@article {5153,
	title = {The Ndc80 kinetochore complex directly modulates microtubule dynamics.},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {109},
	year = {2012},
	month = {2012 Aug 20},
	pages = {16113-8},
	abstract = {<p>The conserved Ndc80 complex is an essential microtubule-binding component of the kinetochore. Recent findings suggest that the Ndc80 complex influences microtubule dynamics at kinetochores in vivo. However, it was unclear if the Ndc80 complex mediates these effects directly, or by affecting other factors localized at the kinetochore. Using a reconstituted system in vitro, we show that the human Ndc80 complex directly stabilizes the tips of disassembling microtubules and promotes rescue (the transition from microtubule shortening to growth). In vivo, an N-terminal domain in the Ndc80 complex is phosphorylated by the Aurora B kinase. Mutations that mimic phosphorylation of the Ndc80 complex prevent stable kinetochore-microtubule attachment, and mutations that block phosphorylation damp kinetochore oscillations. We find that the Ndc80 complex with Aurora B phosphomimetic mutations is defective at promoting microtubule rescue, even when robustly coupled to disassembling microtubule tips. This impaired ability to affect dynamics is not simply because of weakened microtubule binding, as an N-terminally truncated complex with similar binding affinity is able to promote rescue. Taken together, these results suggest that in addition to regulating attachment stability, Aurora B controls microtubule dynamics through phosphorylation of the Ndc80 complex.</p>
},
	issn = {1091-6490},
	doi = {10.1073/pnas.1209615109},
	author = {Umbreit, Neil T and Gestaut, Daniel R and Tien, Jerry F and Vollmar, Breanna S and Gonen, Tamir and Asbury, Charles L and Davis, Trisha N}
}
@article {3636,
	title = {Cooperation of the Dam1 and Ndc80 kinetochore complexes enhances microtubule coupling and is regulated by aurora B.},
	journal = {The Journal of Cell Biology},
	volume = {189},
	year = {2010},
	month = {2010 May 17},
	pages = {713-23},
	abstract = {<p>The coupling of kinetochores to dynamic spindle microtubules is crucial for chromosome positioning and segregation, error correction, and cell cycle progression. How these fundamental attachments are made and persist under tensile forces from the spindle remain important questions. As microtubule-binding elements, the budding yeast Ndc80 and Dam1 kinetochore complexes are essential and not redundant, but their distinct contributions are unknown. In this study, we show that the Dam1 complex is a processivity factor for the Ndc80 complex, enhancing the ability of the Ndc80 complex to form load-bearing attachments to and track with dynamic microtubule tips in vitro. Moreover, the interaction between the Ndc80 and Dam1 complexes is abolished when the Dam1 complex is phosphorylated by the yeast aurora B kinase Ipl1. This provides evidence for a mechanism by which aurora B resets aberrant kinetochore-microtubule attachments. We propose that the action of the Dam1 complex as a processivity factor in kinetochore-microtubule attachment is regulated by conserved signals for error correction.</p>
},
	keywords = {Cell Cycle Proteins, Green Fluorescent Proteins, Kinetochores, Microtubule-Associated Proteins, Microtubules, Mitotic Spindle Apparatus, Nuclear Proteins, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins},
	issn = {1540-8140},
	doi = {10.1083/jcb.200910142},
	author = {Tien, Jerry F and Umbreit, Neil T and Gestaut, Daniel R and Franck, Andrew D and Cooper, Jeremy and Wordeman, Linda and Gonen, Tamir and Asbury, Charles L and Davis, Trisha N}
}
