MASTL Facilitates Mitotic Progression

Cell cycle regulation of Greatwall kinase nuclear localization facilitates mitotic progression

Cell division requires the coordination of critical protein kinases and phosphatases. Greatwall (Gwl) kinase activity inactivates PP2A-B55 at mitotic entry to promote the phosphorylation of cyclin B-Cdk1 substrates, but how Gwl is regulated is poorly understood. We found that the subcellular localization of Gwl changed dramatically during the cell cycle in Drosophila. Gwl translocated from the ...

PP1 initiates the dephosphorylation of MASTL, triggering mitotic exit and bistability in human cells.

Entry into mitosis is driven by the phosphorylation of thousands of substrates, under the master control of Cdk1. During entry into mitosis, Cdk1, in collaboration with MASTL kinase, represses the activity of the major mitotic protein phosphatases, PP1 and PP2A, thereby ensuring mitotic substrates remain phosphorylated. For cells to complete and exit mitosis, these phosphorylation events must b...

NudC Deacetylation Regulates Mitotic Progression

Mitosis is largely driven by posttranslational modifications of proteins. Recent studies suggest that protein acetylation is prevalent in mitosis, but how protein acetylation/deacetylation regulates mitotic progression remains unclear. Nuclear distribution protein C (NudC), a conserved protein that regulates cell division, was previously shown to be acetylated. We found that NudC acetylation wa...

Bleach at the roots of mitotic progression

Bleach at the roots of mitotic progression Lim et al. show how hydrogen peroxide at the centrosome spurs cells to advance through mitosis. Cdk1 and regulatory proteins such as cyclin B1, Plk1, and Aurora A cooperate to initiate mitosis. To exit mitosis, cells destroy the regulatory proteins, an effect triggered by the APC/C when it is bound to its coactivator Cdh1. Cdk1 adds phosphates to Cdh1 ...

The chromosomal passenger complex during mitotic progression