ArticleMolecular biology of the cell2016
Dual mechanisms regulate the recruitment of spindle assembly checkpoint proteins to the budding yeast kinetochore.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Manipulation and Analysis of Cell Cycle-Dependent Processes in Budding Yeast.Journal of visualized experiments : JoVE · 2025Article
- lncreased risk of slippage upon disengagement of the mitotic checkpoint.PLoS computational biology · 2025Article
- Signaling protein abundance modulates the strength of the spindle assembly checkpoint.Current biology : CB · 2023Article
- Aurora B phosphorylates Bub1 to promote spindle assembly checkpoint signaling.Current biology : CB · 2022Article
- Kre28-Spc105 interaction is essential for Spc105 loading at the kinetochore.Open biology · 2022Article
- Molecular mechanism of Mad1 kinetochore targeting by phosphorylated Bub1.EMBO reports · 2021Article
- Chemical tools for dissecting cell division.Nature chemical biology · 2021Review
- Article
- A stochastic model for error correction of kinetochore-microtubule attachments in budding yeast.PloS one · 2020Article
- Delineating the contribution of Spc105-bound PP1 to spindle checkpoint silencing and kinetochore microtubule attachment regulation.The Journal of cell biology · 2019Article
- Ectopic Activation of the Spindle Assembly Checkpoint Signaling Cascade Reveals Its Biochemical Design.Current biology : CB · 2019Article
- The Kinetochore Protein Spc105, a Novel Interaction Partner of LaeA, Regulates Development and Secondary Metabolism inFrontiers in microbiology · 2019Article
- Regulation of kinetochore configuration during mitosis.Current genetics · 2018Review
- A Cell Biological Perspective on Past, Present and Future Investigations of the Spindle Assembly Checkpoint.Biology · 2016Review
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Recruitment of spindle assembly checkpoint (SAC) proteins by an unattached kinetochore leads to SAC activation. This recruitment is licensed by the Mps1 kinase, which phosphorylates the kinetochore protein Spc105 at one or more of its six MELT repeats. Spc105 then recruits the Bub3-Bub1 and Mad1-Mad2 complexes, which produce the inhibitory signal that arrests cell division. The strength of this signal depends, in part, on the number of Bub3-Bub1 and Mad1-Mad2 molecules that Spc105 recruits. Therefore regulation of this recruitment will influence SAC signaling. To understand this regulation, we established the physiological binding curves that describe the binding of Bub3-Bub1 and Mad1-Mad2 to the budding yeast kinetochore. We find that the binding of both follows the mass action law. Mps1 likely phosphorylates all six MELT repeats of Spc105. However, two mechanisms prevent Spc105 from recruiting six Bub3-Bub1 molecules: low Bub1 abundance and hindrance in the binding of more than one Bub3-Bub1 molecule to the same Spc105. Surprisingly, the kinetochore recruits two Mad1-Mad2 heterotetramers for every Bub3-Bub1 molecule. Finally, at least three MELT repeats per Spc105 are needed for accurate chromosome segregation. These data reveal that kinetochore-intrinsic and -extrinsic mechanisms influence the physiological operation of SAC signaling, potentially to maximize chromosome segregation accuracy.
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