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. Author manuscript; available in PMC: 2019 Oct 27.
Published in final edited form as: Science. 2018 May 4;360(6388):552–558. doi: 10.1126/science.aar6436

Fig. 4. Model of the yeast kinetochore-MT interface.

Fig. 4.

(A) Overview from the side (left) and top (right). (B) Close-up view and interactions of DASH/Dam1c with the MT and Ndc80c. Approximate distances between the attachments of the flexible extensions on the DASH/Dam1c ring and their target sites, defined by crosslinking, are shown. Interactions A, B and C are between Ndc80c and DASH/Dam1 subunits Dam1, Ask1 and Spc34:Spc19, respectively. S. cerevisiae residues known to be phosphorylated by Ipl1/Aurora B are shown in the insets, and arrows indicate release of Ndc80c binding upon phosphorylation.