西亞試劑：Type Iγ phosphatidylinositol phosphate kinase targets to th

Type Iγ phosphatidylinositol phosphate kinase targets to the centrosome and restrains centriole duplication

Qingwen Xu, Yuxia Zhang, Xunhao Xiong, Yan Huang, Jeffery L. Salisbury, Jinghua Hu and Kun Ling

Centriole biogenesis depends on the Polo-like kinase PLK4 and a small group of structural proteins. The spatiotemporal regulation of these proteins at pre-existing centrioles is critical to ensure that centriole duplication occurs once per cell cycle. Here we report that type Iγ phosphatidylinositol-4-phosphate 5-kinase (PIPKIγ) plays an important role in centriole fidelity. Depending upon an association with CEP152, PIPKIγ localized in a ring-like pattern in the intermediate pericentriolar materials around the proximal end of the centriole in G1, S, and G2 phases, but not in M phase. Without detaining cells in S or M phase, depletion of PIPKIγ led to centriole amplification in a PLK4/SAS-6 dependent manner. Expression of exogenous PIPKIγ reduced centriole amplification resulted from endogenous PIPKIγ depletion, hydroxyurea treatment, or PLK4 overexpression, suggesting that PIPKIγ likely functions at the PLK4 level to restrain centriole duplication. Importantly, we found that PIPKIγ bound to the cryptic Polo-Box domain of PLK4 and this binding reduced PLK4 kinase activity. Together, our findings suggest that PIPKIγ is a novel negative regulator of centriole duplication by modulating the homeostasis of PLK4 activity.

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