2. Academic Validation
  3. Phosphorylation of the centrosomal protein, Cep169, by Cdk1 promotes its dissociation from centrosomes in mitosis

Phosphorylation of the centrosomal protein, Cep169, by Cdk1 promotes its dissociation from centrosomes in mitosis

  • Biochem Biophys Res Commun. 2015 Dec 25;468(4):642-6. doi: 10.1016/j.bbrc.2015.11.004.
Yusuke Mori 1,  Yoko Inoue 1,  Yuki Taniyama 1,  Sayori Tanaka 1,  Yasuhiko Terada 2
Affiliations

Affiliations

  • 1 Department of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, 3-4-1 Ohkubo, Tokyo 169-8555, Japan.
  • 2 Department of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, 3-4-1 Ohkubo, Tokyo 169-8555, Japan. Electronic address: yterada@waseda.jp.
PMID: 26549230 DOI: 10.1016/j.bbrc.2015.11.004
Abstract

Cep169 is a centrosomal protein conserved among vertebrates. In our previous reports, we showed that mammalian Cep169 interacts and collaborates with CDK5RAP2 to regulate microtubule (MT) dynamics and stabilization. Although Cep169 is required for MT regulation, its precise cellular function remains largely elusive. Here we show that Cep169 associates with centrosomes during interphase, but dissociates from these structures from the onset of mitosis, although CDK5RAP2 (Cep215) is continuously located at the centrosomes throughout cell cycle. Interestingly, treatment with purvalanol A, a CDK1 Inhibitor, nearly completely blocked the dissociation of Cep169 from centrosomes during mitosis. In addition, mass spectrometry analyses identified 7 phosphorylated residues of Cep169 corresponding to consensus phosphorylation sequence for CDK1. These data suggest that the dissociation of Cep169 from centrosomes is controlled by CDK1/Cyclin B during mitosis, and that Cep169 might regulate MT dynamics of mitotic spindle.

Keywords

Cdk1; Centrosome; Cep169; Mitosis; Phosphorylation.

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