Contacts between inner and outer kinetochore protein complexes. The architecture of the outer kinetochore KMN complex (green box) is broadly conserved, with Knl1 and the Ndc80 complex binding at one end of the rod-like Mis12 complex. Within the constitutive centromere-associated network (CCAN; pink box), there are now two Mis12 complex binding activities: one in the N terminus of the dimeric CENP-C/Mif2 (magenta; for simplicity only one monomer is drawn), and the second in Ame1/CENP-U (yellow; for simplicity other CCAN subunits known to associate with Ame1 and Okp1 are not depicted). The Ame1/CENP-U–Mis12 complex interaction, mediated by an N-terminal motif in Ame1, is described in this issue by Hornung et al. (2014) as being essential for outer kinetochore assembly in budding yeast. They also demonstrate DNA binding activity and direct Mif2/CENP-C–binding activity for the Ame1–Okp1 complex (yellow arrows). In addition to CENP-C and Ame1/CENP-U, the CENP-T subunit of a different CCAN complex (T/W/S/X) binds directly to the Ndc80 complex.