Polo‐like kinase‐1 triggers histone phosphorylation by Haspin in mitosis |
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| Authors: | Linli Zhou Xiaoying Tian Cailei Zhu Fangwei Wang Jonathan MG Higgins |
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| Institution: | 1. Life Sciences Institute and Innovation Center for Cell Biology, Zhejiang University, Hangzhou, Zhejiang Province, China;2. Division of Rheumatology, Immunology and Allergy, Brigham & Women's Hospital, Harvard Medical School, Boston, MA, USA;3. Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Newcastle‐upon‐Tyne, UK |
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| Abstract: | Histone modifications coordinate the chromatin localization of key regulatory factors in mitosis. For example, mitotic phosphorylation of Histone H3 threonine‐3 (H3T3ph) by Haspin creates a binding site for the chromosomal passenger complex (CPC). However, how these histone modifications are spatiotemporally controlled during the cell cycle is unclear. Here we show that Plk1 binds to Haspin in a Cdk1‐phosphorylation‐dependent manner. Reducing Plk1 activity decreases the phosphorylation of Haspin and inhibits H3T3ph, particularly in prophase, suggesting that Plk1 is required for initial activation of Haspin in early mitosis. These studies demonstrate that Plk1 can positively regulate CPC recruitment in mitosis. |
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| Keywords: | cyclin‐dependent kinase haspin histone modification mitosis polo‐like kinase‐1 |
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