Linking kinetochore attachment to checkpoint control: the role of Aurora B in BubR1 acetylation.

ABSTRACT: We report that Aurora B kinase-mediated phosphorylation is essential for BubR1 acetylation at lysine 250 (K250), a modification required to preserve the mitotic checkpoint complex (MCC) and ensure accurate chromosome segregation. This Aurora B-BubR1 acetylation axis provides a mechanistic explanation for how kinetochore-microtubule attachment status is transduced to spindle assembly checkpoint (SAC) activity. Aurora B phosphorylates BubR1 at Serine 39 (and Ser16) in response to unattachment, and this phosphorylation is indispensable for subsequent K250 acetylation. Using a monoclonal anti-AcK250 antibody in structured illumination microscopy, we demonstrate that BubR1 acetylation sustains the fibrous corona, as shown by the crescent-shaped expansion of ZW10 and MAD2 surrounding kinetochore

SUBMITTER: Choi SY 

PROVIDER: S-EPMC12802887 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature