Cep152 acts as a scaffold for recruitment of Plk4 and CPAP to the centrosome

被引：213

作者：

Cizmecioglu, Onur ^{[1
]}

Arnold, Marc ^{[1
]}

Bahtz, Ramona ^{[1
]}

Settele, Florian ^{[1
]}

Ehret, Lena ^{[1
]}

Haselmann-Weiss, Uta ^{[2
]}

Antony, Claude ^{[2
]}

Hoffmann, Ingrid ^{[1
]}

机构：

[1] German Canc Res Ctr, D-69120 Heidelberg, Germany

[2] European Mol Biol Lab, Cell Biol & Biophys Program, D-69117 Heidelberg, Germany

来源：

JOURNAL OF CELL BIOLOGY | 2010年 / 191卷 / 04期

关键词：

CELL-CYCLE; CENTRIOLE; DUPLICATION; PROTEIN; OVERDUPLICATION; ASTERLESS; TUBULIN;

D O I：

10.1083/jcb.201007107

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Both gain and loss of function studies have identified the Polo like kinase Plk4/Sak as a crucial regulator of centriole biogenesis, but the mechanisms governing centrosome duplication are incompletely under stood In this study, we show that the pericentriolar material protein, Cep152, interacts with the distinctive cryptic Polo box of Plk4 via its N terminal domain and is required for Plk4 induced centriole overduplication Reduction of endogenous Cep152 levels results in a failure in centriole duplication, loss of centrioles, and formation of mono polar mitotic spindles Interfering with Cep152 function prevents recruitment of Plk4 to the centrosome and promotes loss of CPAP, a protein required for the control of centriole length in Plk4 regulated centriole biogenesis Our results suggest that Cep152 recruits Plk4 and CPAP to the centrosome to ensure a faithful centrosome duplication process

引用

页码：731 / 739

页数：9

共 36 条

[1] Proteomic characterization of the human centrosome by protein correlation profiling [J].