Asymmetric division is crucial for embryonic development and stem cell lineages. In the one-cellC. elegansembryo, a contractile cortical actomyosin network contributes to anterior-posterior (A-P) polarity and asymmetric division by segregating PAR proteins to discrete cortical domains. Here, we discovered that the plasma membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2) forms dynamic structures inC. eleganszygotes, distributing in a polarized and PAR-dependent manner along the A-P

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... . PIP2cortical structures overlap with F-actin and coincide with the actin regulators RHO-1, CDC-42 and ECT-2. Particle image velocimetry analysis revealed that PIP2and F-actin cortical movements are coupled, with PIP2structures moving slightly ahead. Importantly, we established that PIP2cortical structures form in an actin-dependent manner and, conversely, that decreasing or increasing the level of PIP2results in severe F-actin disorganization, revealing the interdependence between these components. Furthermore, we uncovered that PIP2regulates the sizing of PAR cortical domains. Overall, our work establishes for the first time that a lipid membrane component, PIP2, is a critical modulator of actin organization and cell polarity inC. elegansembryos.