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bioRxiv · 10.1101/2023.05.10.540161

A BubR1-independent pathway for CENP-E targeting to the outer corona of kinetochores

Legal, T.·Paterson, C.·Gluszek, A.·Davies, O.·Welburn, J.
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Abstract

For chromosome segregation to take place, unattached kinetochores expand in early mitosis, forming a fibrous structure called the fibrous corona that is captured by microtubules. The corona is assembled from the RZZ complex, Spindly, CENP-E and the Mad1/Mad2 spindle assembly checkpoint proteins. CENP-E aligns chromosomes along the mitotic spindle by moving them to the plus ends of microtubules. Here, we show that CENP-E is recruited to the outer corona independently of BubR1 in a dynein-dependent fashion. We determine the structure of this domain and show that a conserved loop is essential for CENP-E targeting to the outer corona. We show that both domains are essential for CENP-E recruitment to unattached kinetochores. We also report that the kinetochore-targeting domain of CENP-E contributes to the recruitment of the RZZ complex, Mad1 and Spindly, providing a feedback loop to assemble the outer corona. In this study, we propose that CENP-E uses 2 pathways to target to the kinetochore, which allows it to optimize kinetochore capture by microtubules for chromosome alignment and mitotic progression.

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Legal, T., Paterson, C., Gluszek, A., Davies, O., Welburn, J.. 2023-05-10. A BubR1-independent pathway for CENP-E targeting to the outer corona of kinetochores. https://doi.org/10.1101/2023.05.10.540161

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