The dynamics of centromere assembly and disassembly during quiescence.

Quiescence is a state in which cells undergo a proliferative arrest while maintaining their capacity to divide again. Here, we analyze how cells regulate their centromeres during quiescence entry and exit. Despite the constitutive localization of centromere proteins in proliferating cells, cells rapidly disassemble most centromere proteins during quiescence entry while preserving those required to maintain centromere identity. We show that this disassembly occurs primarily through the transcriptional downregulation of centromere proteins. During quiescence exit, the centromere is reassembled during the first S phase to regain normal homeostatic centromere protein levels. CENP-A is typically deposited during G1. However, we find that CENP-A deposition does not occur during the G1 immediately following quiescence exit and instead occurs in the G1 after cells complete their first mitosis. We find that the presence of PLK1 distinguishes these distinct G1 states. These findings reveal centromere dynamics during quiescence entry and exit and highlight paradigms for controlling centromere assembly and disassembly.