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.
A complex interplay between MAST3 and PKA protein kinases and the regulatory protein ARPP-16 allows cAMP to control the activity of protein phosphatase 2A.
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.
Inactivation of the master mitotic checkpoint regulator Mps1 by protein phosphatase 1 is required for timely segregation of the genetic material during cell division.
Interaction of cofactor Phactr1 with PP1 creates a composite substrate-binding surface that defines the sequence specificity of the Phactr1/PP1 holoenzyme.
