Polo-like kinase-1 triggers histone phosphorylation by Haspin in mitosis.
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.
Mesh Terms:
Amino Acid Sequence, Cell Cycle Proteins, HeLa Cells, Histones, Humans, Intracellular Signaling Peptides and Proteins, Mitosis, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein Processing, Post-Translational, Protein Serine-Threonine Kinases, Proto-Oncogene Proteins
Amino Acid Sequence, Cell Cycle Proteins, HeLa Cells, Histones, Humans, Intracellular Signaling Peptides and Proteins, Mitosis, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein Processing, Post-Translational, Protein Serine-Threonine Kinases, Proto-Oncogene Proteins
EMBO Rep
Date: Mar. 01, 2014
PubMed ID: 24413556
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