4.8 Article

Ki-67 is a PP1-interacting protein that organises the mitotic chromosome periphery

Journal

ELIFE
Volume 3, Issue -, Pages -

Publisher

ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.01641

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Funding

  1. Wellcome Trust [073915, 077248, 091020]
  2. Biotechnology and Biological Sciences Research Council [BB/K017632/1]
  3. Wellcome Trust (Centre Core Grant) [077707]
  4. Brunel BRIEF award [LBL301]
  5. Medical Research Council
  6. RIKEN Incentive Research Fund
  7. JSPS KAKENHI [24657124]
  8. RIKEN
  9. BBSRC [BB/K017632/1] Funding Source: UKRI
  10. MRC [MC_U137761446, MC_UU_12021/1] Funding Source: UKRI
  11. Biotechnology and Biological Sciences Research Council [BB/K017632/1] Funding Source: researchfish
  12. Medical Research Council [MC_U137761446, MC_UU_12021/1] Funding Source: researchfish
  13. Grants-in-Aid for Scientific Research [24657124] Funding Source: KAKEN

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When the nucleolus disassembles during open mitosis, many nucleolar proteins and RNAs associate with chromosomes, establishing a perichromosomal compartment coating the chromosome periphery. At present nothing is known about the function of this poorly characterised compartment. In this study, we report that the nucleolar protein Ki-67 is required for the assembly of the perichromosomal compartment in human cells. Ki-67 is a cell-cycle regulated protein phosphatase 1-binding protein that is involved in phospho-regulation of the nucleolar protein B23/nucleophosmin. Following siRNA depletion of Ki-67, NIFK, B23, nucleolin, and four novel chromosome periphery proteins all fail to associate with the periphery of human chromosomes. Correlative light and electron microscopy (CLEM) images suggest a near-complete loss of the entire perichromosomal compartment. Mitotic chromosome condensation and intrinsic structure appear normal in the absence of the perichromosomal compartment but significant differences in nucleolar reassembly and nuclear organisation are observed in post-mitotic cells.

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