Phosphorylation stoichiometries of human Eukaryotic initiation factors

Armann Andaya, Nancy Villa, Weitao Jia, Christopher S. Fraser, Julie A. Leary

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

Eukaryotic translation initiation factors are the principal molecular effectors regulating the process converting nucleic acid to functional protein. Commonly referred to as eIFs (eukaryotic initiation factors), this suite of proteins is comprised of at least 25 individual subunits that function in a coordinated, regulated, manner during mRNA translation. Multiple facets of eIF regulation have yet to be elucidated; however, many of the necessary protein factors are phosphorylated. Herein, we have isolated, identified and quantified phosphosites from eIF2, eIF3, and eIF4G generated from log phase grown HeLa cell lysates. Our investigation is the first study to globally quantify eIF phosphosites and illustrates differences in abundance of phosphorylation between the residues of each factor. Thus, identification of those phosphosites that exhibit either high or low levels of phosphorylation under log phase growing conditions may aid researchers to concentrate their investigative efforts to specific phosphosites that potentially harbor important regulatory mechanisms germane to mRNA translation.

Original languageEnglish (US)
Pages (from-to)11523-11538
Number of pages16
JournalInternational Journal of Molecular Sciences
Volume15
Issue number7
DOIs
StatePublished - Jun 27 2014

Keywords

  • Eukaryotic initiation factor
  • Mass spectrometry
  • Phosphorylation quantification
  • Translation

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Spectroscopy
  • Inorganic Chemistry
  • Catalysis
  • Molecular Biology
  • Computer Science Applications
  • Medicine(all)

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