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.
Genetic and biochemical analysis of two enzymes reveals that inositol pyrophosphate signaling molecules allow plants to sense and regulate cellular phosphate levels, and to take up more phosphate when needed.
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.
The SHIP2 inositol phosphatase is an important upstream regulator of the Akt signaling pathway, which requires a catalytic core formed by the phosphatase domain tightly packed to a C2 domain for its function.
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.
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.
The sphingosine 1-phosphate receptor-1 (S1PR1) signals in heterogenous populations of mouse adventitial lymphatic (LEC) and arterial endothelial cells (aEC1, aEC2) to regulate chromatin and the transcriptome, thus affecting their phenotypes.