ArticleJournal of cell science2010
Membrane assembly modulates the stability of the meiotic spindle-pole body.
Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- Membrane and organelle rearrangement during ascospore formation in budding yeast.Microbiology and molecular biology reviews : MMBR · 2024Review
- Recruitment of the lipid kinase Mss4 to the meiotic spindle pole promotes prospore membrane formation inMolecular biology of the cell · 2023Article
- Autophagy of an Amyloid-like Translational Repressor Regulates Meiotic Exit.Developmental cell · 2020Article
- Analysis of the protein composition of the spindle pole body during sporulation in Ashbya gossypii.PloS one · 2019Article
- Article
- VPS13 regulates membrane morphogenesis during sporulation in Saccharomyces cerevisiae.Journal of cell science · 2012Article
- Sporulation in the budding yeast Saccharomyces cerevisiae.Genetics · 2011Review
- Sme4 coiled-coil protein mediates synaptonemal complex assembly, recombinosome relocalization, and spindle pole body morphogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Vesicle docking to the spindle pole body is necessary to recruit the exocyst during membrane formation in Saccharomyces cerevisiae.Molecular biology of the cell · 2010Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Spore formation in Saccharomyces cerevisiae is driven by de novo assembly of new membranes termed prospore membranes. A vesicle-docking complex called the meiosis II outer plaque (MOP) forms on the cytoplasmic faces of the spindle-pole bodies at the onset of meiosis II and serves as the initiation site for membrane formation. In this study, a fluorescence-recovery assay was used to demonstrate that the dynamics of the MOP proteins change coincident with the coalescence of precursor vesicles into a membrane. Proteins within the MOP exchange freely with a soluble pool prior to membrane assembly, but after membranes are formed they remain stably within the MOP. By contrast, constitutive spindle-pole-body proteins display low exchange in both conditions. The MOP component Ady4p plays a role in maintaining the integrity of the MOP complex, but this role differs depending on whether the MOP is associated with docked vesicles or a fully formed membrane. These results suggest an architectural rearrangement of the MOP coincident with vesicle fusion.
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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.