Centriole and PCM cooperatively recruit CEP192 to spindle poles to promote bipolar spindle assembly

被引:31
|
作者
Chinen, Takumi [1 ]
Yamazaki, Kaho [1 ]
Hashimoto, Kaho [1 ]
Fujii, Ken [2 ,3 ]
Watanabe, Koki [1 ]
Takeda, Yutaka [1 ]
Yamamoto, Shohei [1 ,4 ]
Nozaki, Yuka [2 ]
Tsuchiya, Yuki [2 ,3 ]
Takao, Daisuke [1 ]
Kitagawa, Daiju [1 ,2 ,3 ]
机构
[1] Univ Tokyo, Grad Sch Pharmaceut Sci, Dept Physiol Chem, Bunkyo Ku, Tokyo, Japan
[2] Natl Inst Genet, Div Centrosome Biol, Dept Mol Genet, Mishima, Shizuoka, Japan
[3] Grad Univ Adv Studies SOKENDAI, Sch Life Sci, Dept Genet, Mishima, Shizuoka, Japan
[4] Univ Tokyo, Grad Sch Sci, Grad Program Biosci, Tokyo, Japan
来源
JOURNAL OF CELL BIOLOGY | 2021年 / 220卷 / 02期
基金
日本学术振兴会;
关键词
MICROTUBULE NUCLEATION; CENTROSOME; PROTEIN; RING; PERICENTRIN; ACTIVATION; INHIBITOR; APOPTOSIS; DEPLETION;
D O I
10.1083/jcb.202006085
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The pericentriolar material (PCM) that accumulates around the centriole expands during mitosis and nucleates microtubules. Here, we show the cooperative roles of the centriole and PCM scaffold proteins, pericentrin and CDK5RAP2, in the recruitment of CEP192 to spindle poles during mitosis. Systematic depletion of PCM proteins revealed that CEP192, but not pericentrin and/or CDK5RAP2, was crucial for bipolar spindle assembly in HeLa, RPE1, and A549 cells with centrioles. Upon double depletion of pericentrin and CDK5RAP2, CEP192 that remained at centriole walls was sufficient for bipolar spindle formation. In contrast, through centriole removal, we found that pericentrin and CDK5RAP2 recruited CEP192 at the acentriolar spindle pole and facilitated bipolar spindle formation in mitotic cells with one centrosome. Furthermore, the perturbation of PLK1, a critical kinase for PCM assembly, efficiently suppressed bipolar spindle formation in mitotic cells with one centrosome. Overall, these data suggest that the centriole and PCM scaffold proteins cooperatively recruit CEP192 to spindle poles and facilitate bipolar spindle formation.
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页数:24
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