Chromosome biorientation requires Aurora B’s spatial separation from its outer kinetochore substrates, but not its turnover at kinetochores

Li, Shuyu; Garcia-Rodriguez, Luis J.; Tanaka, Tomoyuki U.

doi:10.1016/j.cub.2023.09.006

Cited by 4 publications

(7 citation statements)

References 69 publications

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“…It was previously proposed that this turnover could be important for error correction as it may help Aurora B reach its distant substrates and/or facilitate Aurora B's activation on the mitotic spindle (and then to shuttle back to the centromere/kinetochore) [ 86 , 87 ]. Recently the dynamic turnover of CPC was also observed in budding yeast [ 88 ]. However, using an engineered recruitment of Aurora B–INCENP, it was suggested that this turnover is not required for error correction [ 88 ].…”

Section: Tension Stabilizes the Kinetochore–microtubule Interactionmentioning

confidence: 99%

“…Recently the dynamic turnover of CPC was also observed in budding yeast [ 88 ]. However, using an engineered recruitment of Aurora B–INCENP, it was suggested that this turnover is not required for error correction [ 88 ]. Another report indicated that the level of CPC at the kinetochore/centromere is reduced a while after the establishment of the bipolar spindle [ 89 ].…”

Section: Tension Stabilizes the Kinetochore–microtubule Interactionmentioning

confidence: 99%

“…See details in the text. ( B ) The diagram shows the outcomes of the engineered recruitment of Aurora B (Ipl1), with INCENP (Sli15), to the outer or inner kinetochore, either with or without physiological Aurora B recruitment mechanisms [ 88 ]. See details in the text.…”

Section: Tension Stabilizes the Kinetochore–microtubule Interactionmentioning

confidence: 99%

Section: Tension Stabilizes the Kinetochore–microtubule Interactionmentioning

confidence: 99%

“…The evidence for the Aurora B spatial separation model was recently obtained in budding yeast, using engineered recruitment of Aurora B–INCENP (Ipl1–Sli15) to the different kinetochore sites [ 88 ]. In the absence of physiological Aurora B–INCENP recruitment mechanism to the centromere/inner kinetochore, engineered recruitment of Aurora B–INCENP to the inner kinetochore, but not the outer kinetochore, prior to biorientation supported the subsequent establishment of biorientation [ 88 ] ( Figure 3B , top). On the other hand, in the presence of physiological Aurora B–INCENP recruitment mechanism, engineered recruitment of Aurora B–INCENP to the outer kinetochore, but not the inner kinetochore, after biorientation establishment subsequently disrupted the biorientation [ 88 ] ( Figure 3B , bottom).…”

Section: Tension Stabilizes the Kinetochore–microtubule Interactionmentioning

confidence: 99%

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Kinetochore–microtubule error correction for biorientation: lessons from yeast

Li,

Kasciukovic,

Tanaka

2024

Biochemical Society Transactions

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Accurate chromosome segregation in mitosis relies on sister kinetochores forming stable attachments to microtubules (MTs) extending from opposite spindle poles and establishing biorientation. To achieve this, erroneous kinetochore–MT interactions must be resolved through a process called error correction, which dissolves improper kinetochore–MT attachment and allows new interactions until biorientation is achieved. The Aurora B kinase plays key roles in driving error correction by phosphorylating Dam1 and Ndc80 complexes, while Mps1 kinase, Stu2 MT polymerase and phosphatases also regulate this process. Once biorientation is formed, tension is applied to kinetochore–MT interaction, stabilizing it. In this review article, we discuss the mechanisms of kinetochore–MT interaction, error correction and biorientation. We focus mainly on recent insights from budding yeast, where the attachment of a single MT to a single kinetochore during biorientation simplifies the analysis of error correction mechanisms.

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Section: Tension Stabilizes the Kinetochore–microtubule Interactionmentioning

confidence: 99%

Section: Tension Stabilizes the Kinetochore–microtubule Interactionmentioning

confidence: 99%

Section: Tension Stabilizes the Kinetochore–microtubule Interactionmentioning

confidence: 99%

Section: Tension Stabilizes the Kinetochore–microtubule Interactionmentioning

confidence: 99%

Section: Tension Stabilizes the Kinetochore–microtubule Interactionmentioning

confidence: 99%

See 3 more Smart Citations

Kinetochore–microtubule error correction for biorientation: lessons from yeast

Li,

Kasciukovic,

Tanaka

2024

Biochemical Society Transactions

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Aurora B controls anaphase onset and error-free chromosome segregation in trypanosomes

Ballmer,

Lou,

Ishii

et al. 2024

Journal of Cell Biology

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Kinetochores form the interface between chromosomes and spindle microtubules and are thus under tight control by a complex regulatory circuitry. The Aurora B kinase plays a central role within this circuitry by destabilizing improper kinetochore–microtubule attachments and relaying the attachment status to the spindle assembly checkpoint. Intriguingly, Aurora B is conserved even in kinetoplastids, a group of early-branching eukaryotes which possess a unique set of kinetochore proteins. It remains unclear how their kinetochores are regulated to ensure faithful chromosome segregation. Here, we show in Trypanosoma brucei that Aurora B activity controls the metaphase-to-anaphase transition through phosphorylation of the divergent Bub1-like protein KKT14. Depletion of KKT14 overrides the metaphase arrest resulting from Aurora B inhibition, while expression of non-phosphorylatable KKT14 delays anaphase onset. Finally, we demonstrate that re-targeting Aurora B to the outer kinetochore suffices to promote mitotic exit but causes extensive chromosome missegregation in anaphase. Our results indicate that Aurora B and KKT14 are involved in an unconventional circuitry controlling cell cycle progression in trypanosomes.

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Concatemer Assisted Stoichiometry Analysis (CASA): targeted mass spectrometry for protein quantification

Cai,

Quan,

Zhang

et al. 2024

Preprint

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Large multi-protein machines are central to multiple biological processes. However, stoichiometric determination of protein complex subunits in their native states presents a significant challenge. This study addresses the limitations of current tools in accuracy and precision by introducing concatemer-assisted stoichiometry analysis (CASA). CASA leverages stable isotope-labeled concatemers and liquid chromatography parallel reaction monitoring mass spectrometry (LC-PRM-MS) to achieve robust quantification of proteins with sub-femtomole sensitivity. As a proof-of-concept, CASA was applied to study budding yeast kinetochores. Stoichiometries were determined for ex vivo reconstituted kinetochore components, including the canonical H3 nucleosomes, centromeric (Cse4CENP-A) nucleosomes, centromere proximal factors (Cbf1 and CBF3 complex), inner kinetochore proteins (Mif2CENP-C, Ctf19CCANcomplex), and outer kinetochore proteins (KMN network). Absolute quantification by CASA revealed Cse4CENP-Aas a cell-cycle controlled limiting factor for kinetochore assembly. These findings demonstrate that CASA is applicable for stoichiometry analysis of multi-protein assemblies.

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Chromosome biorientation requires Aurora B’s spatial separation from its outer kinetochore substrates, but not its turnover at kinetochores

Cited by 4 publications

References 69 publications

Kinetochore–microtubule error correction for biorientation: lessons from yeast

Kinetochore–microtubule error correction for biorientation: lessons from yeast

Aurora B controls anaphase onset and error-free chromosome segregation in trypanosomes

Concatemer Assisted Stoichiometry Analysis (CASA): targeted mass spectrometry for protein quantification

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