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.

Inactivation of the master mitotic checkpoint regulator Mps1 by protein phosphatase 1 is required for timely segregation of the genetic material during cell division.

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.

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.

PP1-Bud14 is a novel Spindle Position Checkpoint component.

Molecular, cellular, and computational analyses reveal key insights into PP2A/B55α's mechanisms of substrate recruitment and active site engagement, and facilitate identification/validation of new substrates, a step towards understanding PP2A/B55α's role in multiple cellular processes.

Time-resolved phosphoproteomics and thermal proteome profiling reveal the Ca²⁺-responsive proteome of the model apicomplexan Taxoplasma gondii, identifying PP1 as a Ca²⁺-responsive enzyme that regulates Ca²⁺ uptake to promote parasite motility.

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.

Structural and biochemical data suggest a mechanism for the Synaptojanin1-catalysed reaction and the role of mutations in the onset of associated neurological diseases.

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