ArticleMolecular biology of the cell2012
Constitutive dynein activity in She1 mutants reveals differences in microtubule attachment at the yeast spindle pole body.
Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- A stable microtubule bundle formed through an orchestrated multistep process controls quiescence exit.eLife · 2024Article
- High throughput mutagenesis and screening for yeast engineering.Journal of biological engineering · 2022Review
- The microtubule-associated protein She1 coordinates directional spindle positioning by spatially restricting dynein activity.Journal of cell science · 2021Article
- The Genetic and Physical Interactomes of theG3 (Bethesda, Md.) · 2020Article
- Astral microtubule forces alter nuclear organization and inhibit DNA repair in budding yeast.Molecular biology of the cell · 2019Article
- Microtubule dynamics regulation reconstituted in budding yeast lysates.Journal of cell science · 2018Article
- Microtubule cross-linking activity of She1 ensures spindle stability for spindle positioning.The Journal of cell biology · 2017Article
- Regulation of mitotic spindle disassembly by an environmental stress-sensing pathway in budding yeast.Genetics · 2014Article
- Stopped in its tracks: negative regulation of the dynein motor by the yeast protein She1.BioEssays : news and reviews in molecular, cellular and developmental biology · 2013Article
- Mechanisms of spindle positioning.The Journal of cell biology · 2013Review
- She1-mediated inhibition of dynein motility along astral microtubules promotes polarized spindle movements.Current biology : CB · 2012Article
- The yeast homologue of the microtubule-associated protein Lis1 interacts with the sumoylation machinery and a SUMO-targeted ubiquitin ligase.Molecular biology of the cell · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The organization of microtubules is determined in most cells by a microtubule-organizing center, which nucleates microtubule assembly and anchors their minus ends. In Saccharomyces cerevisiae cells lacking She1, cytoplasmic microtubules detach from the spindle pole body at high rates. Increased rates of detachment depend on dynein activity, supporting previous evidence that She1 inhibits dynein. Detachment rates are higher in G1 than in metaphase cells, and we show that this is primarily due to differences in the strengths of microtubule attachment to the spindle pole body during these stages of the cell cycle. The minus ends of detached microtubules are stabilized by the presence of γ-tubulin and Spc72, a protein that tethers the γ-tubulin complex to the spindle pole body. A Spc72-Kar1 fusion protein suppresses detachment in G1 cells, indicating that the interaction between these two proteins is critical to microtubule anchoring. Overexpression of She1 inhibits the loading of dynactin components, but not dynein, onto microtubule plus ends. In addition, She1 binds directly to microtubules in vitro, so it may compete with dynactin for access to microtubules. Overall, these results indicate that inhibition of dynein activity by She1 is important to prevent excessive detachment of cytoplasmic microtubules, particularly in G1 cells.
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