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Requirement of the Cep57-Cep63 Interaction for Proper Cep152 Recruitment and Centriole Duplication.


ABSTRACT: Cep57 has been characterized as a component of a pericentriolar complex containing Cep63 and Cep152. Interestingly, Cep63 and Cep152 self-assemble into a pericentriolar cylindrical architecture, and this event is critical for the orderly recruitment of Plk4, a key regulator of centriole duplication. However, the way in which Cep57 interacts with the Cep63-Cep152 complex and contributes to the structure and function of Cep63-Cep152 self-assembly remains unknown. We demonstrate that Cep57 interacts with Cep63 through N-terminal motifs and associates with Cep152 via Cep63. Three-dimensional structured illumination microscopy (3D-SIM) analyses suggested that the Cep57-Cep63-Cep152 complex is concentrically arranged around a centriole in a Cep57-in and Cep152-out manner. Cep57 mutant cells defective in Cep63 binding exhibited improper Cep63 and Cep152 localization and impaired Sas6 recruitment for procentriole assembly, proving the significance of the Cep57-Cep63 interaction. Intriguingly, Cep63 fused to a microtubule (MT)-binding domain of Cep57 functioned in concert with Cep152 to assemble around stabilized MTs in vitro Thus, Cep57 plays a key role in architecting the Cep63-Cep152 assembly around centriolar MTs and promoting centriole biogenesis. This study may offer a platform to investigate how the organization and function of the pericentriolar architecture are altered by disease-associated mutations found in the Cep57-Cep63-Cep152 complex.

SUBMITTER: Wei Z 

PROVIDER: S-EPMC7189096 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature

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Requirement of the Cep57-Cep63 Interaction for Proper Cep152 Recruitment and Centriole Duplication.

Wei Zhuang Z   Kim Tae-Sung TS   Ahn Jong Il JI   Meng Lingjun L   Chen Yaozong Y   Ryu Eun Kyoung EK   Ku Bonsu B   Zhou Ming M   Kim Seung Jun SJ   Bang Jeong Kyu JK   van Deursen Jan M JM   Park Jung-Eun JE   Lee Kyung S KS  

Molecular and cellular biology 20200428 10


Cep57 has been characterized as a component of a pericentriolar complex containing Cep63 and Cep152. Interestingly, Cep63 and Cep152 self-assemble into a pericentriolar cylindrical architecture, and this event is critical for the orderly recruitment of Plk4, a key regulator of centriole duplication. However, the way in which Cep57 interacts with the Cep63-Cep152 complex and contributes to the structure and function of Cep63-Cep152 self-assembly remains unknown. We demonstrate that Cep57 interact  ...[more]

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