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

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.

journal_name

J Cell Sci

journal_title

Journal of cell science

authors

Legal T,Hayward D,Gluszek-Kustusz A,Blackburn EA,Spanos C,Rappsilber J,Gruneberg U,Welburn JPI

doi

10.1242/jcs.246025

subject

Has Abstract

pub_date

2020-08-25 00:00:00

issue

16

eissn

0021-9533

issn

1477-9137

pii

jcs.246025

journal_volume

133

pub_type

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