The CDC25 family protein phosphatase Mih1 promotes downregulation of cell surface proteins in budding yeast by dephosphorylating a subunit of the retromer complex, which mediates plasma membrane recycling.

Degradation of a mitotic inducer coordinates the transition of two successive cell cycle arrests during the infective process of a plant pathogenic fungus.

Time-course phosphoproteomics reveals that selective dephosphorylation is critical for directing the MI/MII transition and that, through its inherent phospho-threonine preference, PP2A-B55 imposes specific phosphoregulated behaviors that distinguish the two meiotic divisions.

Tissue damage induces a reversible cell cycle arrest in G2, which promotes survival and mitogenic signals to facilitate tissue regeneration but drives senescence-like phenotypes under chronic stress conditions.

DNA concentration, cyclin levels, phosphatase activity, and CDK phosphorylation combine to directly link cell size to cell division.

Unfair competition, in which a phosphatase and a phosphoprotein inhibitor/substrate mutually sequester each other from competing substrates and enzymes, is a conserved mechanism for the control of PPP family phosphatases.

Inhibition of phosphatases by kinases develops Whi5 phosphorylation and cell cycle function in low cyclin-dependent kinase activity.

PP1-Bud14 is a novel Spindle Position Checkpoint component.

The cell cycle phosphatase CDC25B controls cell cycle progression and neurogenesis through independent pathways.

The Ras activator RasGRP1 that impacts Ras signals in immune cells, leukemias, and colorectal cancer, switches to an active conformation aided by a pH-sensitive histidine residue in a central location of the RasGRP1 molecule.