ArticleStructure (London, England : 1993)2011
Structure of a Blinkin-BUBR1 complex reveals an interaction crucial for kinetochore-mitotic checkpoint regulation via an unanticipated binding Site.
Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 44 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
44 citing papers in PubMed, 75 citations in OpenAlex.
- BubR1 TPR domain supports the mitotic checkpoint by promoting MCC formation and MCC-APC/C interaction.Communications biology · 2026Article
- Interplay of kinetochores and catalysts drives rapid assembly of the mitotic checkpoint complex.Nature communications · 2025Article
- Article
- 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
- Multimerization of a disordered kinetochore protein promotes accurate chromosome segregation by localizing a core dynein module.The Journal of cell biology · 2024Article
- BubR1 recruitment to the kinetochore via Bub1 enhances spindle assembly checkpoint signaling.Molecular biology of the cell · 2022Article
- On the Regulation of Mitosis by the Kinetochore, a Macromolecular Complex and Organising Hub of Eukaryotic Organisms.Sub-cellular biochemistry · 2022Article
- Knl1 participates in spindle assembly checkpoint signaling in maize.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Identification of Seven Cell Cycle-Related Genes with Unfavorable Prognosis and Construction of their TF-miRNA-mRNA regulatory network in Breast Cancer.Journal of Cancer · 2021Article
- The Bub1-TPR Domain Interacts Directly with Mad3 to Generate Robust Spindle Checkpoint Arrest.Current biology : CB · 2019Article
- Ectopic Activation of the Spindle Assembly Checkpoint Signaling Cascade Reveals Its Biochemical Design.Current biology : CB · 2019Article
- Microcephaly Modeling of Kinetochore Mutation Reveals a Brain-Specific Phenotype.Cell reports · 2018Article
- Leader of the SAC: molecular mechanisms of Mps1/TTK regulation in mitosis.Open biology · 2018Review
- The Ndc80 complex targets Bod1 to human mitotic kinetochores.Open biology · 2017Article
- Molecular analysis of 23 Pakistani families with autosomal recessive primary microcephaly using targeted next-generation sequencing.Journal of human genetics · 2017Article
- The Ins and Outs of Aurora B Inner Centromere Localization.Frontiers in cell and developmental biology · 2017Review
- Association between polymorphisms in segregation genes BUB1B and TTK and gastric cancer risk.Radiology and oncology · 2016Article
- Article
- Cryo-EM of Mitotic Checkpoint Complex-Bound APC/C Reveals Reciprocal and Conformational Regulation of Ubiquitin Ligation.Molecular cell · 2016Article
- Refining the phenotype associated with CASC5 mutation.Neurogenetics · 2016Article
Corrections and comments
- Erratum issued
Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
The maintenance of genomic stability relies on the spindle assembly checkpoint (SAC), which ensures accurate chromosome segregation by delaying the onset of anaphase until all chromosomes are properly bioriented and attached to the mitotic spindle. BUB1 and BUBR1 kinases are central for this process and by interacting with Blinkin, link the SAC with the kinetochore, the macromolecular assembly that connects microtubules with centromeric DNA. Here, we identify the Blinkin motif critical for interaction with BUBR1, define the stoichiometry and affinity of the interaction, and present a 2.2 Å resolution crystal structure of the complex. The structure defines an unanticipated BUBR1 region responsible for the interaction and reveals a novel Blinkin motif that undergoes a disorder-to-order transition upon ligand binding. We also show that substitution of several BUBR1 residues engaged in binding Blinkin leads to defects in the SAC, thus providing the first molecular details of the recognition mechanism underlying kinetochore-SAC signaling.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.