The kinase Mps1, long known to be the 'boss' in mitotic checkpoint signaling, phosphorylates multiple proteins in the checkpoint signaling cascade.

Tissue-resident macrophages sense environmental cues and regulate adaptive immunity via an immune checkpoint molecule CRIg.

Chromosomal instability through spindle assembly checkpoint alleviation facilitates malignant transformation of hepatocytes and T-cells in vivo, resulting in cancers with recurrent karyotypes.

The involvement of SETD2 in an important DNA repair pathway could explain the high frequency of SETD2 mutations in several cancers and may provide an alternative mechanism to evade the p53-mediated checkpoint.

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.

Daughter-cell-associated factors and centrosome-based regulation is important in mitotic exit and spindle position checkpoint control.

Inactivation of the master mitotic checkpoint regulator Mps1 by protein phosphatase 1 is required for timely segregation of the genetic material during cell division.

The spindle assembly protein Bub3 recruits the checkpoint kinase Bub1 to kinetochores by binding to phosphorylated MELT repeats in the kinetochore subunit Knl1.

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.