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The initiation of DNA damage checkpoint recovery involves ATM-mediated E3 ubiquitin ligase E6AP phosphorylation which disrupts E6AP-MASTL association and leads to MASTL protein accumulation and cell cycle resumption.

Chemical inhibition of Bub1 shows that the catalytic activity is not required for normal mitotic progression, but it makes chromosome segregation and cell proliferation more sensitive to the effects of the anti-cancer drug Paclitaxel.

A histone modification that alters the nucleosome structure occurs in mitosis and promotes chromosome packaging and the timely removal of condensin I and cohesion, to achieve chromosome segregation.

The mitotic exit network signals from spindle pole bodies to the nucleolus through the dynamic localization of its terminal kinase complex Dbf2-Mob1.

Cancer cells can grow in vitro and in vivo in the absence of maternal embryonic leucine zipper kinase (MELK).

It is shown that fission yeast cells sense their size by measuring their surface area through a membrane-associated sizer protein cdr2p.

The TRAIP ubiquitin ligase is required during mitosis to disassemble the replisome at sites of incomplete DNA replication, and activate the mitotic DNA repair pathway, thus preserving genome integrity.

Dynamic signaling protein clusters sample and map the cell surface to ensure that cells divide at the proper size.

The polo-like kinase (Plk1) phophorylates the C. elegans lamin LMN-1 to promote timely lamina disassembly, which is essential for the merging of the parental chromosomes at the beginning of life.