ArticleMolecular and cellular biology2011
Protein interaction domain mapping of human kinetochore protein Blinkin reveals a consensus motif for binding of spindle assembly checkpoint proteins Bub1 and BubR1.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 105 citations in OpenAlex.
- BubR1 TPR domain supports the mitotic checkpoint by promoting MCC formation and MCC-APC/C interaction.Communications biology · 2026Article
- CDK1-dependent N-terminal NuMA phosphorylation promotes dynein-dynactin-NuMA assembly for accurate chromosome segregation.Cell reports · 2026Article
- Functional framework of the kinetochore and spindle assembly checkpoint in Arabidopsis.Plant physiology · 2025Article
- CENcyclopedia: dynamic landscape of kinetochore architecture throughout the cell cycle.Nature communications · 2025Article
- Phospho-KNL-1 recognition by a TPR domain targets the BUB-1-BUB-3 complex to C. elegans kinetochores.The Journal of cell biology · 2024Article
- Structure of the human outer kinetochore KMN network complex.Nature structural & molecular biology · 2024Article
- Multimerization of a disordered kinetochore protein promotes accurate chromosome segregation by localizing a core dynein module.The Journal of cell biology · 2024Article
- Role of spindle assembly checkpoint proteins in gametogenesis and embryogenesis.Frontiers in cell and developmental biology · 2024Review
- Phosphorylation of Bub1 by Mph1 promotes Bub1 signaling at the kinetochore to ensure accurate chromosome segregation.The Journal of biological chemistry · 2024Article
- Genetic Primary Microcephalies: When Centrosome Dysfunction Dictates Brain and Body Size.Cells · 2023Review
- Article
- BubR1 recruitment to the kinetochore via Bub1 enhances spindle assembly checkpoint signaling.Molecular biology of the cell · 2022Article
- Kre28-Spc105 interaction is essential for Spc105 loading at the kinetochore.Open biology · 2022Article
- On the Regulation of Mitosis by the Kinetochore, a Macromolecular Complex and Organising Hub of Eukaryotic Organisms.Sub-cellular biochemistry · 2022Article
- Zombies Never Die: The Double Life Bub1 Lives in Mitosis.Frontiers in cell and developmental biology · 2022Review
- Knl1 participates in spindle assembly checkpoint signaling in maize.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Bub1 kinase in the regulation of mitosis.Animal cells and systems · 2021Review
- The centromere comes into focus: from CENP-A nucleosomes to kinetochore connections with the spindle.Open biology · 2020Review
- Article
- Nearly complete deletion of BubR1 causes microcephaly through shortened mitosis and massive cell death.Human molecular genetics · 2019Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The kinetochore is a supramolecular structure essential for microtubule attachment and the mitotic checkpoint. Human blinkin/human Spc105 (hSpc105)/hKNL1 was identified originally as a mixed-lineage leukemia (MLL) fusion partner and later as a kinetochore component. Blinkin directly binds to several structural and regulatory proteins, but the precise binding sites have not been defined. Here, we report distinct and essential binding domains for Bub1 and BubR1 (here designated Bubs) at the N terminus of blinkin and for Zwint-1 and hMis14/hNsl1 at the C terminus. The minimal binding sites for Bub1 and BubR1 are separate but contain a consensus KI motif, KI(D/N)XXXF(L/I)XXLK. RNA interference (RNAi)-mediated replacement with mutant blinkin reveals that the Bubs-binding domain is functionally important for chromosome alignment and segregation. We also provide evidence that hMis14 mediates hNdc80 binding to blinkin at the kinetochore. The C-terminal fragment of blinkin locates at kinetochores in a dominant-negative fashion by displacing endogenous blinkin from kinetochores. This negative dominance is relieved by mutations of the hMis14 binding PPSS motif on the C terminus of blinkin or by fusion of the N sequence that binds to Bub1 and BubR1. Taken together, these results indicate that blinkin functions to connect Bub1 and BubR1 with the hMis12, Ndc80, and Zwint-1 complexes, and disruption of this connection may lead to tumorigenesis.
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