ArticlePloS one2011
Quantitative mass spectrometry analysis reveals similar substrate consensus motif for human Mps1 kinase and Plk1.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 72 citations in OpenAlex.
- Kinetochore clustering is mediated by Mps1 phosphorylation of conserved MELT motifs in Stu1.The Journal of cell biology · 2026Article
- Kinetochore clustering is mediated by Mps1 phosphorylation of conserved MELT motifs in Stu1.bioRxiv : the preprint server for biology · 2026Article
- Chemical Genetics with SP600125 Reveals That Mps1 Protein Kinase Works as a Regulatory Element in Post-embryonic Development of theACS omega · 2025Article
- A chemical-genetic system to rapidly inhibit the PP2A-B56 phosphatase reveals a role at metaphase kinetochores.Nature communications · 2025Article
- Recent Progress on the Localization of PLK1 to the Kinetochore and Its Role in Mitosis.International journal of molecular sciences · 2022Review
- Spindle assembly checkpoint activation and silencing at kinetochores.Seminars in cell & developmental biology · 2021Review
- The association of Plk1 with the astrin-kinastrin complex promotes formation and maintenance of a metaphase plate.Journal of cell science · 2021Article
- BUB1 and CENP-U, Primed by CDK1, Are the Main PLK1 Kinetochore Receptors in Mitosis.Molecular cell · 2021Article
- Kinetochore phosphatases suppress autonomous Polo-like kinase 1 activity to control the mitotic checkpoint.The Journal of cell biology · 2020Article
- Mps1 dimerization and multisite interactions with Ndc80 complex enable responsive spindle assembly checkpoint signaling.Journal of molecular cell biology · 2020Article
- Cyclin B1-Cdk1 facilitates MAD1 release from the nuclear pore to ensure a robust spindle checkpoint.The Journal of cell biology · 2020Article
- Review
- Checkpoint signaling and error correction require regulation of the MPS1 T-loop by PP2A-B56.The Journal of cell biology · 2019Article
- CDK1-CCNB1 creates a spindle checkpoint-permissive state by enabling MPS1 kinetochore localization.The Journal of cell biology · 2019Article
- Recent Progress on the Localization of the Spindle Assembly Checkpoint Machinery to Kinetochores.Cells · 2019Review
- Leader of the SAC: molecular mechanisms of Mps1/TTK regulation in mitosis.Open biology · 2018Review
- Mps1 Phosphorylates Its N-Terminal Extension to Relieve Autoinhibition and Activate the Spindle Assembly Checkpoint.Current biology : CB · 2018Article
- Kinase and Phosphatase Cross-Talk at the Kinetochore.Frontiers in cell and developmental biology · 2018Review
- MAD1: Kinetochore Receptors and Catalytic Mechanisms.Frontiers in cell and developmental biology · 2018Review
- Mechanisms of Mitotic Kinase Regulation: A Structural Perspective.Frontiers in cell and developmental biology · 2018Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMembers of the Mps1 kinase family play an essential and evolutionarily conserved role in the spindle assembly checkpoint (SAC), a surveillance mechanism that ensures accurate chromosome segregation during mitosis. Human Mps1 (hMps1) is highly phosphorylated during mitosis and many phosphorylation sites have been identified. However, the upstream kinases responsible for these phosphorylations are not presently known. METHODOLOGY/PRINCIPAL
findingsHere, we identify 29 in vivo phosphorylation sites in hMps1. While in vivo analyses indicate that Aurora B and hMps1 activity are required for mitotic hyper-phosphorylation of hMps1, in vitro kinase assays show that Cdk1, MAPK, Plk1 and hMps1 itself can directly phosphorylate hMps1. Although Aurora B poorly phosphorylates hMps1 in vitro, it positively regulates the localization of Mps1 to kinetochores in vivo. Most importantly, quantitative mass spectrometry analysis demonstrates that at least 12 sites within hMps1 can be attributed to autophosphorylation. Remarkably, these hMps1 autophosphorylation sites closely resemble the consensus motif of Plk1, demonstrating that these two mitotic kinases share a similar substrate consensus. CONCLUSIONS/SIGNIFICANCE: hMps1 kinase is regulated by Aurora B kinase and its autophosphorylation. Analysis on hMps1 autophosphorylation sites demonstrates that hMps1 has a substrate preference similar to Plk1 kinase.
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