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Plancke, C. N.

Publications and source records attributed to Plancke, C. N..

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↗

Genetically encoded reporters of actin filament organization in living cells and tissues

The cytoskeletal protein actin is crucial for cell shape and integrity throughout eukaryotes. Actin filaments perform essential biological functions, including muscle contraction, cell division and tissue morphogenesis. These diverse activities are achieved through the ability of actin filaments to be arranged into precise architectures. Much progress has been made in defining the proteome of the actin cytoskeleton, but a detailed appreciation of the dynamic organizational state of the actin filaments themselves has been hindered by available tools. Fluorescence polarization microscopy is uniquely placed for measuring actin filament organization by exploiting the sensitivity of polarized light excitation to the orientation of fluorophores attached to actin filaments. By engineering fusions of five widely used actin localization reporters to fluorescent proteins with constrained mobility, we have succeeded in developing genetically-encoded, green- and red-fluorescent-protein-based reporters for non-invasive, quantitative measurements of actin filament organization in living cells and tissues by fluorescence polarization microscopy.

cell biology↗