Katharina Overlack, Ivana Primorac ... Andrea Musacchio
The mechanism behind the recruitment of the spindle assembly checkpoint protein BubR1 to the kinetochore illustrates how gene duplication and sub-functionalization can influence the functional complexity of a protein network.
The spindle assembly protein Bub3 recruits the checkpoint kinase Bub1 to kinetochores by binding to phosphorylated MELT repeats in the kinetochore subunit Knl1.
Chromosomal instability through spindle assembly checkpoint alleviation facilitates malignant transformation of hepatocytes and T-cells in vivo, resulting in cancers with recurrent karyotypes.
The spindle checkpoint kinase Mps1 sequentially phosphorylates multiple substrates to amplify checkpoint signals, making the checkpoint highly dependent on Mps1 function and directly responsive to kinetochore-microtubule attachment.
Inactivation of the master mitotic checkpoint regulator Mps1 by protein phosphatase 1 is required for timely segregation of the genetic material during cell division.