ArticleeLife2016
Bistability of a coupled Aurora B kinase-phosphatase system in cell division.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed, 55 citations in OpenAlex.
- Microtubules guide Aurora B substrate geometries for accurate chromosome segregation.Science advances · 2026Article
- Large intra-chromosome heterogeneity leads to emergent nonlinear mechanics.Nature physics · 2026Article
- Article
- CellDynaMo-stochastic reaction-diffusion-dynamics model: Application to search-and-capture process of mitotic spindle assembly.PLoS computational biology · 2022Article
- Increased Aurora B expression reduces substrate phosphorylation and induces chromosomal instability.Frontiers in cell and developmental biology · 2022Article
- Tension promotes kinetochore-microtubule release by Aurora B kinase.The Journal of cell biology · 2021Article
- Cytokinesis regulators as potential diagnostic and therapeutic biomarkers for human hepatocellular carcinoma.Experimental biology and medicine (Maywood, N.J.) · 2021Review
- Derivation of stationary distributions of biochemical reaction networks via structure transformation.Communications biology · 2021Article
- Shake It Off: The Elimination of Erroneous Kinetochore-Microtubule Attachments and Chromosome Oscillation.International journal of molecular sciences · 2021Review
- Chiasmata and the kinetochore component Dam1 are crucial for elimination of erroneous chromosome attachments and centromere oscillation at meiosis I.Open biology · 2021Article
- Dynamic bistable switches enhance robustness and accuracy of cell cycle transitions.PLoS computational biology · 2021Article
- The Borealin dimerization domain interacts with Sgo1 to drive Aurora B-mediated spindle assembly.Molecular biology of the cell · 2020Article
- The whole is greater than the sum of its parts: at the intersection of order, disorder, and kinetochore function.Essays in biochemistry · 2020Review
- A Condensed View of the Chromosome Passenger Complex.Trends in cell biology · 2020Review
- Dynamics of kinetochore structure and its regulations during mitotic progression.Cellular and molecular life sciences : CMLS · 2020Review
- Mechanics of Multicentrosomal Clustering in Bipolar Mitotic Spindles.Biophysical journal · 2020Article
- Co-regulation of the antagonistic RepoMan:Aurora-B pair in proliferating cells.Molecular biology of the cell · 2020Article
- Untangling the contribution of Haspin and Bub1 to Aurora B function during mitosis.The Journal of cell biology · 2020Article
- Aurora B kinase activity is regulated by SET/TAF1 on Sgo2 at the inner centromere.The Journal of cell biology · 2019Article
- Enrichment of Aurora B kinase at the inner kinetochore controls outer kinetochore assembly.The Journal of cell biology · 2019Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
Aurora B kinase, a key regulator of cell division, localizes to specific cellular locations, but the regulatory mechanisms responsible for phosphorylation of substrates located remotely from kinase enrichment sites are unclear. Here, we provide evidence that this activity at a distance depends on both sites of high kinase concentration and the bistability of a coupled kinase-phosphatase system. We reconstitute this bistable behavior and hysteresis using purified components to reveal co-existence of distinct high and low Aurora B activity states, sustained by a two-component kinase autoactivation mechanism. Furthermore, we demonstrate these non-linear regimes in live cells using a FRET-based phosphorylation sensor, and provide a mechanistic theoretical model for spatial regulation of Aurora B phosphorylation. We propose that bistability of an Aurora B-phosphatase system underlies formation of spatial phosphorylation patterns, which are generated and spread from sites of kinase autoactivation, thereby regulating cell division.
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What OpenQuestion holds
Registered trials
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.