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

Author:

Wei Zhuang1,Kim Tae-Sung1,Ahn Jong Il1,Meng Lingjun1,Chen Yaozong1,Ryu Eun Kyoung2,Ku Bonsu3ORCID,Zhou Ming4,Kim Seung Jun3,Bang Jeong Kyu2,van Deursen Jan M.56,Park Jung-Eun1,Lee Kyung S.1ORCID

Affiliation:

1. Laboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, USA

2. Division of Magnetic Resonance, Korea Basic Science Institute, Ochang, Republic of Korea

3. Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea

4. Laboratory of Proteomics and Analytical Technologies, Frederick National Laboratory for Cancer Research, Frederick, Maryland, USA

5. Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota, USA

6. Department of Pediatric and Adolescent Medicine, Mayo Clinic, Rochester, Minnesota, USA

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.

Funder

Korean Biomedical Scientist Fellowship

HHS | National Institutes of Health

National Research Foundation of Korea

Korea Research Institute of Bioscience and Biotechnology

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

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