Eukaryotic elongation factor-2 (eEF2): its regulation and peptide chain elongation

Cell Biochem Funct. 2011 Apr;29(3):227-34. doi: 10.1002/cbf.1740. Epub 2011 Mar 10.

Abstract

Regulation at the level of translation in eukaryotes is feasible because of the longer lifetime of eukaryotic mRNAs in the cell. The elongation stage of mRNA translation requires a substantial amount of energy and also eukaryotic elongation factors (eEFs). The important component of eEFs, i.e. eEF2 promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome. Mostly the eEF2 is regulated by phosphorylation and dephosphorylation by a specific kinase known as eEF2 kinase, which itself is up-regulated by various mechanisms in the eukaryotic cell. The activity of this kinase is dependent on calcium ions and calmodulin. Recently it has been shown that the activity of eEF2 kinase is regulated by MAP kinase signalling and mTOR signalling pathway. There are also various stimuli that control the peptide chain elongation in eukaryotic cell; some stimuli inhibit and some activate eEF2. These reports provide the mechanisms by which cells likely serve to slow down protein synthesis and conserve energy under nutrient deprived conditions via regulation of eEF2. The regulation via eEF2 has also been seen in mammary tissue of lactating cows, suggesting that eEF2 may be a limiting factor in milk protein synthesis. Regulation at this level provides the molecular understanding about the control of protein translocation reactions in eukaryotes, which is critical for numerous biological phenomenons. Further the elongation factors could be potential targets for regulation of protein synthesis like milk protein synthesis and hence probably its foreseeable application to synthetic biology.

Publication types

  • Review

MeSH terms

  • Animals
  • Calcium / metabolism
  • Calmodulin / metabolism
  • Cattle
  • Elongation Factor 2 Kinase / genetics
  • Elongation Factor 2 Kinase / metabolism*
  • Eukaryota
  • Female
  • Gene Expression Regulation
  • Guanosine Triphosphate / metabolism
  • Humans
  • Lactation / genetics
  • Lactation / metabolism
  • Milk Proteins / genetics
  • Milk Proteins / metabolism*
  • Mitogen-Activated Protein Kinases / genetics
  • Mitogen-Activated Protein Kinases / metabolism
  • Peptide Elongation Factor 2 / genetics
  • Peptide Elongation Factor 2 / metabolism*
  • Phosphorylation
  • Protein Biosynthesis* / physiology
  • RNA, Messenger / metabolism
  • Ribosomes / metabolism
  • Signal Transduction / physiology
  • Synthetic Biology
  • TOR Serine-Threonine Kinases / genetics
  • TOR Serine-Threonine Kinases / metabolism

Substances

  • Calmodulin
  • Milk Proteins
  • Peptide Elongation Factor 2
  • RNA, Messenger
  • Guanosine Triphosphate
  • TOR Serine-Threonine Kinases
  • Elongation Factor 2 Kinase
  • Mitogen-Activated Protein Kinases
  • Calcium