Mitotic phosphorylation of MPP8 by cyclin-dependent kinases regulates chromatin dissociation

Makoto Nishigaki, Yu Kawada, Toshinori Misaki, Kazuhiro Murata, Takahiro Goshima, Takahisa Hirokawa, Chisato Yamada, Midori Shimada, Makoto Nakanishi

研究成果: Article査読

6 被引用数 (Scopus)

抄録

Repressive epigenetic modifications, DNA methylation at CpG sites and histone H3 lysine 9 (H3K9) methylation, are enriched in heterochromatin, which undergoes drastic changes in structure during mitosis. MPP8 (M phase phosphoprotein 8) has been proposed to regulate positive association between these two repressive modifications, but actual involvement of this protein in changes in the heterochromatin structure during mitosis remains elusive. We demonstrate here that MPP8 predominantly localized to, but dissociated from, chromatin during interphase and early mitosis, respectively. Chromatin dissociation from MPP8 appeared to correlate with the phosphorylation status of MPP8. Experiments using inhibitors of various mitotic kinases demonstrated that the chromatin dissociation of MPP8 during metaphase to anaphase was specifically regulated by cyclin B1-Cdk1. Indeed, cyclin B1-Cdk1 effectively phosphorylated MPP8 in vitro and on STA mutant of MPP8 (all possible sites phosphorylated by Cdk were substituted by alanine) failed to dissociate from chromatin during early mitosis. Taken together, our results indicate that the chromatin association of MPP8 is regulated by Cdk-dependent phosphorylation.

本文言語English
ページ(範囲)654-659
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
432
4
DOI
出版ステータスPublished - 22-03-2013
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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