ArticleJournal of proteome research2011
Assessing the components of the eIF3 complex and their phosphorylation status.
Article in Journal of proteome research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- DivergentLife science alliance · 2025Article
- Knockdown of eIF3a alleviates pulmonary arterial hypertension by inhibiting endothelial-to-mesenchymal transition via TGFβ1/SMAD pathway.Journal of translational medicine · 2025Article
- The eIF3 complex of Leishmania-subunit composition and mode of recruitment to different cap-binding complexes.Nucleic acids research · 2015Article
- Differential phosphorylation of a regulatory subunit of protein kinase CK2 by target of rapamycin complex 1 signaling and the Cdc-like kinase Kns1.The Journal of biological chemistry · 2015Article
- Control of Paip1-eukayrotic translation initiation factor 3 interaction by amino acids through S6 kinase.Molecular and cellular biology · 2014Article
- Quantitative phosphoproteomics analysis of nitric oxide-responsive phosphoproteins in cotton leaf.PloS one · 2014Article
- Proteomics-based methods for discovery, quantification, and validation of protein-protein interactions.Analytical chemistry · 2013Review
- Novel insights into the architecture and protein interaction network of yeast eIF3.RNA (New York, N.Y.) · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The eukaryotic initiation factor 3 (eIF3) is an essential, highly conserved multiprotein complex that is a key component in the recruitment and assembly of the translation initiation machinery. To better understand the molecular function of eIF3, we examined its composition and phosphorylation status in Saccharomyces cerevisiae. The yeast eIF3 complex contains five core components: Rpg1, Nip1, Prt1, Tif34, and Tif35. 2-D LC-MS/MS analysis of affinity purified eIF3 complexes showed that several other initiation factors (Fun12, Tif5, Sui3, Pab1, Hcr1, and Sui1) and the casein kinase 2 complex (CK2) copurify. In Vivo metabolic labeling of proteins with (32)P revealed that Nip1 is phosphorylated. Using 2-D LC-MS/MS analysis of eIF3 complexes, we identified Prt1 phosphopeptides indicating phosphorylation at S22 and T707 and a Tif5 phosphopeptide with phosphorylation at T191. Additionally, we used immobilized metal affinity chromatography (IMAC) to enrich for eIF3 phosphopeptides and tandem mass spectrometry to identify phosphorylated residues. We found that three CK2 consensus sequences in Nip1 are phosphorylated: S98, S99, and S103. Using in vitro kinase assays, we showed that CK2 phophorylates Nip1 and that a synthetic Nip1 peptide containing S98, S99, and S103 competitively inhibits the reaction. Replacement of these three Nip1 serines with alanines causes a slow growth phenotype.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.