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Lee M, Kim IS, Park KC, et al. Mitosis-specific phosphorylation of Mis18α by Aurora B kinase enhances kinetochore recruitment of polo-like kinase 1. Oncotarget. 2017;9(2):1563-1576doi: 10.18632/oncotarget.22707.
Lee, M., Kim, I. S., Park, K. C., Kim, J. S., Baek, S. H., & Kim, K. I. (2018). Mitosis-specific phosphorylation of Mis18α by Aurora B kinase enhances kinetochore recruitment of polo-like kinase 1. Oncotarget, 9(2), 1563-1576. https://doi.org/10.18632/oncotarget.22707
Lee, Minkyoung, et al. "Mitosis-specific phosphorylation of Mis18α by Aurora B kinase enhances kinetochore recruitment of polo-like kinase 1." Oncotarget vol. 9,2 (2018): 1563-1576. doi: https://doi.org/10.18632/oncotarget.22707
Lee M, Kim IS, Park KC, Kim JS, Baek SH, Kim KI. Mitosis-specific phosphorylation of Mis18α by Aurora B kinase enhances kinetochore recruitment of polo-like kinase 1. Oncotarget. 2017 Nov 27;9(2):1563-1576. doi: 10.18632/oncotarget.22707. eCollection 2018 Jan 05. PMID: 29416714; PMCID: PMC5788582.
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Oncotarget. 2017 Nov 27;9(2):1563-1576. doi: 10.18632/oncotarget.22707. eCollection 2018 Jan 05.

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

Oncotarget

Minkyoung Lee, Ik Soo Kim, Koog Chan Park, Jong-Seo Kim, Sung Hee Baek, Keun Il Kim

Affiliations

  1. Creative Research Initiatives Center for Chromatin Dynamics, Department of Biological Sciences, Seoul National University, Seoul 08826, South Korea.
  2. Department of Biological Sciences, Cellular Heterogeneity Research Center, Sookmyung Women's University, Seoul 04310, South Korea.
  3. Center for RNA Research, Institute for Basic Science, Department of Biological Sciences, Seoul National University, Seoul 08826, South Korea.

PMID: 29416714 PMCID: PMC5788582 DOI: 10.18632/oncotarget.22707

Abstract

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 Mis18α during mitosis not affecting neither centromere localization of Mis18 complex nor centromere loading of CENP-A. However, the replacement of endogenous Mis18α 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 Mis18α is a crucial event for faithful cell cycle progression through the enhanced recruitment of polo-like kinase 1 to the kinetochore.

Keywords: Aurora B kinase; Mis18α; PLK1; mitosis-specific phosphorylation; polo box domain

Conflict of interest statement

CONFLICTS OF INTEREST None.

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