Concerted action of Aurora B, Polo and NHK-1 kinases in centromere-specific histone 2A phosphorylation.
The spatial and temporal control of histone modifications is crucial for precise regulation of chromatin structure and function. Here we report that phosphorylation of H2A at threonine 119 (T119) is enriched at centromere regions in Drosophila mitosis. We found that the Aurora B kinase complex is essential for this phosphorylation at centromeres, while Polo kinase is required to down-regulate H2A phosphorylation on chromosome arms in mitosis. Cyclin B degradation triggers loss of centromeric H2A phosphorylation at anaphase onset. Epistasis analysis indicated that Polo functions upstream of the H2A kinase NHK-1 but parallel to Aurora B. Therefore, multiple mitotic kinases work together to specify the spatial and temporal pattern of H2A T119 phosphorylation.
Brittle
Amy L
AL
The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, School of Biological Sciences, The University of Edinburgh, Edinburgh, UK.
Nanba
Yasuaki
Y
Ito
Takashi
T
Ohkura
Hiroyuki
H
D000818:Animals; D064127:Aurora Kinases; D002503:Centromere / Q000737:chemistry / Q000378:metabolism*; D004330:Drosophila / Q000166:cytology / Q000235:genetics / Q000502:physiology*; D029721:Drosophila Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D006657:Histones / Q000032:analysis / Q000378:metabolism*; D008938:Mitosis; D010766:Phosphorylation; D006656:Protamine Kinase / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*
D029721:Drosophila Proteins; D006657:Histones; C072004:polo protein, Drosophila; D064127:Aurora Kinases; C506651:Ball protein, Drosophila; D006656:Protamine Kinase; D017346:Protein Serine-Threonine Kinases