A comprehensive structural, biochemical, and cell biological analysis reveals the molecular mechanism and significance of the conserved interaction of centromeric protein N (CENP-N) with the centromeric nucleosome.

The number of CENP-A molecules at human centromeres helps to explain how this structure is built and epigenetically inherited.

The stoichiometry and mechanism of interactions of the Mis18 complex with M18BP1 was analysed to unveil the molecular basis of new CENP-A deposition during the G1 phase of the cell cycle.

Two components of the inner kinetochore (OA and Mif2) are independently capable of transmitting physiologically relevant forces to a centromeric nucleosome.

The chromosomal passenger complex interacts with the inner kinetochore COMA complex through the Ctf19 C-terminus in vitro which is shown to be important for mediating accurate chromosome segregation.

Centromeric protein M (CENP-M) is required for the stabilization of a quaternary complex that plays a crucial role in kinetochore organization and function.

The outer domain of the kinetochore can rotate (swivel) around the centromere, and this rather than intra-kinetochore stretching is coupled to anaphase onset.

The centromeric protein CENP-T assembles the microtubule-binding interface of kinetochores through direct recruitment of two Ndc80 complexes and indirect recruitment of a third one through the Mis12 complex.

Centromeric histones, the foundation for accurate chromosome segregation, have now been re-engineered to allow for analysis of the stoichiometry of required domains.

Optogenetic experiments show that bridging microtubules buffer chromosome movements and promote their alignment through forces transferred to the associated kinetochore fibers, which rely on precise regulation of the overlap region.