4.8 Article

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

Journal

NATURE CELL BIOLOGY
Volume 12, Issue 7, Pages 719-U212

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/ncb2075

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Funding

  1. JSPS (Japan Society for the Promotion of Science)
  2. MEXT (Ministry of Education, Culture, Sports, Science and Technology) of Japan
  3. Inamori
  4. Matrix Science K.K. Foundations
  5. Uehara Memorial
  6. Naito
  7. Mochida Memorial
  8. Grants-in-Aid for Scientific Research [20114001, 21570196, 20114006] Funding Source: KAKEN

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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 HP1 alpha-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 HP1 alpha through a zinc-finger-like motif. Binding by POGZ, mediated through its zinc-finger-like motif, competed with PxVxL proteins and destabilized the HP1 alpha-chromatin interaction. Depletion experiments confirmed that the POGZ HP1-binding domain is essential for normal mitotic progression and dissociation of HP1 alpha 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 HP1 alpha dissociation with Aurora B kinase activation during mitosis.

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