ArticleInternational journal of molecular sciences2014
Phosphorylation stoichiometries of human eukaryotic initiation factors.
Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Domain architecture of plant eukaryotic translation initiation factor 3 subunit E governs interaction with translational cis-elements to regulatepollen tube growth.The Plant cell · 2026Article
- Purification and characterization of recombinant human translation initiation factor eIF3.Protein science : a publication of the Protein Society · 2026Article
- eIF3d controls the persistent integrated stress response.Molecular cell · 2023Article
- Reconstitution of Multi-Protein Complexes through Ribozyme-Assisted Polycistronic Co-Expression.ACS synthetic biology · 2023Article
- Controlling tissue patterning by translational regulation of signaling transcripts through the core translation factor eIF3c.Developmental cell · 2021Article
- Structure of the RNA Specialized Translation Initiation Element that Recruits eIF3 to the 5'-UTR of c-Jun.Journal of molecular biology · 2020Article
- Phosphorylation and Signal Transduction Pathways in Translational Control.Cold Spring Harbor perspectives in biology · 2019Review
- Heterogeneity and specialized functions of translation machinery: from genes to organisms.Nature reviews. Genetics · 2018Review
- Human eIF3: from 'blobology' to biological insight.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Article
- eIF3 targets cell-proliferation messenger RNAs for translational activation or repression.Nature · 2015Article
- eIF2 interactions with initiator tRNA and eIF2B are regulated by post-translational modifications and conformational dynamics.Cell discovery · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
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.
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