ArticleMolecular and cellular biology2013
The yeast eukaryotic translation initiation factor 2B translation initiation complex interacts with the fatty acid synthesis enzyme YBR159W and endoplasmic reticulum membranes.
Article in Molecular and cellular biology, 2013. 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.
- Regulation and function of elF2B in neurological and metabolic disorders.Bioscience reports · 2022Review
- Critical Role for Saccharomyces cerevisiae Asc1p in Translational Initiation at Elevated Temperatures.Proteomics · 2018Article
- Article
- Farnesol inhibits translation to limit growth and filamentation inMicrobial cell (Graz, Austria) · 2017Article
- Drosophila TRF2 and TAF9 regulate lipid droplet size and phospholipid fatty acid composition.PLoS genetics · 2017Article
- A cell-based systems biology assessment of human blood to monitor immune responses after influenza vaccination.PloS one · 2015Article
- Environmental Interactions and Epistasis Are Revealed in the Proteomic Responses to Complex Stimuli.PloS one · 2015Article
- Mutational analysis of the alpha subunit of eIF2B provides insights into the role of eIF2B bodies in translational control and VWM disease.The Journal of biological chemistryArticle
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5 authors.
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Abstract
Using affinity purifications coupled with mass spectrometry and yeast two-hybrid assays, we show the Saccharomyces cerevisiae translation initiation factor complex eukaryotic translation initiation factor 2B (eIF2B) and the very-long-chain fatty acid (VLCFA) synthesis keto-reductase enzyme YBR159W physically interact. The data show that the interaction is specifically between YBR159W and eIF2B and not between other members of the translation initiation or VLCFA pathways. A ybr159wΔ null strain has a slow-growth phenotype and a reduced translation rate but a normal GCN4 response to amino acid starvation. Although YBR159W localizes to the endoplasmic reticulum membrane, subcellular fractionation experiments show that a fraction of eIF2B cofractionates with lipid membranes in a YBR159W-independent manner. We show that a ybr159wΔ yeast strain and other strains with null mutations in the VLCFA pathway cause eIF2B to appear as numerous foci throughout the cytoplasm.
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Registered trials
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