SGT1-HSP90 complex is required for CENP-A deposition at centromeres

Yohei Niikura, Risa Kitagawa, Hiroo Ogi, Katsumi Kitagawa

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

The centromere plays an essential role in accurate chromosome segregation, and defects in its function lead to aneuploidy and thus cancer. The centromere-specific histone H3 variant CENP-A is proposed to be the epigenetic mark of the centromere, as active centromeres require CENP-A–containing nucleosomes to direct the recruitment of multiple kinetochore proteins. CENP-A K124 ubiquitylation, mediated by CUL4A-RBX1-COPS8 E3 ligase activity, is required for CENP-A deposition at the centromere. However, the mechanism that controls the E3 ligase activity of the CUL4A-RBX1-COPS8 complex remains obscure. We have discovered that the SGT1-HSP90 complex is required for recognition of CENP-A by COPS8. Thus, the SGT1-HSP90 complex contributes to the E3 ligase activity of the CUL4A complex that is necessary for CENP-A ubiquitylation and CENP-A deposition at the centromere.

Original languageEnglish (US)
Pages (from-to)1683-1694
Number of pages12
JournalCell Cycle
Volume16
Issue number18
DOIs
StatePublished - Sep 17 2017

Keywords

  • CENP-A
  • CUL4 E3 ligase
  • HSP90
  • SGT1
  • SUGT1
  • cancer
  • cell cycle
  • centromere
  • epigenetic mark
  • kinetochore
  • mitosis
  • ubiquitylation

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

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