Kinetochores require oligomerization of Dam1 complex to maintain microtubule attachments against tension and promote biorientation

Neil T. Umbreit, Matthew P. Miller, Jerry F. Tien, Jérôme Cattin Ortolá, Long Gui, Kelly K. Lee, Sue Biggins, Charles L. Asbury and Trisha N. Davis ()
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Neil T. Umbreit: University of Washington
Matthew P. Miller: Fred Hutchinson Cancer Research Center
Jerry F. Tien: University of Washington
Jérôme Cattin Ortolá: University of Washington
Long Gui: University of Washington
Kelly K. Lee: University of Washington
Sue Biggins: Fred Hutchinson Cancer Research Center
Charles L. Asbury: University of Washington
Trisha N. Davis: University of Washington

Nature Communications, 2014, vol. 5, issue 1, 1-11

Abstract: Abstract Kinetochores assemble on centromeric DNA and present arrays of proteins that attach directly to the dynamic ends of microtubules. Kinetochore proteins coordinate at the microtubule interface through oligomerization, but how oligomerization contributes to kinetochore function has remained unclear. Here, using a combination of biophysical assays and live-cell imaging, we find that oligomerization of the Dam1 complex is required for its ability to form microtubule attachments that are robust against tension in vitro and in vivo. An oligomerization-deficient Dam1 complex that retains wild-type microtubule binding activity is primarily defective in coupling to disassembling microtubule ends under mechanical loads applied by a laser trap in vitro. In cells, the oligomerization-deficient Dam1 complex is unable to support stable bipolar alignment of sister chromatids, indicating failure of kinetochore–microtubule attachments under tension. We propose that oligomerization is an essential and conserved feature of kinetochore components that is required for accurate chromosome segregation during mitosis.

Date: 2014
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DOI: 10.1038/ncomms5951

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