Proteasome activity is required for centromere separation independently of securin degradation in human cells.

Juan F. Giménez-Abián, Laura A. Díaz-Martínez, Karin G. Wirth, Consuelo De la Torre, Duncan J. Clarke

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

Loss of centromere cohesion during anaphase in human cells is regulated by the spindle assembly checkpoint and is thought to depend on a ubiquitin ligase, the Anaphase Promoting Complex/Cyclosome (APC). APC-Cdc20 adds ubiquitin chains to securin inducing its destruction by the proteasome and these events correlate with the loss of sister chromatid cohesion and the onset of anaphase. But whether securin destruction is necessary and sufficient for anaphase initiation is not clear. Therefore, we asked if proteasome activity is needed for anaphase onset in human cells that lack securin. We find that even in the absence of securin, a metaphase block with cohered sister centromeres can be enforced in the absence of proteasome activity. Therefore, other targets of the proteasome must be degraded to allow anaphase onset.

Original languageEnglish (US)
Pages (from-to)1558-1560
Number of pages3
JournalCell Cycle
Volume4
Issue number11
DOIs
StatePublished - Nov 2005

Keywords

  • Anaphase promoting complex
  • Centromere cohesion
  • Cyclosome
  • Pds1
  • Proteasome
  • Securin
  • Separase
  • VELCADE®

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