Eukaryotic chromosomes segregate by attaching to microtubules of the mitotic 
spindle through a chromosomal microtubule binding site called the kinetochore. 
Kinetochores assemble on a specialized chromosomal locus termed the centromere, 
which is characterized by the replacement of histone H3 in centromeric 
nucleosomes with the essential histone H3 variant CENP-A (centromere protein A). 
Understanding how CENP-A chromatin is assembled and maintained is central to 
understanding chromosome segregation mechanisms. CENP-A nucleosome assembly 
requires the Mis18 complex and the CENP-A chaperone HJURP. These factors 
localize to centromeres in telophase/G1, when new CENP-A chromatin is assembled. 
The mechanisms that control their targeting are unknown. In this paper, we 
identify a mechanism for recruiting the Mis18 complex protein M18BP1 to 
centromeres. We show that depletion of CENP-C prevents M18BP1 targeting to 
metaphase centromeres and inhibits CENP-A chromatin assembly. We find that 
M18BP1 directly binds CENP-C through conserved domains in the CENP-C protein. 
Thus, CENP-C provides a link between existing CENP-A chromatin and the proteins 
required for new CENP-A nucleosome assembly.