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Mps1 promotes rapid centromere accumulation of Aurora B
Author(s) -
van der Waal Maike S,
Saurin Adrian T,
Vromans Martijn J M,
Vleugel Mathijs,
Wurzenberger Claudia,
Gerlich Daniel W,
Medema René H,
Kops Geert J P L,
Lens Susanne M A
Publication year - 2012
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2012.93
Subject(s) - centromere , aurora b kinase , kinetochore , microbiology and biotechnology , mitosis , bub1 , chromosome segregation , biology , spindle checkpoint , histone h3 , histone , genetics , chromosome , dna , gene
Aurora B localization to mitotic centromeres, which is required for proper chromosome alignment during mitosis, relies on Haspin‐dependent histone H3 phosphorylation and on Bub1‐dependent histone H2A phosphorylation—which interacts with Borealin through a Shugoshin (Sgo) intermediate. We demonstrate that Mps1 stimulates the latter recruitment axis. Mps1 activity enhances H2A‐T120ph and is critical for Sgo1 recruitment to centromeres, thereby promoting Aurora B centromere recruitment in early mitosis. Importantly, chromosome biorientation defects caused by Mps1 inhibition are improved by restoring Aurora B centromere recruitment. As Mps1 kinetochore localization reciprocally depends on Aurora B, we propose that this Aurora B‐Mps1 recruitment circuitry cooperates with the Aurora B‐Haspin feedback loop to ensure rapid centromere accumulation of Aurora B at the onset of mitosis.