Ubiquitin E3 ligases including SCF complex are key regulators of cell cycle. 
Here, we show that Mis18β, a component of Mis18 complex governing CENP-A 
localization, is a new substrate of βTrCP-containing SCF complex. βTrCP 
interacted with Mis18β exclusively during interphase but not during mitosis and 
mediated proteasomal degradation of Mis18β leading to the inactivation of Mis18 
complex during interphase. In addition, uncontrolled stabilization of Mis18β 
caused cell death. Together, we propose that βTrCP-mediated regulation of Mis18β 
stability is a mechanism to restrict centromere function of Mis18 complex from 
late mitosis to early G1 phase.