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 language | English (US) |
|---|---|
| Pages (from-to) | 11523-11538 |
| Number of pages | 16 |
| Journal | International Journal of Molecular Sciences |
| Volume | 15 |
| Issue number | 7 |
| DOIs | |
| State | Published - Jun 27 2014 |
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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)
Cite this
Phosphorylation stoichiometries of human Eukaryotic initiation factors. / Andaya, Armann; Villa, Nancy; Jia, Weitao; Fraser, Christopher S.; Leary, Julie A.
In: International Journal of Molecular Sciences, Vol. 15, No. 7, 27.06.2014, p. 11523-11538.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Phosphorylation stoichiometries of human Eukaryotic initiation factors
AU - Andaya, Armann
AU - Villa, Nancy
AU - Jia, Weitao
AU - Fraser, Christopher S.
AU - Leary, Julie A.
PY - 2014/6/27
Y1 - 2014/6/27
N2 - 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.
AB - 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.
KW - Eukaryotic initiation factor
KW - Mass spectrometry
KW - Phosphorylation quantification
KW - Translation
UR - http://www.scopus.com/inward/record.url?scp=84903432949&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84903432949&partnerID=8YFLogxK
U2 - 10.3390/ijms150711523
DO - 10.3390/ijms150711523
M3 - Article
VL - 15
SP - 11523
EP - 11538
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
SN - 1661-6596
IS - 7
ER -