To ensure accurate chromosome segregation, interactions between kinetochores and microtubules are regulated by a combination of mechanics and biochemistry. Tension provides a signal to discriminate attachment errors from bi-oriented kinetochores with sisters correctly attached to opposite spindle poles. Biochemically, Aurora B kinase phosphorylates kinetochores to destabilize interactions with microtubules. To link mechanics and biochemistry, current models regard tension as an input signal to locally regulate Aurora B activity. Here, we show that the outcome of kinetochore phosphorylation depends on tension. Using optogenetics to manipulate Aurora B at individual kinetochores, we find that kinase activity promotes microtubule release when tension is high. Conversely, when tension is low, Aurora B activity promotes depolymerization of kinetochore–microtubules while maintaining attachment. Thus, phosphorylation converts a catch-bond, in which tension stabilizes attachments, to a slip-bond, which releases microtubules under tension. We propose that tension is a signal inducing distinct error-correction pathways, with release or depolymerization being advantageous for typical errors characterized by high or low tension, respectively.
Tension promotes kinetochore–microtubule release by Aurora B kinase
H. Zhang’s present address is Department of Biological Sciences, Mellon College of Science, Carnegie Mellon University, Pittsburgh, PA.
A preprint of this paper was posted in bioRxiv on June 2, 2020.
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Geng-Yuan Chen, Fioranna Renda, Huaiying Zhang, Alper Gokden, Daniel Z. Wu, David M. Chenoweth, Alexey Khodjakov, Michael A. Lampson; Tension promotes kinetochore–microtubule release by Aurora B kinase. J Cell Biol 7 June 2021; 220 (6): e202007030. doi: https://doi.org/10.1083/jcb.202007030
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