Two related DNA replication initiation proteins contribute to the decision of whether to enter a new round of the cell division cycle or enter into a period of proliferative quiescence.

The SCF-family of ubiquitin ligases regulates the key cancer proliferation node by controlling the degradation of RB-like tumor suppressor RBL2/p130.

DNA-PK and PTEN protect breast cancer cells from lethal replication stress induced by the WEE1 inhibitor AZD1775 and constitute new potential biomarkers for AZD1775 sensitivity.

The retinoblastoma tumor suppressor regulates cell cycle progression when it's in 14 mono-phosphorylated isoforms.

The decision to commit to cell division-the Start transition-in budding yeast is governed by time integration of G1 cyclin-CDK activity by the transcription factor Whi5.

Human cullin-RING ligases are buffered to a much greater extent than had been previously appreciated, and the roles of ubiquitin chain extension enzymes are far more nuanced at physiological concentrations.

The unique cell cycle variations of pluripotent stem cells ensures that the first step in DNA replication is particularly fast and this rapid rate, in turn, restrains early differentiation.

Cyclin-dependent kinase 5 regulates the circadian clock involving phosphorylation of the PER2 protein.

A mitochondria-based 'priming' of stemness happens by fine-tuned repression of the level or activity of the master regulator of mitochondrial fission, Drp1, which supports carcinogen-induced transformation in a keratinocyte model.

Application of a live-cell reporter for CDK4/6 activity reveals rapid activity changes and reversibility in the cell-cycle entry signaling program.