ArticleGenetics2010
Changes in the nuclear envelope environment affect spindle pole body duplication in Saccharomyces cerevisiae.
Article in Genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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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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
25 citing papers in PubMed, 42 citations in OpenAlex.
- A mutation in budding yeastmicroPublication biology · 2021Article
- SUNny Ways: The Role of the SUN-Domain Protein Mps3 Bridging Yeast Nuclear Organization and Lipid Homeostasis.Frontiers in genetics · 2020Review
- Synthetic Physical Interactions with the Yeast Centrosome.G3 (Bethesda, Md.) · 2019Article
- Yeast centrosome components form a noncanonical LINC complex at the nuclear envelope insertion site.The Journal of cell biology · 2019Article
- The budding yeast RSC complex maintains ploidy by promoting spindle pole body insertion.The Journal of cell biology · 2018Article
- Review
- Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes.The Journal of cell biology · 2017Article
- LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission yeast and human cells.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mitotic Nuclear Envelope Breakdown and Spindle Nucleation Are Controlled by Interphase Contacts between Centromeres and the Nuclear Envelope.Developmental cell · 2016Article
- The Malleable Nature of the Budding Yeast Nuclear Envelope: Flares, Fusion, and Fenestrations.Journal of cellular physiology · 2016Review
- Border Safety: Quality Control at the Nuclear Envelope.Trends in cell biology · 2016Review
- Article
- Kar5p is required for multiple functions in both inner and outer nuclear envelope fusion in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2014Article
- Tts1, the fission yeast homologue of the TMEM33 family, functions in NE remodeling during mitosis.Molecular biology of the cell · 2014Article
- The SUN protein Mps3 controls Ndc1 distribution and function on the nuclear membrane.The Journal of cell biology · 2014Article
- The nuclear basket proteins Mlp1p and Mlp2p are part of a dynamic interactome including Esc1p and the proteasome.Molecular biology of the cell · 2013Article
- Genetic analysis of Mps3 SUN domain mutants in Saccharomyces cerevisiae reveals an interaction with the SUN-like protein Slp1.G3 (Bethesda, Md.) · 2012Article
- Article
- Shaping the nucleus: factors and forces.Journal of cellular biochemistry · 2012Review
- Acetylation of the SUN protein Mps3 by Eco1 regulates its function in nuclear organization.Molecular biology of the cell · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The Saccharomyces cerevisiae nuclear membrane is part of a complex nuclear envelope environment also containing chromatin, integral and peripheral membrane proteins, and large structures such as nuclear pore complexes (NPCs) and the spindle pole body. To study how properties of the nuclear membrane affect nuclear envelope processes, we altered the nuclear membrane by deleting the SPO7 gene. We found that spo7Δ cells were sickened by the mutation of genes coding for spindle pole body components and that spo7Δ was synthetically lethal with mutations in the SUN domain gene MPS3. Mps3p is required for spindle pole body duplication and for a variety of other nuclear envelope processes. In spo7Δ cells, the spindle pole body defect of mps3 mutants was exacerbated, suggesting that nuclear membrane composition affects spindle pole body function. The synthetic lethality between spo7Δ and mps3 mutants was suppressed by deletion of specific nucleoporin genes. In fact, these gene deletions bypassed the requirement for Mps3p entirely, suggesting that under certain conditions spindle pole body duplication can occur via an Mps3p-independent pathway. These data point to an antagonistic relationship between nuclear pore complexes and the spindle pole body. We propose a model whereby nuclear pore complexes either compete with the spindle pole body for insertion into the nuclear membrane or affect spindle pole body duplication by altering the nuclear envelope environment.
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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.