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Mitosis-specific phosphorylation of Mis18? by Aurora B kinase enhances kinetochore recruitment of polo-like kinase 1.


ABSTRACT: Mis18?, a component of Mis18 complex comprising of Mis18?, Mis18?, and M18BP1, is known to localize at the centromere from late telophase to early G1 phase and plays a priming role in CENP-A deposition. Although its role in CENP-A deposition is well established, the other function of Mis18? remains unknown. Here, we elucidate a new function of Mis18? that is critical for the proper progression of cell cycle independent of its role in CENP-A deposition. We find that Aurora B kinase phosphorylates Mis18? during mitosis not affecting neither centromere localization of Mis18 complex nor centromere loading of CENP-A. However, the replacement of endogenous Mis18? by phosphorylation-defective mutant causes mitotic defects including micronuclei formation, chromosome misalignment, and chromosomal bridges. Together, our data demonstrate that Aurora B kinase-mediated mitotic phosphorylation of Mis18? is a crucial event for faithful cell cycle progression through the enhanced recruitment of polo-like kinase 1 to the kinetochore.

SUBMITTER: Lee M 

PROVIDER: S-EPMC5788582 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

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Mitosis-specific phosphorylation of Mis18α by Aurora B kinase enhances kinetochore recruitment of polo-like kinase 1.

Lee Minkyoung M   Kim Ik Soo IS   Park Koog Chan KC   Kim Jong-Seo JS   Baek Sung Hee SH   Kim Keun Il KI  

Oncotarget 20171127 2


Mis18α, a component of Mis18 complex comprising of Mis18α, Mis18β, and M18BP1, is known to localize at the centromere from late telophase to early G1 phase and plays a priming role in CENP-A deposition. Although its role in CENP-A deposition is well established, the other function of Mis18α remains unknown. Here, we elucidate a new function of Mis18α that is critical for the proper progression of cell cycle independent of its role in CENP-A deposition. We find that Aurora B kinase phosphorylates  ...[more]

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