2018
DOI: 10.1111/gtc.12630
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Defects in centromeric/pericentromeric histone H2A T120 phosphorylation by hBUB1 cause chromosome missegregation producing multinucleated cells

Abstract: Histone H2A phosphorylation plays a role both in chromatin condensation during mitosis and in transcriptional activation during the G1/S transition. Bub1 and NHK1/VRK1 have been identified as histone H2A kinases. However, little is known about the importance of histone H2A phosphorylation in chromosome segregation. Here, we expressed recombinant hBUB1 and confirmed that it phosphorylates histone H2A T120 in the in vitro-assembled nucleosome. Knockdown (KD) of BUB1 decreases bulk H2A T120 phosphorylation in HeL… Show more

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Cited by 10 publications
(3 citation statements)
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“…In yeast, the corresponding S121 is phosphorylated by Bub1 to recruit shugoshin, an important step for centromere function in chromosome segregation [58][59][60]. This serine is replaced by threonine (T120) in human H2A and H2A.X, and its phosphorylation is associated with transcriptional activation and mitotic chromosome segregation [61][62][63]. Consistent with these data, we detected only a few events of S129 phosphorylation in H2A.W in samples originating from leaves or seedlings that contain low amounts of dividing cells.…”
Section: Discussionsupporting
confidence: 85%
“…In yeast, the corresponding S121 is phosphorylated by Bub1 to recruit shugoshin, an important step for centromere function in chromosome segregation [58][59][60]. This serine is replaced by threonine (T120) in human H2A and H2A.X, and its phosphorylation is associated with transcriptional activation and mitotic chromosome segregation [61][62][63]. Consistent with these data, we detected only a few events of S129 phosphorylation in H2A.W in samples originating from leaves or seedlings that contain low amounts of dividing cells.…”
Section: Discussionsupporting
confidence: 85%
“…Moreover, neither mutation nor depletion of NHK-1 prevents mitotic H2AT119ph in flies or Drosophila S2 cells 86 , 88 . Instead, the kinetochore-binding kinase Bub1 is clearly vital for H2AT120ph in budding and fission yeast, mice, and human cells 18 , 89 , 90 . Together, there is little evidence to support a significant role for VRK1 in direct phosphorylation of H3T3ph or other histone residues in mitosis.…”
Section: Discussionmentioning
confidence: 99%
“…Moreover, neither mutation nor depletion of NHK-1 prevents mitotic H2AT119ph in flies or Drosophila S2 cells (70,74). Instead, the kinetochore-binding kinase Bub1 is clearly vital for H2AT120ph in budding and fission yeast, mice, and human cells (75-77). Together, there is little evidence to support a significant role for VRK1 in direct phosphorylation of H3T3ph or other histone residues in mitosis.…”
Section: Discussionmentioning
confidence: 99%