Sds22 defines protein phosphatase 1 location and function at kinetochores and subsequent activity of aurora B in mitosis

DeLuca, Jennifer G.

Khoudoli, Guennadi A.

King, Emma M.

Posch, Markus

Swedlow, Jason R.

Swift, Sam

English

PubMed

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 inter-actions. 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.</p

Discovery Research Portal

Sds22 regulates aurora B activity and microtubule-kinetochore interactions at mitosis

Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and CenpE to kinetochores.

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S. pombe gene sds22+ essential for a midmitotic transition encodes a leucinerich repeat protein that posi tively modulates protein phosphatase1.

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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.</jats:p

Markus Posch

Guennadi A. Khoudoli

Sam Swift

Emma M. King

Jennifer G. DeLuca

Jason R. Swedlow

Crossref

The Journal of Cell Biology

Sds22 regulates aurora B activity and microtubule–kinetochore interactions at mitosis

http://discovery.dundee.ac.uk/portal/files/852006/Posch_2010.pdf

Sds22 regulates aurora B activity and microtubule-kinetochore interactions at mitosis

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