Aurora B Is Enriched at Merotelic Attachment Sites, Where It Regulates MCAK

183Citations
Citations of this article
98Readers
Mendeley users who have this article in their library.

Abstract

Kinetochores often form merotelic attachments, in which a single kinetochore is attached to microtubules from both spindle poles. These attachments can result in improper chromosome segregation and are a significant source of aneuploidy [1, 2], a hallmark of cancer [3-5]. Aurora B kinase and the kinesin-13 microtubule depolymerase mitotic-centromere-associated kinesin (MCAK) are required to release improper microtubule attachments [6-9]. Aurora B regulates MCAK's activity and localization [10-12]. We set out to understand why MCAK and Aurora B are more abundant at some metaphase-aligned centromeres but are present at low amounts on most others. We found that members of the Aurora B complex are specifically enriched at merotelic attachment sites. We also found that Aurora B does not require its activity to become enriched at these sites; however, inhibition of Aurora B activity causes a significant increase in the number of merotelic attachments per cell. Aurora B activity enriches MCAK at merotelic attachments and phosphorylates MCAK on residues that regulate its microtubule depolymerase activity. These data demonstrate that proteins that resolve the defect are specifically localized to merotelic attachments, where their enzymatic activities are regulated. © 2006 Elsevier Ltd. All rights reserved.

Author supplied keywords

Cite

CITATION STYLE

APA

Knowlton, A. L., Lan, W., & Stukenberg, P. T. (2006). Aurora B Is Enriched at Merotelic Attachment Sites, Where It Regulates MCAK. Current Biology, 16(17), 1705–1710. https://doi.org/10.1016/j.cub.2006.07.057

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free