Structures of active and inactive conformations of a PP2C family phosphatase reveal a conserved switch that controls enzymatic activity and point to an unexpected relationship between phosphatases and proteasomal proteases.
A combination of transcriptomics, proteomics and modelling identifies a network of interacting protein phosphatases that act as a biological switch to move cells from the stem cell compartment to the differentiated compartment in cultured human epidermis.
Protein phosphatase 1 activity promotes cohesive collective cell migration by restricting actomyosin contractility to the periphery of the collective and maintaining proper cadherin–catenin complex protein levels at cell–cell junctions.
Mitogen-activated protein kinase phosphatase 1 (DUSP1) deficiency causes early redox imbalance and increased inflammatory response in the cochlea, leading to cell loss and progressive neurosensory hearing loss.
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.
Microtubule binding by the Spindle and Kinetochore Associated (Ska) complex concentrates protein phosphatase 1 at metaphase kinetochores to overcome the spindle checkpoint thus driving anaphase onset and mitotic exit.