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Pinard, E.

Publications and source records attributed to Pinard, E..

2 recordsLinked to original sources

Kinetic Control of Out-Of-Equilibrium Dynamics in the RhoA Signaling Cascade Shapes Actomyosin Contractility

Cellular functions rely on the precise timing of signal transmission through sequential activation cascades, yet the origin and functional role of signaling delays remain poorly understood. Here, we dissect the temporal organization of the RhoA signaling cascade during pulsed actomyosin contractility in the early C. elegans embryo. We uncover a stereotypical delay between upstream RhoA/ROCK activation and downstream myosin II recruitment. Using TIRF single-molecule microscopy, we show that this delay arises from binding and unbinding kinetics of myosin rather than from slow biochemical reactions. A simple and versatile kinetic model parameterized by these measurements accurately predicts the temporal evolution of myosin accumulation and reveals active control of the dynamic range of the cascade. Perturbing actin and myosin turnover experimentally confirms these predictions, and numerical simulations show that the delay between actin and myosin plays a critical role in force deployment during pulsed contraction. Together, our results indicate that kinetic delays in signaling cascades are not simply tolerated during morphogenesis, but actively shape force deployment in the cell.

developmental biology↗

Structural insights into glycine reuptake inhibition

The human glycine transporter 1 (GlyT1) regulates glycine mediated neuronal excitation and inhibition through sodium- and chloride-dependent reuptake of the neurotransmitter1-3. Inhibition of glycine reuptake via GlyT1 prolongs neurotransmitter signaling and has long served as a key therapeutic development strategy for treatment of a broad range of central nervous system disorders including schizophrenia and cognitive impairments4. Using an inhibition state-selective sybody and serial synchrotron crystallography, we determined the structure of GlyT1 in complex with a benzoylpiperazine chemotype inhibitor at 3.4 [A] resolution. The inhibitor locks GlyT1 in an inward-open conformation and binds at the intracellular gate of the release pathway, overlapping with the glycine release site. The inhibitor likely reaches GlyT1 from the cytoplasmic leaflet of the plasma membrane. The study defines the mechanism of non-competitive inhibition and enables the rational design of new, clinically efficacious GlyT1 inhibitors.

neuroscience↗