ArticleRNA (New York, N.Y.)2007
Microtubule disruption stimulates P-body formation.
Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
47 citing papers in PubMed, 80 citations in OpenAlex.
- The role of ER exit sites in maintaining P-body organization and integrity during Drosophila melanogaster oogenesis.EMBO reports · 2025Article
- Exploring the Role of the Processing Body in Plant Abiotic Stress Response.Current issues in molecular biology · 2024Review
- The role of ER exit sites in maintaining P-body organization and transmitting ER stress response duringbioRxiv : the preprint server for biology · 2024Article
- A distinct P-body-like granule is induced in response to the disruption of microtubule integrity in Saccharomyces cerevisiae.Genetics · 2022Article
- Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022Review
- Microtubule integrity regulates budding yeast RAM pathway gene expression.Frontiers in cell and developmental biology · 2022Article
- Pby1 is a direct partner of the Dcp2 decapping enzyme.Nucleic acids research · 2020Article
- Complex Interactions Between Membrane-Bound Organelles, Biomolecular Condensates and the Cytoskeleton.Frontiers in cell and developmental biology · 2020Review
- Aggregation of SND1 in Stress Granules is Associated with the Microtubule Cytoskeleton During Heat Shock Stimulus.Anatomical record (Hoboken, N.J. : 2007) · 2017Article
- Numerous interactions act redundantly to assemble a tunable size of P bodies inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- RNAi Screen Identifies Novel Regulators of RNP Granules in the Caenorhabditis elegans Germ Line.G3 (Bethesda, Md.) · 2016Article
- Membrane-association of mRNA decapping factors is independent of stress in budding yeast.Scientific reports · 2016Article
- General and MicroRNA-Mediated mRNA Degradation Occurs on Ribosome Complexes in Drosophila Cells.Molecular and cellular biology · 2015Article
- Tudor staphylococcal nuclease links formation of stress granules and processing bodies with mRNA catabolism in Arabidopsis.The Plant cell · 2015Article
- Somatic insulin signaling regulates a germline starvation response in Drosophila egg chambers.Developmental biology · 2015Article
- DNA Damage Response Checkpoint Activation Drives KP1019 Dependent Pre-Anaphase Cell Cycle Delay in S. cerevisiae.PloS one · 2015Article
- Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS?Frontiers in cellular neuroscience · 2015Review
- Viral activation of MK2-hsp27-p115RhoGEF-RhoA signaling axis causes cytoskeletal rearrangements, p-body disruption and ARE-mRNA stabilization.PLoS pathogens · 2015Article
- Divergence of the expression and subcellular localization of CCR4-associated factor 1 (CAF1) deadenylase proteins in Oryza sativa.Plant molecular biology · 2014Article
- mRNP granules. Assembly, function, and connections with disease.RNA biology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Processing bodies (P-bodies) are subcellular ribonucleoprotein (RNP) granules that have been hypothesized to be sites of mRNA degradation, mRNA translational control, and/or mRNA storage. Importantly, P-bodies are conserved from yeast to mammals and contain a common set of evolutionarily conserved protein constituents. P-bodies are dynamic structures and their formation appears to fluctuate in correlation with alterations in mRNA metabolism. Despite these observations, little is understood about how P-body structures are formed within the cell. In this study, we demonstrate a relationship between P-bodies and microtubules in the budding yeast, Saccharomyces cerevisiae. First, we demonstrate that disruption of microtubules by treatment with the drug benomyl leads to aggregation of P-body components. Consistent with this finding, we also demonstrate that disruption of microtubules by a temperature-sensitive allele of the major alpha tubulin, TUB1 (tub1-724) stimulates P-body formation. Second, we find that the alpha-tubulin protein Tub1 colocalizes with P-bodies upon microtubule destabilization. Third, we determine that a putative tubulin tyrosine ligase, encoded by YBR094W, is a protein component of P-bodies, providing additional evidence for a physical connection between P-bodies and microtubules. Finally, we establish that P-bodies formed by microtubule destabilization fail to correlate with global changes in the stability of mRNA or in general mRNA translation. These findings demonstrate that the aggregation of P-body components is linked to the intracellular microtubule network, and, further, that P-bodies formed by disruption of microtubules aggregate independent of broad alterations in either mRNA decay or mRNA translation.
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What OpenQuestion holds
Registered trials
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.