Unfair competition, in which a phosphatase and a phosphoprotein inhibitor/substrate mutually sequester each other from competing substrates and enzymes, is a conserved mechanism for the control of PPP family phosphatases.
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.
The polarity protein crumbs controls apical secretion and the architecture of the apical domain by modulating PI(4,5)P2 levels and the organization of apical Rab6-, Rab11-, and Rab30-dependent trafficking.
Quantitative phosphoproteomics defines the substrates for Cyclin A/Cdk1 kinase during early mitosis and follow up studies validate that one identified substrate, MYPT1, influences the stability of k-MT attachments by regulating Plk1.
The axonal cytoskeletal contains an actomyosin-II network that controls circumferential axonal contraction and expansion with the potential of regulating fluctuations in diameter during action potential firing, trafficking, and degeneration.
Genetic mouse models identify a critical mechanism of myogenic vasoconstriction and reveal the in vivo function of myogenic autoregulation in protecting from organ overperfusion and in maintaining vascular resistance.