Direct binding between BubR1 and B56-PP2A phosphatase complexes regulate mitotic progression.

@article{Kruse2013DirectBB,
  title={Direct binding between BubR1 and B56-PP2A phosphatase complexes regulate mitotic progression.},
  author={Thomas Kruse and Gang Zhang and Marie Sofie Yoo Larsen and Tiziana Lischetti and Werner W. Streicher and Tine Kragh Nielsen and Sara Petersen Bj\orn and Jakob Nilsson},
  journal={Journal of cell science},
  year={2013},
  volume={126 Pt 5},
  pages={1086-92}
}
BubR1 is a central component of the spindle assembly checkpoint that inhibits progression into anaphase in response to improper kinetochore-microtubule interactions. In addition, BubR1 also helps stabilize kinetochore-microtubule interactions by counteracting the Aurora B kinase but the mechanism behind this is not clear. Here we show that BubR1 directly binds to the B56 family of protein phosphatase 2A (PP2A) regulatory subunits through a conserved motif that is phosphorylated by cyclin… CONTINUE READING
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