Abstract
Elongation factor-1 (EF-1) is a major substrate for cdc2 kinase in Xenopus oocytes. The guanine-nucleotide exchange factor EF-1βγδ, appears to have a highly complex macromolecular structure containing several GTP/GDP exchange proteins, valyl-tRNA synthetase, and a putative anchoring protein EF-1γ. During meiotic cell division, the factor becomes phosphorylated by cdc2 kinase, not only on EF-1γ, but also on two different phospho-acceptors on EF-1δ. Phosphorylation is concomitant with changes in protein synthesis in vivo. Xenopus oocytes, and potentially all cells, contain a multitude of heteromeric forms of the complex which postulates that EF-1βγδ is not a “house keeping” factor but a sophisticated regulatory element.
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Bellé, R., Minella, O., Cormier, P., Morales, J., Poulhe, R., Mulner-Lorillon, O. (1995). Phosphorylation of elongation factor-1 (EF-1) by cdc2 kinase. In: Meijer, L., Guidet, S., Tung, H.Y.L. (eds) Progress in Cell Cycle Research. Progress in Cell Cycle Research. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1809-9_21
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