TY - JOUR
T1 - Phosphorylation of the centrosomal protein, Cep169, by Cdk1 promotes its dissociation from centrosomes in mitosis
AU - Mori, Yusuke
AU - Inoue, Yoko
AU - Taniyama, Yuki
AU - Tanaka, Sayori
AU - Terada, Yasuhiko
N1 - Funding Information:
We are grateful to S. Nakaya (Shimadzu, Kyoto, Japan) for the proteomic analyses. We thank members of the Terada laboratory for discussions and critical reading of the manuscript. This work was supported by JSPS (20058039) .
Publisher Copyright:
© 2015 Elsevier Inc. All rights reserved.
PY - 2015/12/25
Y1 - 2015/12/25
N2 - 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.
AB - 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.
KW - Cdk1
KW - Centrosome
KW - Cep169
KW - Mitosis
KW - Phosphorylation
UR - http://www.scopus.com/inward/record.url?scp=84949624415&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84949624415&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2015.11.004
DO - 10.1016/j.bbrc.2015.11.004
M3 - Article
C2 - 26549230
AN - SCOPUS:84949624415
SN - 0006-291X
VL - 468
SP - 642
EP - 646
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -