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The C-terminal helix of BubR1 is essential for CENP-E-dependent chromosome alignment.

Authors
  • Legal, Thibault1
  • Hayward, Daniel2
  • Gluszek-Kustusz, Agata1
  • Blackburn, Elizabeth A1
  • Spanos, Christos1
  • Rappsilber, Juri1, 3
  • Gruneberg, Ulrike2
  • Welburn, Julie P I4
  • 1 Wellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, Scotland, UK.
  • 2 Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
  • 3 Chair of Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin 10623, Germany. , (Germany)
  • 4 Wellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, Scotland, UK [email protected]
Type
Published Article
Journal
Journal of Cell Science
Publisher
The Company of Biologists
Publication Date
Aug 25, 2020
Volume
133
Issue
16
Identifiers
DOI: 10.1242/jcs.246025
PMID: 32665320
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

During cell division, misaligned chromosomes are captured and aligned by motors before their segregation. The CENP-E motor is recruited to polar unattached kinetochores to facilitate chromosome alignment. The spindle checkpoint protein BubR1 (also known as BUB1B) has been reported as a CENP-E interacting partner, but the extent to which BubR1 contributes to CENP-E localization at kinetochores has remained controversial. Here we define the molecular determinants that specify the interaction between BubR1 and CENP-E. The basic C-terminal helix of BubR1 is necessary but not sufficient for CENP-E interaction, and a minimal key acidic patch on the kinetochore-targeting domain of CENP-E is also essential. We then demonstrate that BubR1 is required for the recruitment of CENP-E to kinetochores to facilitate chromosome alignment. This BubR1-CENP-E axis is critical for alignment of chromosomes that have failed to congress through other pathways and recapitulates the major known function of CENP-E. Overall, our studies define the molecular basis and the function for CENP-E recruitment to BubR1 at kinetochores during mammalian mitosis.This article has an associated First Person interview with the first author of the paper. © 2020. Published by The Company of Biologists Ltd.

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