Journal
CELL CYCLE
Volume 18, Issue 20, Pages 2651-2659Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15384101.2019.1654795
Keywords
Chk2; Plk1; MYPT1; Phosphoprotein phosphatase 1 beta (PP1 beta); centrosome
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Funding
- National Natural Science Foundation of China (NSFC) [31872720]
- Capacity Building for Sci-Tech Innovation - Fundamental Scientific Research Funds [19530050137]
- NSFC [31461143012, 31130017]
- 973 projects [2013CB911002, 2015CB910601]
- Shenzhen Science and Technology Innovation Commission [JCYJ20170412112009742]
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Checkpoint kinase 2 (Chk2) is a pivotal effector kinase in the DNA damage response, with an emerging role in mitotic chromosome segregation. In this study, we show that Chk2 interacts with myosin phosphatase targeting subunit 1 (MYPT1), the targeting subunit of protein phosphatase 1c beta (PP1c beta). Previous studies have shown that MYPT1 is phosphorylated by CDK1 at S473 during mitosis, and subsequently docks to the polo-binding domain of PLK1 and dephosphorylates PLK1. Herein we present data that Chk2 phosphorylates MYPT1 at S507 in vitro and in vivo, which antagonizes pS473. Chk2 inhibition results in failure of gamma-tubulin recruitment to the centrosomes, phenocopying Plk1 inhibition defects. These aberrancies were also observed in the MYPT1-S507A stable transfectants, suggesting that Chk2 exerts its effect on centrosomes via MYPT1. Collectively, we have identified a Chk2-MYPT1-PLK1 axis in regulating centrosome maturation.
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