Cep57 and Cep57L1 maintain centriole engagement in interphase to ensure centriole duplication cycle

J Cell Biol. 2021 Mar 1;220(3):e202005153. doi: 10.1083/jcb.202005153.

Abstract

Centrioles duplicate in interphase only once per cell cycle. Newly formed centrioles remain associated with their mother centrioles. The two centrioles disengage at the end of mitosis, which licenses centriole duplication in the next cell cycle. Therefore, timely centriole disengagement is critical for the proper centriole duplication cycle. However, the mechanisms underlying centriole engagement during interphase are poorly understood. Here, we show that Cep57 and Cep57L1 cooperatively maintain centriole engagement during interphase. Codepletion of Cep57 and Cep57L1 induces precocious centriole disengagement in interphase without compromising cell cycle progression. The disengaged daughter centrioles convert into centrosomes during interphase in a Plk1-dependent manner. Furthermore, the centrioles reduplicate and the centriole number increases, which results in chromosome segregation errors. Overall, these findings demonstrate that the maintenance of centriole engagement by Cep57 and Cep57L1 during interphase is crucial for the tight control of centriole copy number and thus for proper chromosome segregation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Cycle Proteins / metabolism
  • Centrioles / metabolism*
  • Centrosome / metabolism
  • Chromosome Segregation
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Interphase*
  • Microtubule-Associated Proteins / chemistry
  • Microtubule-Associated Proteins / metabolism*
  • Models, Biological
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / metabolism*
  • Phenotype
  • Polo-Like Kinase 1
  • Protein Serine-Threonine Kinases / metabolism
  • Protein Transport
  • Proto-Oncogene Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Spindle Apparatus / metabolism

Substances

  • CEP57 protein, human
  • Cell Cycle Proteins
  • Microtubule-Associated Proteins
  • Nuclear Proteins
  • Proto-Oncogene Proteins
  • Protein Serine-Threonine Kinases