phosphorylation stoichiometries of human eukaryotic initiation factors

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ID: 157201
2014
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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.
Reference Key
andaya2014internationalphosphorylation Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Armann Andaya;Nancy Villa;Weitao Jia;Christopher S. Fraser;Julie A. Leary
Journal Intertax
Year 2014
DOI
10.3390/ijms150711523
URL
http://www.mdpi.com/1422-0067/15/7/11523
Keywords
Mass spectrometry translation

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