Phosphorylation of elongation factor-1 (EF-1) by cdc2 kinase

Prog Cell Cycle Res. 1995:1:265-70. doi: 10.1007/978-1-4615-1809-9_21.

Abstract

Elongation factor-1 (EF-1) is a major substrate for cdc2 kinase in Xenopus oocytes. The guanine-nucleotide exchange factor EF-1 beta gamma delta, appears to have a highly complex macromolecular structure containing several GTP/GDP exchange proteins, valyl-tRNA synthetase, and a putative anchoring protein EF-1 gamma. During meiotic cell division, the factor becomes phosphorylated by cdc2 kinase, not only on EF-1 gamma, but also on two different phospho-acceptors on EF-1 delta. 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-1 beta gamma delta is not a "house keeping" factor but a sophisticated regulatory element.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • CDC2 Protein Kinase / physiology*
  • Meiosis
  • Oocytes
  • Peptide Elongation Factor 1
  • Peptide Elongation Factors / metabolism*
  • Phosphorylation
  • Xenopus

Substances

  • Peptide Elongation Factor 1
  • Peptide Elongation Factors
  • CDC2 Protein Kinase