We have studied Sds22, a conserved regulator of protein phosphatase 1 (PP1) activity, and determined its role in modulating the activity of aurora B kinase and kinetochore-microtubule interactions. Sds22 is required for proper progression through mitosis and localization of PP1 to mitotic kinetochores. Depletion of Sds22 increases aurora B T-loop phosphorylation and the rate of recovery from monastrol arrest. Phospho-aurora B accumulates at kinetochores in Sds22-depleted cells juxtaposed to critical kinetochore substrates. Sds22 modulates sister kinetochore distance and the interaction between Hec1 and the microtubule lattice and, thus, the activation of the spindle assembly checkpoint. These results demonstrate that Sds22 specifically defines PP1 function and localization in mitosis. Sds22 regulates PP1 targeting to the kinetochore, accumulation of phospho-aurora B, and force generation at the kinetochore-microtubule interface.
详细资料
文献种类: Journal Article
期刊名称: The Journal of Cell Biology
期刊缩写: J Cell Biol
期卷页: 2010年第191卷第1期 61-74页
地址: Wellcome Trust Centre for Gene Regulation and Expression and 2 Light Microscopy Facility, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK