTOR signaling and may involve modulation of the activity of the PP-2A or the eEF2 kinase or both.

References

[1] Nairn, A.C. and Palfrey, H.C. (1987) J. Biol. Chem. 262, 17299-17303.
[2] Ryazanov, A.G. et al. (1988) Nature 334, 170-173.
[3] Carlberg, U. et al. (1990) Eur. J. Biochem. 191, 639-645.
[4] Redpath, N.T. et al. (1993) Eur. J. Biochem. 213, 689-699.
[5] Nairn, A.C. et al. (1985) Proc. Natl. Acad. Sci. USA 82, 7939-7943.
[6] Palfrey, H.C. et al. (1987) J. Biol. Chem. 262, 9785-9792.
[7] Redpath, N.T. and Proud, C.G. (1993) Biochem. J. 293, 31-34.
[8] Diggle, T. et al. (1998) Biochem. J. 336, 525-529.
[9] Hovland, R. et al. (1999) FEBS Lett. 444, 97-101.
[10] Proud, C. (2000) Translational Control of Gene Expression. Cold Spring Harbor Laboratory Press, NY, 719-739.

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