AI Article Synopsis
- The protein kinase Mps1 is crucial for the spindle assembly checkpoint (SAC) and interacts with Ndc80, a component of the kinetochore complex in yeast.
- Mps1 can phosphorylate the N-terminal domain of Ndc80 both in vitro and in vivo, and mutations to the phosphorylation sites disrupt checkpoint signaling during drug treatment.
- Mutating the same sites to mimic constant phosphorylation leads to a metaphase arrest due to continuous SAC activation, suggesting that Mps1's phosphorylation of Ndc80 is essential for activating the SAC at kinetochores.
Article Abstract
The protein kinase Mps1 is, among others, essential for the spindle assembly checkpoint (SAC). We found that Saccharomyces cerevisiae Mps1 interacts physically with the N-terminal domain of Ndc80 (Ndc80(1-257)), a constituent of the Ndc80 kinetochore complex. Furthermore, Mps1 effectively phosphorylates Ndc80(1-257) in vitro and facilitates Ndc80 phosphorylation in vivo. Mutating 14 of the phosphorylation sites to alanine results in compromised checkpoint signalling upon nocodazole treatment of mutants. Mutating the identical sites to aspartate (to simulate constitutive phosphorylation) causes a metaphase arrest with wild-type-like bipolar kinetochore-microtubule attachment. This arrest is due to a constitutively active SAC and consequently the inviable aspartate mutant can be rescued by disrupting SAC signalling. Therefore, we conclude that a putative Mps1-dependent phosphorylation of Ndc80 is important for SAC activation at kinetochores.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2683709 | PMC |
| http://dx.doi.org/10.1038/emboj.2009.62 | DOI Listing |
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