ArticleScientific reports2016
Membrane-association of mRNA decapping factors is independent of stress in budding yeast.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Transcriptome-wide mRNP condensation precedes stress granule formation and excludes new mRNAs.Molecular cell · 2025Article
- Transcriptome-wide mRNP condensation precedes stress granule formation and excludes new mRNAs.bioRxiv : the preprint server for biology · 2025Article
- Energy stress promotes P-bodies formation via lysine-63-linked polyubiquitination of HAX1.The EMBO journal · 2024Article
- Atlas of mRNA translation and decay for bacteria.Nature microbiology · 2023Article
- Seeking a Role for Translational Control by Alternative Polyadenylation inMicroorganisms · 2021Review
- Article
- Control of tissue size and development by a regulatory element in theAmerican journal of cancer research · 2017Article
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Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent evidence has suggested that the degradation of mRNA occurs on translating ribosomes or alternatively within RNA granules called P bodies, which are aggregates whose core constituents are mRNA decay proteins and RNA. In this study, we examined the mRNA decapping proteins, Dcp1, Dcp2, and Dhh1, using subcellular fractionation. We found that decapping factors co-sediment in the polysome fraction of a sucrose gradient and do not alter their behaviour with stress, inhibition of translation or inhibition of the P body formation. Importantly, their localisation to the polysome fraction is independent of the RNA, suggesting that these factors may be constitutively localised to the polysome. Conversely, polysomal and post-polysomal sedimentation of the decapping proteins was abolished with the addition of a detergent, which shifts the factors to the non-translating RNP fraction and is consistent with membrane association. Using a membrane flotation assay, we observed the mRNA decapping factors in the lower density fractions at the buoyant density of membrane-associated proteins. These observations provide further evidence that mRNA decapping factors interact with subcellular membranes, and we suggest a model in which the mRNA decapping factors interact with membranes to facilitate regulation of mRNA degradation.
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Registered trials
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