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.

Interaction of cofactor Phactr1 with PP1 creates a composite substrate-binding surface that defines the sequence specificity of the Phactr1/PP1 holoenzyme.

Direct inhibition of pyridoxal phosphatase activity by 7,8-dihydroxyflavone indicates a pharmacological entry point into brain disorders associated with vitamin B6 deficiency.

PPM1H protein phosphatase dephosphorylates Rab proteins modulating LRRK2 signalling.

Conventional studies have focused on enzymatic residues directly involved in catalysis; dissecting a potential interaction network within which these ‘catalytic residues’ are embedded provides insights fundamental to enzyme function, evolution, and engineering.

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.

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.

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.

Two receptor tyrosine phosphatases having overlapping function for the determination of the final axon stabilizing layer is encoded for their cumulative cytoplasmic activity and ligand specificity in the visual system.

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.