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Published online
doi:10.1083/jcb.200609153
The Journal of Cell Biology, Vol. 176, No. 7, 911-918
The Rockefeller University Press, 0021-9525 $30.00
© Yu et al.
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Article

The Aurora kinase Ipl1 maintains the centromeric localization of PP2A to protect cohesin during meiosis



Hong-Guo Yu1,2,3 and Douglas Koshland1,2

1 Howard Hughes Medical Institute and 2 Department of Embryology, Carnegie Institution, Baltimore, MD 21210
3 Department of Biological Science, Florida State University, Tallahassee, FL 32306

Correspondence to Hong-Guo Yu: hyu{at}bio.fsu.edu

Homologue segregation during the first meiotic division requires the proper spatial regulation of sister chromatid cohesion and its dissolution along chromosome arms, but its protection at centromeric regions. This protection requires the conserved MEI-S332/Sgo1 proteins that localize to centromeric regions and also recruit the PP2A phosphatase by binding its regulatory subunit, Rts1. Centromeric Rts1/PP2A then locally prevents cohesion dissolution possibly by dephosphorylating the protein complex cohesin. We show that Aurora B kinase in Saccharomyces cerevisiae (Ipl1) is also essential for the protection of meiotic centromeric cohesion. Coupled with a previous study in Drosophila melanogaster, this meiotic function of Aurora B kinase appears to be conserved among eukaryotes. Furthermore, we show that Sgo1 recruits Ipl1 to centromeric regions. In the absence of Ipl1, Rts1 can initially bind to centromeric regions but disappears from these regions after anaphase I onset. We suggest that centromeric Ipl1 ensures the continued centromeric presence of active Rts1/PP2A, which in turn locally protects cohesin and cohesion.

Abbreviations used in this paper: ChIP, chromatin immunoprecipitation; INCENP, inner centromere protein.


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