PLK1 regulation of PCNT cleavage ensures fidelity of centriole separation during mitotic exit.
PLK1 regulation of PCNT cleavage ensures fidelity of centriole separation during mitotic exit.
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DOI：
10.1038/ncomms10076
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发表时间：
2015-12-09
影响因子：
16.6
通讯作者：
Rhee K
中科院分区：
文献类型：
--
作者：
Kim J;Lee K;Rhee K
Centrioles are duplicated and segregated in close link to the cell cycle. During mitosis, daughter centrioles are disengaged and eventually separated from mother centrioles. New daughter centrioles may be generated only after centriole separation. Therefore, centriole separation is considered a licensing step for centriole duplication. It was previously known that separase specifically cleaves pericentrin (PCNT) during mitotic exit. Here we report that PCNT has to be phosphorylated by PLK1 to be a suitable substrate of separase. Phospho-resistant mutants of PCNT are not cleaved by separase and eventually inhibit centriole separation. Furthermore, phospho-mimetic PCNT mutants rescue centriole separation even in the presence of a PLK1 inhibitor. On the basis on these results, we propose that PLK1 phosphorylation is a priming step for separase-mediated cleavage of PCNT and eventually for centriole separation. PLK1 phosphorylation of PCNT provides an additional layer of regulatory mechanism to ensure the fidelity of centriole separation during mitotic exit. Separase-mediated cleavage of pericentrin is an essential step for centriole separation during mitotic exit. Here, Kim et al. show that pericentrin has to be phosphorylated by PLK1 in order to be cleaved by separase, which provides an additional layer of regulation for centriole separation during mitotic exit.
