HIGHLIGHTS
SUMMARY
The C-terminal region of CenpC dimerizes through its structured cupin domain, which at least in_vitro, allows it to bind two nucleosomes, though the significance of this for kinetochore function in_vivo is unclear. In budding yeast, a four-subunit complex called monopolin is required for monoorientation in_vivo and is sufficient to alter the biophysical properties of kinetochores in_vitro. Indeed, two residues (S109 and S110) within the monopolin binding_site on Dsn1 are phosphorylated in_vivo and phospho-mimetic mutations increased Csm1-Dsn1 binding in_vitro, though whether CK1d or some other kinase is responsible remains unknown. Such . . .
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