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Polo‐like kinase‐1 triggers histone phosphorylation by Haspin in mitosis
Author(s) -
Zhou Linli,
Tian Xiaoying,
Zhu Cailei,
Wang Fangwei,
Higgins Jonathan MG
Publication year - 2014
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1002/embr.201338080
Subject(s) - polo like kinase , mitosis , phosphorylation , microbiology and biotechnology , histone , kinase , histone h3 , biology , chemistry , genetics , cell cycle , gene
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.