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

Markus Posch, Guennadi A. Khoudoli, Sam Swift, Emma M. King, Jennifer G. DeLuca, Jason R. Swedlow (Lead / Corresponding author)

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    Abstract

    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.

    Original languageEnglish
    Pages (from-to)61-74
    Number of pages14
    JournalJournal of Cell Biology
    Volume191
    Issue number1
    DOIs
    Publication statusPublished - 4 Oct 2010

    Keywords

    • HISTONE H3 PHOSPHORYLATION
    • STRUCTURED ILLUMINATION MICROSCOPY
    • LIFETIME IMAGING MICROSCOPY
    • PROTEIN PHOSPHATASE 1
    • CHROMOSOME SEGREGATION
    • ESSENTIAL ROLES
    • CELL-DIVISION
    • KINASE
    • SPINDLE
    • YEAST

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