Open AccessCep57 and Cep57l1 function redundantly to recruit the Cep63-Cep152 complex for centriole biogenesis
Author(s) -
Huijie Zhao,
Sen Yang,
Qingxia Chen,
Xiaomeng Duan,
Guoqing Li,
Qiongping Huang,
Xueliang Zhu,
Xiumin Yan
Publication year - 2020
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.241836
Subject(s) - centriole , biology , biogenesis , microbiology and biotechnology , centrosome , basal body , cilium , genetics , flagellum , mitosis , cell cycle , cell , gene
The Cep63-Cep152 complex located at the mother centriole recruits Plk4 to initiate the centriole biogenesis. How the complex is targeted to mother centrioles, however, is unclear. In this study, we show that Cep57 and its paralog, Cep57l1, colocalize with Cep63 and Cep152 at the proximal end of mother centrioles in both cycling cells and multiciliated cells undergoing centriole amplification. Both Cep57 and Cep57l1 bind to the centrosomal targeting region of Cep63. The depletion of both proteins, but not either one, blocks the loading of Cep63-Cep152 complex to mother centrioles and consequently prevents centriole duplication. We propose that Cep57 and Cep57l1 function redundantly to ensure the recruitment of the Cep63-Cep152 complex to the mother centrioles for procentriole formation.