Letter abstract


Nature Cell Biology 12, 719 - 727 (2010)
Published online: 20 June 2010 | doi:10.1038/ncb2075

Human POGZ modulates dissociation of HP1α from mitotic chromosome arms through Aurora B activation

Ryu-Suke Nozawa1, Koji Nagao1,2, Hiro-Taka Masuda1, Osamu Iwasaki1,6, Toru Hirota3, Naohito Nozaki4, Hiroshi Kimura5 & Chikashi Obuse1

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Heterochromatin protein 1 (HP1) has an essential role in heterochromatin formation and mitotic progression through its interaction with various proteins. We have identified a unique HP1α-binding protein, POGZ (pogo transposable element-derived protein with zinc finger domain), using an advanced proteomics approach. Proteins generally interact with HP1 through a PxVxL (where x is any amino-acid residue) motif; however, POGZ was found to bind to HP1α through a zinc-finger-like motif. Binding by POGZ, mediated through its zinc-finger-like motif, competed with PxVxL proteins and destabilized the HP1α–chromatin interaction. Depletion experiments confirmed that the POGZ HP1-binding domain is essential for normal mitotic progression and dissociation of HP1α from mitotic chromosome arms. Furthermore, POGZ is required for the correct activation and dissociation of Aurora B kinase from chromosome arms during M phase. These results reveal POGZ as an essential protein that links HP1α dissociation with Aurora B kinase activation during mitosis.

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  1. Graduate School of Life Science, Hokkaido University, Sapporo 001-0021, Japan.
  2. Initial Research Project, Okinawa Institute of Science and Technology, Okinawa 904-2234, Japan.
  3. Cancer Institute of the Japanese Foundation for Cancer Research (JFCR), Tokyo 135-8550, Japan.
  4. Kanagawa Dental College, Yokosuka 238-8580, Japan.
  5. Graduate School of Frontier Bioscience, Osaka University, Suita 565-0871, Japan.
  6. Present address: The Wistar Institute, Philadelphia, PA 19104, USA.

Correspondence to: Chikashi Obuse1 e-mail: obuse@sci.hokudai.ac.jp



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